ID A0A509AJC3_PLABA Unreviewed; 335 AA.
AC A0A509AJC3;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=PBANKA_0620500 {ECO:0000313|EMBL:VUC54880.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000313|EMBL:VUC54880.1, ECO:0000313|Proteomes:UP000074855};
RN [1] {ECO:0000313|EMBL:VUC54880.1, ECO:0000313|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ANKA {ECO:0000313|EMBL:VUC54880.1,
RC ECO:0000313|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/preaccept-1233682211145405;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
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; LK023121; VUC54880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A509AJC3; -.
DR STRING; 5823.A0A509AJC3; -.
DR VEuPathDB; PlasmoDB:PBANKA_0620500; -.
DR InParanoid; A0A509AJC3; -.
DR OMA; WKQHTEI; -.
DR OrthoDB; 239198at2759; -.
DR Proteomes; UP000074855; Chromosome 6.
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:UP000074855};
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..135
FT /note="tRNAHis guanylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF04446"
FT DOMAIN 139..247
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 335 AA; 40432 MW; 6805D878009609BF CRC64;
MANSKFAYVK LFEEEKKILL NCYFVVRIDG SDFKKFIKQH EYIKPNDLRG LNLMNECAIN
VLKNYDEIDL CYGHSDEFSF LFRKSTKLWN RRHDKILTNV VSYFTSSFTF NWKKYFPNKE
LIYLPSFDAR IIVYPTESEI KDYFSWRQAD CHINTQYNEC FWNLVLKSNY THEEAYKFLL
ATQTKDKNEL LFTRFDINYN NIPEIFRRGT IIIRNKNYKK NTTQHIQNND KHIDYMQGEQ
TKEEWKKQIN PHIYKENTDT DLCDISNVET NNNSNNSNSN NFDPNILKPF QNDQSNTLDK
FIITHENLIS ETFWNKYDFV FKKKKELKCI KYPHS
//