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Database: UniProt
Entry: B9WJL5_CANDC
LinkDB: B9WJL5_CANDC
Original site: B9WJL5_CANDC 
ID   B9WJL5_CANDC            Unreviewed;       268 AA.
AC   B9WJL5;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
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   OrderedLocusNames=Cd36_70100 {ECO:0000313|CGD:CAL0000168687};
GN   ORFNames=CD36_70100 {ECO:0000313|EMBL:CAX40562.1};
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX40562.1, ECO:0000313|Proteomes:UP000002605};
RN   [1] {ECO:0000313|EMBL:CAX40562.1, ECO:0000313|Proteomes:UP000002605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC   {ECO:0000313|Proteomes:UP000002605};
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
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; FM992694; CAX40562.1; -; Genomic_DNA.
DR   RefSeq; XP_002421230.1; XM_002421185.1.
DR   AlphaFoldDB; B9WJL5; -.
DR   GeneID; 8049123; -.
DR   KEGG; cdu:CD36_70100; -.
DR   CGD; CAL0000168687; Cd36_70100.
DR   VEuPathDB; FungiDB:CD36_70100; -.
DR   eggNOG; KOG2721; Eukaryota.
DR   HOGENOM; CLU_044271_1_0_1; -.
DR   OrthoDB; 239198at2759; -.
DR   Proteomes; UP000002605; Chromosome 7.
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR028980};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW   ECO:0000256|PIRNR:PIRNR028980}.
FT   DOMAIN          6..137
FT                   /note="tRNAHis guanylyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF04446"
FT   DOMAIN          140..255
FT                   /note="Thg1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14413"
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   268 AA;  32386 MW;  5E59EE6276D2EBB4 CRC64;
     MANSKYEYVK LFEKENYLLP DTYIVIRVDG KGFHKFSQFY QFEKPNDLKA LQVMNSAAEK
     IMSKYSDVML AYGDSDEYSF LLRKNCQLYE RREMKLTTLF ASLMSTYYMY FWQQHFPDKP
     LDIDHLPNFD ARAVLYPDFK HIRNYFSWRQ VDCHINNLYN TTFWNLVLKL KMTPQEAEQR
     LMGTVASDKN EILFKECGIN YNNELEMFKK GTIIVREFEN YEIEDETGLS KRQAQRLEKK
     RKKADLKTYH VDIINDNSWW DNRPWLRD
//
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