Full text data of THG1L
THG1L
(ICF45)
[Confidence: low (only semi-automatic identification from reviews)]
Probable tRNA(His) guanylyltransferase; 2.7.7.79 (Interphase cytoplasmic foci protein 45; tRNA-histidine guanylyltransferase)
Probable tRNA(His) guanylyltransferase; 2.7.7.79 (Interphase cytoplasmic foci protein 45; tRNA-histidine guanylyltransferase)
UniProt
Q9NWX6
ID THG1_HUMAN Reviewed; 298 AA.
AC Q9NWX6; D3DQJ5; Q53G12; Q7L5R3; Q9H0S2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2007, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Probable tRNA(His) guanylyltransferase;
DE EC=2.7.7.79;
DE AltName: Full=Interphase cytoplasmic foci protein 45;
DE AltName: Full=tRNA-histidine guanylyltransferase;
GN Name=THG1L; Synonyms=ICF45;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15459185; DOI=10.1074/jbc.M406737200;
RA Guo D., Hu K., Lei Y., Wang Y., Ma T., He D.;
RT "Identification and characterization of a novel cytoplasm protein
RT ICF45 that is involved in cell cycle regulation.";
RL J. Biol. Chem. 279:53498-53505(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-232.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-232.
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-232.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-232.
RC TISSUE=Brain, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH
RP MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, COFACTOR, SUBUNIT, AND
RP MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127;
RP HIS-181; LYS-216 AND ASN-227.
RX PubMed=21059936; DOI=10.1073/pnas.1010436107;
RA Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H.,
RA Jackman J.E., Doublie S.;
RT "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl
RT transferase, shares unexpected structural homology with canonical 5'-
RT 3' DNA polymerases.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010).
CC -!- FUNCTION: Adds a GMP to the 5'-end of tRNA(His) after
CC transcription and RNase P cleavage. This step is essential for
CC proper recognition of the tRNA and for the fidelity of protein
CC synthesis.
CC -!- CATALYTIC ACTIVITY: p-tRNA(His) + ATP + GTP = pppG-P-tRNA(His) +
CC AMP + diphosphate.
CC -!- COFACTOR: Binds 2 magnesium ions per subunit.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Found near the nuclear
CC membrane.
CC -!- TISSUE SPECIFICITY: Expressed in many tissues.
CC -!- SIMILARITY: Belongs to the tRNA(His) guanylyltransferase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01523.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH01852.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AY463216; AAS21134.1; -; mRNA.
DR EMBL; AL136669; CAB66604.1; -; mRNA.
DR EMBL; AK000553; BAA91249.1; -; mRNA.
DR EMBL; AK021663; BAB13870.1; -; mRNA.
DR EMBL; CR533503; CAG38534.1; -; mRNA.
DR EMBL; AK223119; BAD96839.1; -; mRNA.
DR EMBL; CH471062; EAW61590.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61591.1; -; Genomic_DNA.
DR EMBL; BC001523; AAH01523.2; ALT_INIT; mRNA.
DR EMBL; BC001852; AAH01852.2; ALT_INIT; mRNA.
DR EMBL; BC023521; AAH23521.1; -; mRNA.
DR RefSeq; NP_060342.2; NM_017872.3.
DR UniGene; Hs.353090; -.
DR PDB; 3OTB; X-ray; 2.95 A; A/B=30-298.
DR PDB; 3OTC; X-ray; 3.01 A; A/B=30-298.
DR PDB; 3OTD; X-ray; 2.28 A; A/B=30-298.
DR PDB; 3OTE; X-ray; 2.56 A; A/B=30-298.
DR PDBsum; 3OTB; -.
DR PDBsum; 3OTC; -.
DR PDBsum; 3OTD; -.
DR PDBsum; 3OTE; -.
DR ProteinModelPortal; Q9NWX6; -.
DR SMR; Q9NWX6; 33-296.
DR DIP; DIP-59479N; -.
DR IntAct; Q9NWX6; 1.
DR MINT; MINT-4873002; -.
DR STRING; 9606.ENSP00000231198; -.
DR PhosphoSite; Q9NWX6; -.
DR DMDM; 146325755; -.
DR PaxDb; Q9NWX6; -.
DR PeptideAtlas; Q9NWX6; -.
DR PRIDE; Q9NWX6; -.
DR DNASU; 54974; -.
DR Ensembl; ENST00000231198; ENSP00000231198; ENSG00000113272.
DR GeneID; 54974; -.
DR KEGG; hsa:54974; -.
DR UCSC; uc003lxd.3; human.
DR CTD; 54974; -.
DR GeneCards; GC05P157159; -.
DR HGNC; HGNC:26053; THG1L.
DR HPA; HPA035877; -.
DR HPA; HPA035878; -.
DR neXtProt; NX_Q9NWX6; -.
DR PharmGKB; PA162405691; -.
DR eggNOG; COG4021; -.
DR HOGENOM; HOG000204890; -.
DR HOVERGEN; HBG054289; -.
DR InParanoid; Q9NWX6; -.
DR KO; K10761; -.
DR OMA; KFEYVRN; -.
DR OrthoDB; EOG7X0VHR; -.
DR PhylomeDB; Q9NWX6; -.
DR ChiTaRS; THG1L; human.
DR EvolutionaryTrace; Q9NWX6; -.
DR GeneWiki; THG1L; -.
DR GenomeRNAi; 54974; -.
DR NextBio; 58226; -.
DR PRO; PR:Q9NWX6; -.
DR ArrayExpress; Q9NWX6; -.
DR Bgee; Q9NWX6; -.
DR CleanEx; HS_THG1L; -.
DR Genevestigator; Q9NWX6; -.
DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
DR GO; GO:0005525; F:GTP binding; IDA:BHF-UCL.
DR GO; GO:0000287; F:magnesium ion binding; IDA:BHF-UCL.
DR GO; GO:0000049; F:tRNA binding; TAS:BHF-UCL.
DR GO; GO:0008193; F:tRNA guanylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR InterPro; IPR025845; Thg1_C_dom.
DR InterPro; IPR024956; tRNAHis_GuaTrfase_cat.
DR InterPro; IPR007537; tRNAHis_GuaTrfase_Thg1.
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; Complete proteome; Cytoplasm; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Polymorphism; Reference proteome; Transferase; tRNA processing.
FT CHAIN 1 298 Probable tRNA(His) guanylyltransferase.
FT /FTId=PRO_0000284984.
FT NP_BIND 58 63 GTP.
FT NP_BIND 104 105 GTP.
FT METAL 58 58 Magnesium 1; catalytic.
FT METAL 58 58 Magnesium 2; catalytic.
FT METAL 59 59 Magnesium 1; via carbonyl oxygen;
FT catalytic.
FT METAL 105 105 Magnesium 1; catalytic.
FT METAL 105 105 Magnesium 2; catalytic.
FT VARIANT 232 232 L -> P (in dbSNP:rs2270812).
FT /FTId=VAR_031871.
FT MUTAGEN 58 58 D->A: Reduces activity by 99.5%.
FT MUTAGEN 63 63 H->A: Slightly reduced enzyme activity.
FT MUTAGEN 104 104 S->A: Slightly reduced enzyme activity.
FT MUTAGEN 105 105 D->A: Loss of enzyme activity.
FT MUTAGEN 106 106 E->A: Reduces activity by 95%.
FT MUTAGEN 127 127 T->A: Abolishes oligomerization. Loss of
FT enzyme activity.
FT MUTAGEN 181 181 H->A: Loss of enzyme activity.
FT MUTAGEN 216 216 K->A: Reduces activity by 98.5%.
FT MUTAGEN 227 227 N->A: Loss of enzyme activity.
FT CONFLICT 57 57 L -> Q (in Ref. 5; BAD96839).
FT HELIX 36 41
FT STRAND 51 59
FT HELIX 62 68
FT HELIX 77 93
FT STRAND 94 103
FT STRAND 106 111
FT TURN 117 120
FT HELIX 122 139
FT HELIX 141 144
FT STRAND 146 148
FT STRAND 156 165
FT HELIX 166 195
FT HELIX 201 208
FT HELIX 213 224
FT HELIX 228 230
FT HELIX 233 237
FT STRAND 239 243
FT STRAND 274 277
FT STRAND 281 283
FT HELIX 284 289
FT HELIX 292 295
SQ SEQUENCE 298 AA; 34831 MW; A6C941B75611C448 CRC64;
MWGACKVKVH DSLATISITL RRYLRLGATM AKSKFEYVRD FEADDTCLAH CWVVVRLDGR
NFHRFAEKHN FAKPNDSRAL QLMTKCAQTV MEELEDIVIA YGQSDEYSFV FKRKTNWFKR
RASKFMTHVA SQFASSYVFY WRDYFEDQPL LYPPGFDGRV VVYPSNQTLK DYLSWRQADC
HINNLYNTVF WALIQQSGLT PVQAQGRLQG TLAADKNEIL FSEFNINYNN ELPMYRKGTV
LIWQKVDEVM TKEIKLPTEM EGKKMAVTRT RTKPVPLHCD IIGDAFWKEH PEILDEDS
//
ID THG1_HUMAN Reviewed; 298 AA.
AC Q9NWX6; D3DQJ5; Q53G12; Q7L5R3; Q9H0S2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2007, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Probable tRNA(His) guanylyltransferase;
DE EC=2.7.7.79;
DE AltName: Full=Interphase cytoplasmic foci protein 45;
DE AltName: Full=tRNA-histidine guanylyltransferase;
GN Name=THG1L; Synonyms=ICF45;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15459185; DOI=10.1074/jbc.M406737200;
RA Guo D., Hu K., Lei Y., Wang Y., Ma T., He D.;
RT "Identification and characterization of a novel cytoplasm protein
RT ICF45 that is involved in cell cycle regulation.";
RL J. Biol. Chem. 279:53498-53505(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-232.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-232.
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-232.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-232.
RC TISSUE=Brain, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH
RP MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, COFACTOR, SUBUNIT, AND
RP MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127;
RP HIS-181; LYS-216 AND ASN-227.
RX PubMed=21059936; DOI=10.1073/pnas.1010436107;
RA Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H.,
RA Jackman J.E., Doublie S.;
RT "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl
RT transferase, shares unexpected structural homology with canonical 5'-
RT 3' DNA polymerases.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010).
CC -!- FUNCTION: Adds a GMP to the 5'-end of tRNA(His) after
CC transcription and RNase P cleavage. This step is essential for
CC proper recognition of the tRNA and for the fidelity of protein
CC synthesis.
CC -!- CATALYTIC ACTIVITY: p-tRNA(His) + ATP + GTP = pppG-P-tRNA(His) +
CC AMP + diphosphate.
CC -!- COFACTOR: Binds 2 magnesium ions per subunit.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Found near the nuclear
CC membrane.
CC -!- TISSUE SPECIFICITY: Expressed in many tissues.
CC -!- SIMILARITY: Belongs to the tRNA(His) guanylyltransferase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01523.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH01852.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AY463216; AAS21134.1; -; mRNA.
DR EMBL; AL136669; CAB66604.1; -; mRNA.
DR EMBL; AK000553; BAA91249.1; -; mRNA.
DR EMBL; AK021663; BAB13870.1; -; mRNA.
DR EMBL; CR533503; CAG38534.1; -; mRNA.
DR EMBL; AK223119; BAD96839.1; -; mRNA.
DR EMBL; CH471062; EAW61590.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61591.1; -; Genomic_DNA.
DR EMBL; BC001523; AAH01523.2; ALT_INIT; mRNA.
DR EMBL; BC001852; AAH01852.2; ALT_INIT; mRNA.
DR EMBL; BC023521; AAH23521.1; -; mRNA.
DR RefSeq; NP_060342.2; NM_017872.3.
DR UniGene; Hs.353090; -.
DR PDB; 3OTB; X-ray; 2.95 A; A/B=30-298.
DR PDB; 3OTC; X-ray; 3.01 A; A/B=30-298.
DR PDB; 3OTD; X-ray; 2.28 A; A/B=30-298.
DR PDB; 3OTE; X-ray; 2.56 A; A/B=30-298.
DR PDBsum; 3OTB; -.
DR PDBsum; 3OTC; -.
DR PDBsum; 3OTD; -.
DR PDBsum; 3OTE; -.
DR ProteinModelPortal; Q9NWX6; -.
DR SMR; Q9NWX6; 33-296.
DR DIP; DIP-59479N; -.
DR IntAct; Q9NWX6; 1.
DR MINT; MINT-4873002; -.
DR STRING; 9606.ENSP00000231198; -.
DR PhosphoSite; Q9NWX6; -.
DR DMDM; 146325755; -.
DR PaxDb; Q9NWX6; -.
DR PeptideAtlas; Q9NWX6; -.
DR PRIDE; Q9NWX6; -.
DR DNASU; 54974; -.
DR Ensembl; ENST00000231198; ENSP00000231198; ENSG00000113272.
DR GeneID; 54974; -.
DR KEGG; hsa:54974; -.
DR UCSC; uc003lxd.3; human.
DR CTD; 54974; -.
DR GeneCards; GC05P157159; -.
DR HGNC; HGNC:26053; THG1L.
DR HPA; HPA035877; -.
DR HPA; HPA035878; -.
DR neXtProt; NX_Q9NWX6; -.
DR PharmGKB; PA162405691; -.
DR eggNOG; COG4021; -.
DR HOGENOM; HOG000204890; -.
DR HOVERGEN; HBG054289; -.
DR InParanoid; Q9NWX6; -.
DR KO; K10761; -.
DR OMA; KFEYVRN; -.
DR OrthoDB; EOG7X0VHR; -.
DR PhylomeDB; Q9NWX6; -.
DR ChiTaRS; THG1L; human.
DR EvolutionaryTrace; Q9NWX6; -.
DR GeneWiki; THG1L; -.
DR GenomeRNAi; 54974; -.
DR NextBio; 58226; -.
DR PRO; PR:Q9NWX6; -.
DR ArrayExpress; Q9NWX6; -.
DR Bgee; Q9NWX6; -.
DR CleanEx; HS_THG1L; -.
DR Genevestigator; Q9NWX6; -.
DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
DR GO; GO:0005525; F:GTP binding; IDA:BHF-UCL.
DR GO; GO:0000287; F:magnesium ion binding; IDA:BHF-UCL.
DR GO; GO:0000049; F:tRNA binding; TAS:BHF-UCL.
DR GO; GO:0008193; F:tRNA guanylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR InterPro; IPR025845; Thg1_C_dom.
DR InterPro; IPR024956; tRNAHis_GuaTrfase_cat.
DR InterPro; IPR007537; tRNAHis_GuaTrfase_Thg1.
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; Complete proteome; Cytoplasm; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Polymorphism; Reference proteome; Transferase; tRNA processing.
FT CHAIN 1 298 Probable tRNA(His) guanylyltransferase.
FT /FTId=PRO_0000284984.
FT NP_BIND 58 63 GTP.
FT NP_BIND 104 105 GTP.
FT METAL 58 58 Magnesium 1; catalytic.
FT METAL 58 58 Magnesium 2; catalytic.
FT METAL 59 59 Magnesium 1; via carbonyl oxygen;
FT catalytic.
FT METAL 105 105 Magnesium 1; catalytic.
FT METAL 105 105 Magnesium 2; catalytic.
FT VARIANT 232 232 L -> P (in dbSNP:rs2270812).
FT /FTId=VAR_031871.
FT MUTAGEN 58 58 D->A: Reduces activity by 99.5%.
FT MUTAGEN 63 63 H->A: Slightly reduced enzyme activity.
FT MUTAGEN 104 104 S->A: Slightly reduced enzyme activity.
FT MUTAGEN 105 105 D->A: Loss of enzyme activity.
FT MUTAGEN 106 106 E->A: Reduces activity by 95%.
FT MUTAGEN 127 127 T->A: Abolishes oligomerization. Loss of
FT enzyme activity.
FT MUTAGEN 181 181 H->A: Loss of enzyme activity.
FT MUTAGEN 216 216 K->A: Reduces activity by 98.5%.
FT MUTAGEN 227 227 N->A: Loss of enzyme activity.
FT CONFLICT 57 57 L -> Q (in Ref. 5; BAD96839).
FT HELIX 36 41
FT STRAND 51 59
FT HELIX 62 68
FT HELIX 77 93
FT STRAND 94 103
FT STRAND 106 111
FT TURN 117 120
FT HELIX 122 139
FT HELIX 141 144
FT STRAND 146 148
FT STRAND 156 165
FT HELIX 166 195
FT HELIX 201 208
FT HELIX 213 224
FT HELIX 228 230
FT HELIX 233 237
FT STRAND 239 243
FT STRAND 274 277
FT STRAND 281 283
FT HELIX 284 289
FT HELIX 292 295
SQ SEQUENCE 298 AA; 34831 MW; A6C941B75611C448 CRC64;
MWGACKVKVH DSLATISITL RRYLRLGATM AKSKFEYVRD FEADDTCLAH CWVVVRLDGR
NFHRFAEKHN FAKPNDSRAL QLMTKCAQTV MEELEDIVIA YGQSDEYSFV FKRKTNWFKR
RASKFMTHVA SQFASSYVFY WRDYFEDQPL LYPPGFDGRV VVYPSNQTLK DYLSWRQADC
HINNLYNTVF WALIQQSGLT PVQAQGRLQG TLAADKNEIL FSEFNINYNN ELPMYRKGTV
LIWQKVDEVM TKEIKLPTEM EGKKMAVTRT RTKPVPLHCD IIGDAFWKEH PEILDEDS
//