THG2_ARATH
ID THG2_ARATH Reviewed; 537 AA.
AC F4ISV6; F4ISV7; F4ISV8; Q6IDC3; Q9ZV60; Q9ZV61;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=tRNA(His) guanylyltransferase 2;
DE EC=2.7.7.79 {ECO:0000269|PubMed:20660484};
GN Name=THG2; OrderedLocusNames=At2g32320; ORFNames=T32F6.16;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-189.
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=20660484; DOI=10.1093/nar/gkq646;
RA Placido A., Sieber F., Gobert A., Gallerani R., Giege P.,
RA Marechal-Drouard L.;
RT "Plant mitochondria use two pathways for the biogenesis of tRNAHis.";
RL Nucleic Acids Res. 38:7711-7717(2010).
CC -!- FUNCTION: Adds a GMP to the 5'-end of tRNA(His) after transcription and
CC RNase P cleavage. {ECO:0000269|PubMed:20660484}.
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:0000269|PubMed:20660484};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:20660484}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=F4ISV6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4ISV6-2; Sequence=VSP_044437;
CC Name=3;
CC IsoId=F4ISV6-3; Sequence=VSP_044436;
CC -!- SIMILARITY: Belongs to the tRNA(His) guanylyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC69945.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC69946.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAT41733.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAU94397.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC005700; AAC69945.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC005700; AAC69946.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08668.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08669.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08670.1; -; Genomic_DNA.
DR EMBL; BT014750; AAT41733.1; ALT_FRAME; mRNA.
DR EMBL; BT015834; AAU94397.1; ALT_FRAME; mRNA.
DR PIR; F84731; F84731.
DR PIR; G84731; G84731.
DR RefSeq; NP_001154544.1; NM_001161072.1. [F4ISV6-1]
DR RefSeq; NP_001154545.1; NM_001161073.1. [F4ISV6-2]
DR RefSeq; NP_180791.3; NM_128791.4. [F4ISV6-3]
DR AlphaFoldDB; F4ISV6; -.
DR SMR; F4ISV6; -.
DR STRING; 3702.AT2G32320.2; -.
DR iPTMnet; F4ISV6; -.
DR PaxDb; F4ISV6; -.
DR PRIDE; F4ISV6; -.
DR ProteomicsDB; 234216; -. [F4ISV6-1]
DR EnsemblPlants; AT2G32320.1; AT2G32320.1; AT2G32320. [F4ISV6-3]
DR EnsemblPlants; AT2G32320.2; AT2G32320.2; AT2G32320. [F4ISV6-1]
DR EnsemblPlants; AT2G32320.3; AT2G32320.3; AT2G32320. [F4ISV6-2]
DR GeneID; 817793; -.
DR Gramene; AT2G32320.1; AT2G32320.1; AT2G32320. [F4ISV6-3]
DR Gramene; AT2G32320.2; AT2G32320.2; AT2G32320. [F4ISV6-1]
DR Gramene; AT2G32320.3; AT2G32320.3; AT2G32320. [F4ISV6-2]
DR KEGG; ath:AT2G32320; -.
DR Araport; AT2G32320; -.
DR TAIR; locus:2062611; AT2G32320.
DR eggNOG; KOG2721; Eukaryota.
DR HOGENOM; CLU_044271_4_0_1; -.
DR InParanoid; F4ISV6; -.
DR OMA; SCISCFT; -.
DR OrthoDB; 425615at2759; -.
DR PRO; PR:F4ISV6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4ISV6; baseline and differential.
DR Genevisible; F4ISV6; AT.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008193; F:tRNA guanylyltransferase activity; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; TAS:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR Gene3D; 3.30.70.3000; -; 2.
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; PTHR12729; 1.
DR Pfam; PF04446; Thg1; 2.
DR Pfam; PF14413; Thg1C; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; GTP-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..537
FT /note="tRNA(His) guanylyltransferase 2"
FT /id="PRO_0000420272"
FT BINDING 307..312
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 353..354
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT VAR_SEQ 216..227
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_044436"
FT VAR_SEQ 216..226
FT /note="VIFSIISFFYF -> KSKSFQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044437"
SQ SEQUENCE 537 AA; 62676 MW; 8CFA66CD0FAFDCE4 CRC64;
MANSKYEYVK SFEVEDEVMF PNLIIIRIDG RDFSRFSQVH KFEKPNDETS LNLMNSCASS
VLVEYPDIVF AYGYSDEYSF VFKKASRFYQ RRASKILSLV ASFFAAVYVT KWKEFFPHTK
LEYAPSFASK VVSCASVEVL QAYLAWRQHD CHISNQYDTC LWMLVKSGKT LSETQEILKD
TQKQQRNELL FQQFGINYKM LPVLFRQGSC LFKTKVIFSI ISFFYFLLEE TVKHDENGKP
VKRLRRRETL VHSENVAGRS FWNEHSSLHK DLGHFAKDIG KIEPDYVKSF QFESRLLPLT
WVVVRIDGCH FHRFSEVHEF EKPNDEQALK LMNSCAVAVL EEFQDIAFAY GVSDEFSFVL
KNKSELYKRQ SSKIISAVVS FFTSTYMMRW GDFFPHKKLK YPPSFDGRAV CYPTSDILLD
YLAWRQVDCH INNQYNTCFW MLVKSGKSKI QAQDYLKGTQ TREKNELLSQ QFGIEYNSLP
VIFRMGSSVF RLKTQEGVTE ENGEVSGKQV EAEVGVDYSN IIDQCFWQQH PHILSFS
