ID A0A0L1I3M5_PLAFA Unreviewed; 297 AA.
AC A0A0L1I3M5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 08-NOV-2023, entry version 27.
DE RecName: Full=tRNA(His) guanylyltransferase {ECO:0000256|ARBA:ARBA00012511, 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|PIRNR:PIRNR028980};
GN ORFNames=PFMG_00455 {ECO:0000313|EMBL:KNG74229.1};
OS Plasmodium falciparum IGH-CR14.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=580059 {ECO:0000313|EMBL:KNG74229.1, ECO:0000313|Proteomes:UP000054562};
RN [1] {ECO:0000313|Proteomes:UP000054562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGH-CR14 {ECO:0000313|Proteomes:UP000054562};
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "Annotation of Plasmodium falciparum IGH-CR14.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGH-CR14 {ECO:0000313|Proteomes:UP000054562};
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Godfrey P., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Wirth D.F., Nusbaum C., Birren B.;
RT "The genome sequence of Plasmodium falciparum IGH-CR14.";
RL Submitted (JUL-2015) 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. {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; GG664976; KNG74229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L1I3M5; -.
DR EnsemblProtists; KNG74229; KNG74229; PFMG_00455.
DR Proteomes; UP000054562; 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:UP000054562};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR028980};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR028980}.
FT DOMAIN 7..134
FT /note="tRNAHis guanylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF04446"
FT DOMAIN 137..239
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 297 AA; 35964 MW; A4EA513827F029F5 CRC64;
MANSKFSYVK LFEEERKILL NCYFIVRIDG CDFKHFVKAH NYNKPNDIKG LNLMNECALD
ILKKFDDIDL CYGHSDEYSF LFNKSTKLWN RRYDKILTNV VSYFTSCFLY KWKNYFQKEM
LYAPSFDARI VVYPNEKEIK DYFSWRQVDC HINTQYNECF WNLIRQANYT NDEAHKFLLT
TQTKDKNELL FSRFNINYNN LPEIFRRGTI IIRNKTFQKK NEALGTIYNN DTANNIDDNN
NNNNNNTFND NNDIENFEKL KKECLPKFII SHENLVSEKF WDKYDYIFKK KKDLEKK
//