ID A0A074X122_9PEZI Unreviewed; 293 AA.
AC A0A074X122;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 08-NOV-2023, entry version 34.
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=M436DRAFT_70174 {ECO:0000313|EMBL:KEQ75737.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ75737.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ75737.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ75737.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(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; KL584704; KEQ75737.1; -; Genomic_DNA.
DR RefSeq; XP_013430358.1; XM_013574904.1.
DR AlphaFoldDB; A0A074X122; -.
DR STRING; 1043004.A0A074X122; -.
DR GeneID; 25414729; -.
DR HOGENOM; CLU_044271_1_0_1; -.
DR OrthoDB; 239198at2759; -.
DR Proteomes; UP000027730; 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:UP000027730};
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 140..281
FT /note="Thg1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14413"
FT REGION 225..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 34567 MW; 6595D6A7F80199DF CRC64;
MANSEFEYVR KFEDWDALAP SNWIVVRIDG RGFSKFSKRQ NFSKPNDRRA IDLMNAAAVE
VVKQFTDIVV AYGQSDEYSF VLHEDCQLFE RRAAKLATSI STAFSVEYCM QWDKYFPGQI
LERPFPTFDG RCVLYPKKKI LRDYLSWRQA DCHVNNLYNT TFWNMVKGNP VTDTPAMTPT
EAELALKGTF SKDKHEILFQ KFKLNYDKED EIWKKGSVVY RKFEDKQSVK EPTSENQPPQ
SRNERGTEQG KKKPLSRTQM EKERKRKQKA RVVVEHIDII KDNFWQENPW ILE
//
