Protein : Qrob_P0128400.2 Q. robur
Protein Identifier  ? Qrob_P0128400.2 Organism . Name  Quercus robur
Score  95.0 Score Type  egn
Protein Description  (M=1) 2.3.1.221 - Noranthrone synthase. Code Enzyme  EC:2.3.1.221
Gene Prediction Quality  validated Protein length 

Sequence

Length: 235  
Kegg Orthology  K14292
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0 Synonyms

3 GO Terms

Identifier Name Description
GO:0008168 methyltransferase activity Catalysis of the transfer of a methyl group to an acceptor molecule.
GO:0001510 RNA methylation Posttranscriptional addition of a methyl group to either a nucleotide or 2'-O ribose in a polyribonucleotide. Usually uses S-adenosylmethionine as a cofactor.
GO:0009452 7-methylguanosine RNA capping The sequence of enzymatic reactions by which the 5' cap structure, an inverted 7-methylguanosine linked via a 5'-5' triphosphate bridge (m7G(5')ppp(5')X) to the first transcribed residue, is added to a nascent transcript.

35 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pper:PRUPE_ppa010390mg 1 225 + 225 Gaps:10 88.84 251 70.85 1e-108 hypothetical protein
blastp_kegg lcl|pmum:103328239 1 225 + 225 Gaps:10 88.84 251 70.85 2e-108 trimethylguanosine synthase
blastp_kegg lcl|fve:101305582 25 233 + 209 Gaps:6 82.33 249 74.63 1e-107 trimethylguanosine synthase-like
blastp_kegg lcl|vvi:100262065 2 225 + 224 Gaps:11 86.69 248 71.63 5e-107 trimethylguanosine synthase-like
blastp_kegg lcl|pxb:103960253 2 225 + 224 Gaps:7 87.15 249 69.59 5e-106 trimethylguanosine synthase-like
blastp_kegg lcl|pxb:103945399 2 225 + 224 Gaps:7 87.15 249 69.59 5e-106 trimethylguanosine synthase-like
blastp_kegg lcl|mdm:103426088 25 227 + 203 Gaps:6 79.12 249 75.13 7e-106 trimethylguanosine synthase-like
blastp_kegg lcl|sot:102588042 3 233 + 231 Gaps:10 89.45 256 64.19 3e-100 trimethylguanosine synthase-like
blastp_kegg lcl|sly:101266167 27 233 + 207 Gaps:7 83.47 242 70.30 5e-100 trimethylguanosine synthase-like
blastp_kegg lcl|eus:EUTSA_v10008708mg 18 226 + 209 Gaps:9 89.69 223 67.00 9e-99 hypothetical protein
blastp_pdb 3gdh_C 36 233 + 198 Gaps:6 80.50 241 53.09 9e-63 mol:protein length:241 Trimethylguanosine synthase homolog
blastp_pdb 3gdh_B 36 233 + 198 Gaps:6 80.50 241 53.09 9e-63 mol:protein length:241 Trimethylguanosine synthase homolog
blastp_pdb 3gdh_A 36 233 + 198 Gaps:6 80.50 241 53.09 9e-63 mol:protein length:241 Trimethylguanosine synthase homolog
blastp_pdb 3egi_D 48 233 + 186 Gaps:6 88.35 206 52.75 6e-57 mol:protein length:206 Trimethylguanosine synthase homolog
blastp_pdb 3egi_C 48 233 + 186 Gaps:6 88.35 206 52.75 6e-57 mol:protein length:206 Trimethylguanosine synthase homolog
blastp_pdb 3egi_B 48 233 + 186 Gaps:6 88.35 206 52.75 6e-57 mol:protein length:206 Trimethylguanosine synthase homolog
blastp_pdb 3egi_A 48 233 + 186 Gaps:6 88.35 206 52.75 6e-57 mol:protein length:206 Trimethylguanosine synthase homolog
blastp_pdb 2as0_B 85 161 + 77 Gaps:6 20.96 396 39.76 2e-06 mol:protein length:396 hypothetical protein PH1915
blastp_pdb 2as0_A 85 161 + 77 Gaps:6 20.96 396 39.76 2e-06 mol:protein length:396 hypothetical protein PH1915
blastp_uniprot_sprot sp|Q923W1|TGS1_MOUSE 36 233 + 198 Gaps:16 22.74 853 54.12 4e-61 Trimethylguanosine synthase OS Mus musculus GN Tgs1 PE 1 SV 2
blastp_uniprot_sprot sp|P85107|TGS1_RAT 36 233 + 198 Gaps:6 22.82 850 53.09 4e-60 Trimethylguanosine synthase OS Rattus norvegicus GN Tgs1 PE 1 SV 1
blastp_uniprot_sprot sp|Q96RS0|TGS1_HUMAN 36 233 + 198 Gaps:6 22.74 853 53.61 1e-58 Trimethylguanosine synthase OS Homo sapiens GN TGS1 PE 1 SV 3
blastp_uniprot_sprot sp|Q09814|TGS1_SCHPO 34 220 + 187 Gaps:9 79.50 239 41.58 7e-42 Trimethylguanosine synthase OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN tgs1 PE 1 SV 3
blastp_uniprot_sprot sp|Q12052|TGS1_YEAST 16 214 + 199 Gaps:21 69.21 315 36.24 1e-26 Trimethylguanosine synthase OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN TGS1 PE 1 SV 1
blastp_uniprot_sprot sp|Q5UQR2|YL320_MIMIV 89 207 + 119 Gaps:11 47.66 256 32.79 3e-10 Uncharacterized protein L320 OS Acanthamoeba polyphaga mimivirus GN MIMI_L320 PE 4 SV 1
blastp_uniprot_sprot sp|Q7NGN4|Y3134_GLOVI 57 171 + 115 Gaps:1 24.95 457 28.95 8e-08 Uncharacterized RNA methyltransferase gll3134 OS Gloeobacter violaceus (strain PCC 7421) GN gll3134 PE 3 SV 1
blastp_uniprot_sprot sp|Q74I68|Y1698_LACJO 53 164 + 112 Gaps:6 25.78 450 26.72 1e-06 Uncharacterized RNA methyltransferase LJ_1698 OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533) GN LJ_1698 PE 3 SV 1
blastp_uniprot_sprot sp|Q9KF10|Y687_BACHD 2 164 + 163 Gaps:19 37.55 458 23.26 5e-06 Uncharacterized RNA methyltransferase BH0687 OS Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) GN BH0687 PE 3 SV 1
rpsblast_cdd gnl|CDD|150199 89 225 + 137 Gaps:7 87.27 165 45.83 4e-43 pfam09445 Methyltransf_15 RNA cap guanine-N2 methyltransferase. RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.
rpsblast_cdd gnl|CDD|176216 65 157 + 93 Gaps:20 29.88 338 27.72 1e-08 cd08254 hydroxyacyl_CoA_DH 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase N-benzyl-3-pyrrolidinol dehydrogenase and other MDR family members. This group contains enzymes of the zinc-dependent alcohol dehydrogenase family including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA NADH and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR) which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants mammals) or tetramers (yeast bacteria) and have 2 tightly bound zinc atoms per subunit a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis the zinc ion helps coordinate the alcohol followed by deprotonation of a histidine the ribose of NAD a serine then the alcohol which allows the transfer of a hydride to NAD+ creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria the active site zinc binds an aldehyde polarizing it and leading to the reverse reaction.

5 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Gene3D 80 172 93 G3DSA:3.40.50.150 none none IPR029063
Pfam 89 225 137 PF09445 none RNA cap guanine-N2 methyltransferase IPR019012
PANTHER 1 223 223 PTHR14741 none none none
SUPERFAMILY 39 206 168 SSF53335 none none IPR029063
PANTHER 1 223 223 PTHR14741:SF32 none none none

0 Localization

0 Qtllist

0 Targeting