THG1_ARATH
ID THG1_ARATH Reviewed; 567 AA.
AC F4IRQ5; Q9SIQ0;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=tRNA(His) guanylyltransferase 1;
DE EC=2.7.7.79 {ECO:0000269|PubMed:20660484};
GN Name=THG1; OrderedLocusNames=At2g31580; ORFNames=T9H9.10;
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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-397 AND LYS-403, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
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 -!- SIMILARITY: Belongs to the tRNA(His) guanylyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD24854.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007071; AAD24854.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08563.1; -; Genomic_DNA.
DR PIR; E84722; E84722.
DR RefSeq; NP_565727.2; NM_128715.3.
DR AlphaFoldDB; F4IRQ5; -.
DR SMR; F4IRQ5; -.
DR STRING; 3702.AT2G31580.1; -.
DR iPTMnet; F4IRQ5; -.
DR PaxDb; F4IRQ5; -.
DR PRIDE; F4IRQ5; -.
DR EnsemblPlants; AT2G31580.1; AT2G31580.1; AT2G31580.
DR GeneID; 817716; -.
DR Gramene; AT2G31580.1; AT2G31580.1; AT2G31580.
DR KEGG; ath:AT2G31580; -.
DR Araport; AT2G31580; -.
DR TAIR; locus:2065934; AT2G31580.
DR eggNOG; KOG2721; Eukaryota.
DR HOGENOM; CLU_044271_4_0_1; -.
DR InParanoid; F4IRQ5; -.
DR OrthoDB; 425615at2759; -.
DR PRO; PR:F4IRQ5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IRQ5; baseline and differential.
DR Genevisible; F4IRQ5; 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:0006974; P:cellular response to DNA damage stimulus; IMP:TAIR.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:TAIR.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:TAIR.
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 GTP-binding; Isopeptide bond; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase;
KW tRNA processing; Ubl conjugation.
FT CHAIN 1..567
FT /note="tRNA(His) guanylyltransferase 1"
FT /id="PRO_0000420271"
FT BINDING 342..347
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 388..389
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CROSSLNK 397
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT CROSSLNK 403
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
SQ SEQUENCE 567 AA; 66218 MW; 805BD3011BC75F2A CRC64;
MINSVGVVRK EAENCNCLQV FFVSGSFKVD SVEAKKKEEN FRETLRDMAN SKYEYVKSFE
LEDEVMLPNL MVVRIDGRDF SRFSQVHEFE KPNDETALNL MNSCSAAVLE EFPDIIFAYG
YSDEYSFVFK KTSRFYQRRA SKILSLVASF FAAVYVTKWK EFFPQRKLLY APSFSSKVVS
CASAEVLQAY LAWRQQDCHA NNQYDTCFWM LVKSGKSVSE TQEILKDTQK QQKNELLFQK
FGINYKTLPE LFRQGSCLFK KKVEETVKHD ENGNPVKRLR RKAVFVHSEN IAGRSFWNEQ
PSLYNDLGHF TKDIGKIEPD FIRSFQFENK LLPLTWVVVR IDGCHFHRFS DVHEFEKPND
EQALKLMNSC AVAVLEEFED IHFAYGVSDE YSFVLKKESE LYKRQSSKII SAVASFFTST
YVLQWGEFFP HKELKYPPSF DGRAVCYPTY NILLDYLAWR QVDCHINNQY NTCFWMLVKS
GKNKTQSQDY LKGTQTREKN ELLSRQFGIE YNSLPVIFRM GSSVFRLKEA ENGVVSGKKL
EGEVVVDHCN IIERCFWEEH LHILSYS