Modomics - A Database of RNA Modifications

ID Card:

Full name: tRNA (guanine(26)-N(2))-dimethyltransferase, mitochondrial
GI: 136242
Orf: YDR120C
COG: COG1867
UniProt: P15565
Alpha Fold Predicted Structure: AF-P15565-F1
Enzyme type: methyltransferase
Position of modification - modification: t:26 - m2,2G



Protein sequence:

MEGFFRIPLKRANLHGMLKAAISKIKANFTAYGAPRINIEDFNIVKEGKAEILFPKKETVFYNPIQQFNRDLSVTCIKAWDNLYGEECGQKRNNKKSKKKRCAETNDDSSKRQKMGNGSPKEAVGNSNRNEPYINILEALSATGLRAIRYAHEIPHVREVIANDLLPEAVESIKRNVEYNSVENIVKPNLDDANVLMYRNKATNNKFHVIDLDPYGTVTPFVDAAIQSIEEGGLMLVTCTDLSVLAGNGYPEKCFALYGGANMVSHESTHESALRLVLNLLKQTAAKYKKTVEPLLSLSIDFYVRVFVKVKTSPIEVKNVMSSTMTTYHCSRCGSYHNQPLGRISQREGRNNKTFTKYSVAQGPPVDTKCKFCEGTYHLAGPMYAGPLHNKEFIEEVLRINKEEHRDQDDTYGTRKRIEGMLSLAKNELSDSPFYFSPNHIASVIKLQVPPLKKVVAGLGSLGFECSLTHAQPSSLKTNAPWDAIWYVMQKCDDEKKDLSKMNPNTTGYKILSAMPGWLSGTVKSEYDSKLSFAPNEQSGNIEKLRKLKIVRYQENPTKNWGPKARPNTS

Comments:

S-Adenosyl methionine (SAM or AdoMet) consists of an adenosyl cation attached to the sulfur methionine. It is synthesized from ATP and methionine by S-Adenosylmethionine synthetase enzyme through the the reaction of ATP with L-methionine and water forming as catalytical product S-adenosyl-L-methionine. SAM is a common cosubstrate involved in several reactions, among which methyl group transfers. Trm1 di-methylates a single guanine residue at position 26 of most tRNAs using SAM as a donor of the methyl groups, and is required for the modification of both mitochondrial and cytoplasmic tRNAs.





Alpha Fold Predicted Structure:




Downloading... [233210/517076]


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Protein sequence:

M E G F F R I P L K R A N L H G M L K A A I S K I K A N F T A Y G A P R I N I E D F N I V K E G K A E I L F P K K E T V F Y N P I Q Q F N R D L S V T C I K A W D N L Y G E E C G Q K R N N K K S K K K R C A E T N D D S S K R Q K M G N G S P K E A V G N S N R N E P Y I N I L E A L S A T G L R A I R Y A H E I P H V R E V I A N D L L P E A V E S I K R N V E Y N S V E N I V K P N L D D A N V L M Y R N K A T N N K F H V I D L D P Y G T V T P F V D A A I Q S I E E G G L M L V T C T D L S V L A G N G Y P E K C F A L Y G G A N M V S H E S T H E S A L R L V L N L L K Q T A A K Y K K T V E P L L S L S I D F Y V R V F V K V K T S P I E V K N V M S S T M T T Y H C S R C G S Y H N Q P L G R I S Q R E G R N N K T F T K Y S V A Q G P P V D T K C K F C E G T Y H L A G P M Y A G P L H N K E F I E E V L R I N K E E H R D Q D D T Y G T R K R I E G M L S L A K N E L S D S P F Y F S P N H I A S V I K L Q V P P L K K V V A G L G S L G F E C S L T H A Q P S S L K T N A P W D A I W Y V M Q K C D D E K K D L S K M N P N T T G Y K I L S A M P G W L S G T V K S E Y D S K L S F A P N E Q S G N I E K L R K L K I V R Y Q E N P T K N W G P K A R P N T S
50100150200250300350400450500550SequenceGHTBSN

Secondary Structure Alphabet

  • G: 3-turn helix (310helix)
  • H: α-helix
  • I: 𝝅-helix (5 - turn helix)
  • T: Hydrogen Bonded Turn
  • B: β-sheet
  • S: Bend
  • C: Coil (residues not present in any of the above conformations)
  • N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files   AF-P15565-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-P15565-F1.cif  
DSSP Secondary Structures   P15565.dssp  





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