Modomics - A Database of RNA Modifications

ID Card:

Full name: Casein kinase I homolog HRR25
Synonym: HRR25
GI: 6325052
COG: COG0515
UniProt: P29295
Structures: | 4XHL | 5CYZ | 5CZO |
Alpha Fold Predicted Structure: AF-P29295-F1


PDB Structures:


4XHL

Structure Description:

Title:
Classification:
Technique:

Abstract of the PDB Structure's related Publication:

In budding yeast, the monopolin complex mediates sister kinetochore cross-linking and co-orientation in meiosis I. The CK1δ kinase Hrr25 is critical for sister kinetochore co-orientation, but its roles are not well understood. Here, we present the structures of Hrr25 and its complex with the monopolin subunit Mam1. Hrr25 possesses a "central domain" that packs tightly against the kinase C-lobe, adjacent to the binding site for Mam1. Together, the Hrr25 central domain and Mam1 form a novel, contiguous embellishment to the Hrr25 kinase domain that affects Hrr25 conformational dynamics and enzyme kinetics. Mam1 binds a hydrophobic surface on the Hrr25 N-lobe that is conserved in CK1δ-family kinases, suggesting a role for this surface in recruitment and/or regulation of these enzymes throughout eukaryotes. Finally, using purified proteins, we find that Hrr25 phosphorylates the kinetochore receptor for monopolin, Dsn1. Together with our new structural insights into the fully assembled monopolin complex, this finding suggests that tightly localized Hrr25 activity modulates monopolin complex-kinetochore interactions through phosphorylation of both kinetochore and monopolin complex components.

Download RCSB-PDB Structures:

Pdb Files   4XHL.pdb   5CYZ.pdb   5CZO.pdb  
Pdbx/mmCIF Files   4XHL.cif   5CYZ.cif   5CZO.cif  


Protein sequence:

MDLRVGRKFRIGRKIGSGSFGDIYHGTNLISGEEVAIKLESIRSRHPQLDYESRVYRYLSGGVGIPFIRWFGREGEYNAMVIDLLGPSLEDLFNYCHRRFSFKTVIMLALQMFCRIQYIHGRSFIHRDIKPDNFLMGVGRRGSTVHVIDFGLSKKYRDFNTHRHIPYRENKSLTGTARYASVNTHLGIEQSRRDDLESLGYVLIYFCKGSLPWQGLKATTKKQKYDRIMEKKLNVSVETLCSGLPLEFQEYMAYCKNLKFDEKPDYLFLARLFKDLSIKLEYHNDHLFDWTMLRYTKAMVEKQRDLLIEKGDLNANSNAASASNSTDNKSETFNKIKLLAMKKFPTHFHYYKNEDKHNPSPEEIKQQTILNNNAASSLPEELLNALDKGMENLRQQQPQQQVQSSQPQPQPQQLQQQPNGQRPNYYPEPLLQQQQRDSQEQQQQVPMATTRATQYPPQINSNNFNTNQASVPPQMRSNPQQPPQDKPAGQSIWL

Comments:

One of the many protein cofactors required for an early step in synthesis of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) groups present on uridines at the wobble position in tRNA. The enzyme that catalyzes this reaction is still unknown (2012).





Alpha Fold Predicted Structure:






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Protein sequence:

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

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-P29295-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-P29295-F1.cif  
DSSP Secondary Structures   P29295.dssp  





Publications:

Title Authors Journal Details PubMed Id DOI
A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae. Huang B, Lu J, Bystrom AS RNA [details] 18755837 -

Links:

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