THG1_YEAST
ID THG1_YEAST Reviewed; 237 AA.
AC P53215; D6VUF8; Q45U59;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=tRNA(His) guanylyltransferase;
DE EC=2.7.7.79 {ECO:0000269|PubMed:14633974};
DE AltName: Full=tRNA-histidine guanylyltransferase;
GN Name=THG1; OrderedLocusNames=YGR024C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14633974; DOI=10.1101/gad.1148603;
RA Gu W., Jackman J.E., Lohan A.J., Gray M.W., Phizicky E.M.;
RT "tRNAHis maturation: an essential yeast protein catalyzes addition of a
RT guanine nucleotide to the 5' end of tRNAHis.";
RL Genes Dev. 17:2889-2901(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Adds a GMP to the 5'-end of tRNA(His) after transcription and
CC RNase P cleavage. {ECO:0000269|PubMed:14633974}.
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:14633974};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC P53215; P53215: THG1; NbExp=3; IntAct=EBI-23112, EBI-23112;
CC -!- MISCELLANEOUS: Present with 1170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the tRNA(His) guanylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; DQ115389; AAZ22487.1; -; Genomic_DNA.
DR EMBL; Z72809; CAA97007.1; -; Genomic_DNA.
DR EMBL; AY558269; AAS56595.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08119.1; -; Genomic_DNA.
DR PIR; S64315; S64315.
DR RefSeq; NP_011538.3; NM_001181153.3.
DR PDB; 5XOX; X-ray; 3.00 A; A/B/C/D/E/F=1-237.
DR PDBsum; 5XOX; -.
DR AlphaFoldDB; P53215; -.
DR SMR; P53215; -.
DR BioGRID; 33266; 81.
DR DIP; DIP-1670N; -.
DR IntAct; P53215; 72.
DR MINT; P53215; -.
DR STRING; 4932.YGR024C; -.
DR iPTMnet; P53215; -.
DR MaxQB; P53215; -.
DR PaxDb; P53215; -.
DR PRIDE; P53215; -.
DR EnsemblFungi; YGR024C_mRNA; YGR024C; YGR024C.
DR GeneID; 852908; -.
DR KEGG; sce:YGR024C; -.
DR SGD; S000003256; THG1.
DR VEuPathDB; FungiDB:YGR024C; -.
DR eggNOG; KOG2721; Eukaryota.
DR GeneTree; ENSGT00390000011705; -.
DR HOGENOM; CLU_044271_0_1_1; -.
DR InParanoid; P53215; -.
DR OMA; WKQHTEI; -.
DR BioCyc; MetaCyc:G3O-30749-MON; -.
DR BioCyc; YEAST:G3O-30749-MON; -.
DR BRENDA; 2.7.7.79; 984.
DR PRO; PR:P53215; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53215; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008193; F:tRNA guanylyltransferase activity; IDA:SGD.
DR GO; GO:0006400; P:tRNA modification; IDA:SGD.
DR GO; GO:0008033; P:tRNA processing; ISS:UniProtKB.
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; PTHR12729; 1.
DR Pfam; PF04446; Thg1; 1.
DR Pfam; PF14413; Thg1C; 1.
DR PIRSF; PIRSF028980; tRNAHis_guanylyltransferase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; GTP-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..237
FT /note="tRNA(His) guanylyltransferase"
FT /id="PRO_0000202788"
FT BINDING 29..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 76..77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:5XOX"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:5XOX"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:5XOX"
FT HELIX 48..64
FT /evidence="ECO:0007829|PDB:5XOX"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:5XOX"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5XOX"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:5XOX"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:5XOX"
FT HELIX 94..116
FT /evidence="ECO:0007829|PDB:5XOX"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5XOX"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:5XOX"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:5XOX"
FT HELIX 140..171
FT /evidence="ECO:0007829|PDB:5XOX"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:5XOX"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:5XOX"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:5XOX"
FT STRAND 213..221
FT /evidence="ECO:0007829|PDB:5XOX"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:5XOX"
SQ SEQUENCE 237 AA; 27757 MW; CCB018E24B9EEA26 CRC64;
MANSKFGYVR QFETHDVILP QCYIVVRIDG KKFHEFSKFY EFAKPNDENA LKLMNACAKN
LVLKYKNDII LAFGESDEYS FILKSSTTLF NRRKDKLATL FGSFFTSNYV ALWAKFFPEK
PLNIKHLPYF DSRCVAYPNL QTIKDYLSWR YVDTHINNLY NTTFWQLIIK CGLTPQESEK
KLCGTFSNEK QEILFSECGI NYNNEPEMFK KGSLVTRKGE ILHINVIAQI DELFEGY
