Modomics - A Database of RNA Modifications

ID Card:

Full name: Multisite-specific tRNA:(cytosine-C(5))-methyltransferase
Synonym: Ncl1p
GI: 586408
Orf: YBL024W
COG: COG0144
UniProt: P38205
Alpha Fold Predicted Structure: AF-P38205-F1
Enzyme type: methyltransferase
Position of modification - modification: t:34 - m5C
t:40 - m5C
t:48 - m5C



Protein sequence:

MARRKNFKKGNKKTFGARDDSRAQKNWSELVKENEKWEKYYKTLALFPEDQWEEFKKTCQAPLPLTFRITGSRKHAGEVLNLFKERHLPNLTNVEFEGEKIKAPVELPWYPDHLAWQLDVPKTVIRKNEQFAKTQRFLVVENAVGNISRQEAVSMIPPIVLEVKPHHTVLDMCAAPGSKTAQLIEALHKDTDEPSGFVVANDADARRSHMLVHQLKRLNSANLMVVNHDAQFFPRIRLHGNSNNKNDVLKFDRILCDVPCSGDGTMRKNVNVWKDWNTQAGLGLHAVQLNILNRGLHLLKNNGRLVYSTCSLNPIENEAVVAEALRKWGDKIRLVNCDDKLPGLIRSKGVSKWPVYDRNLTEKTKGDEGTLDSFFSPSEEEASKFNLQNCMRVYPHQQNTGGFFITVFEKVEDSTEAATEKLSSETPALESEGPQTKKIKVEEVQKKERLPRDANEEPFVFVDPQHEALKVCWDFYGIDNIFDRNTCLVRNATGEPTRVVYTVCPALKDVIQANDDRLKIIYSGVKLFVSQRSDIECSWRIQSESLPIMKHHMKSNRIVEANLEMLKHLLIESFPNFDDIRSKNIDNDFVEKMTKLSSGCAFIDVSRNDPAKENLFLPVWKGNKCINLMVCKEDTHELLYRIFGIDANAKATPSAEEKEKEKETTESPAETTTGTSTEAPSAAN

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. Trm4 is a multisite-specific—monomeric enzyme using SAM as a cosubstrate. In most mature tRNAs modifies either 48 or 49, and only two tRNAs Trm4 modifies either 34 or 40, but only before the intron is removed. In yeast, the activity of Trm4 and consequently the degree of m5C modification in tRNALeu depends on certain stress conditions (presence of H2O2), which causes selective translation of mRNA from genes enriched in the TTG codon.





Alpha Fold Predicted Structure:




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Protein sequence:

M A R R K N F K K G N K K T F G A R D D S R A Q K N W S E L V K E N E K W E K Y Y K T L A L F P E D Q W E E F K K T C Q A P L P L T F R I T G S R K H A G E V L N L F K E R H L P N L T N V E F E G E K I K A P V E L P W Y P D H L A W Q L D V P K T V I R K N E Q F A K T Q R F L V V E N A V G N I S R Q E A V S M I P P I V L E V K P H H T V L D M C A A P G S K T A Q L I E A L H K D T D E P S G F V V A N D A D A R R S H M L V H Q L K R L N S A N L M V V N H D A Q F F P R I R L H G N S N N K N D V L K F D R I L C D V P C S G D G T M R K N V N V W K D W N T Q A G L G L H A V Q L N I L N R G L H L L K N N G R L V Y S T C S L N P I E N E A V V A E A L R K W G D K I R L V N C D D K L P G L I R S K G V S K W P V Y D R N L T E K T K G D E G T L D S F F S P S E E E A S K F N L Q N C M R V Y P H Q Q N T G G F F I T V F E K V E D S T E A A T E K L S S E T P A L E S E G P Q T K K I K V E E V Q K K E R L P R D A N E E P F V F V D P Q H E A L K V C W D F Y G I D N I F D R N T C L V R N A T G E P T R V V Y T V C P A L K D V I Q A N D D R L K I I Y S G V K L F V S Q R S D I E C S W R I Q S E S L P I M K H H M K S N R I V E A N L E M L K H L L I E S F P N F D D I R S K N I D N D F V E K M T K L S S G C A F I D V S R N D P A K E N L F L P V W K G N K C I N L M V C K E D T H E L L Y R I F G I D A N A K A T P S A E E K E K E K E T T E S P A E T T T G T S T E A P S A A N
100200300400500600SequenceGHITBSN

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-P38205-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-P38205-F1.cif  
DSSP Secondary Structures   P38205.dssp  





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