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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
 
 
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