Q9U6M1 · JBP1_LEITA

Function

function

Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Also specifically binds to base J-containing DNA (J-DNA). Involved in propagation and maintenance of DNA base J synthesis initiated by JBP2 by specifically binding already synthesized DNA base J and propagating J synthesis. Thymine dioxygenase activity and J-DNA-binding are independent functions.

Catalytic activity

Cofactor

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 1 Fe2+ ion per subunit.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site189Fe cation (UniProtKB | ChEBI); catalytic
Binding site191Fe cation (UniProtKB | ChEBI); catalytic
Binding site239Fe cation (UniProtKB | ChEBI); catalytic
Binding site2552-oxoglutarate (UniProtKB | ChEBI)
Site525Involved in J base recognition and binding, conferring specificity towards J-DNA

GO annotations

AspectTerm
Cellular Componentnucleus
Molecular FunctionDNA binding
Molecular Functionmetal ion binding
Molecular Functionthymine dioxygenase activity
Biological Processbase J metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Thymine dioxygenase JBP1
  • EC number
  • Alternative names
    • J-binding protein 1
    • Thymidine hydroxylase JBP1

Gene names

    • Name
      JBP1

Organism names

Accessions

  • Primary accession
    Q9U6M1

Organism-specific databases

Subcellular Location

Nucleus
Note: Localizes to discrete spots in the nucleus, probably the J-rich telomeres.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis189Impairs DNA base J biosynthesis.
Mutagenesis191Impairs DNA base J biosynthesis.
Mutagenesis239Impairs DNA base J biosynthesis.
Mutagenesis255Impairs DNA base J biosynthesis.
Mutagenesis259No effect.
Mutagenesis391No effect.
Mutagenesis436No effect.
Mutagenesis465No effect.
Mutagenesis468No effect.
Mutagenesis487-488No effect.
Mutagenesis518Decreases binding affinity for both J-DNA and normal DNA.
Mutagenesis522Decreases binding affinity for both J-DNA and normal DNA.
Mutagenesis524Slightly decreases binding affinity for both J-DNA and normal DNA.
Mutagenesis525Abolishes preference for J-DNA-binding.
Mutagenesis532Decreases binding affinity for both J-DNA and normal DNA.
Mutagenesis535No effect.
Mutagenesis536No effect.
Mutagenesis540-541No effect.
Mutagenesis553No effect.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003775541-827Thymine dioxygenase JBP1

Interaction

Subunit

Monomer. Binds to DNA as a monomer.

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region62-264Thymine dioxygenase
Region364-383Disordered
Region392-561DNA-binding JBP1 domain
Compositional bias539-564Basic and acidic residues
Region539-568Disordered

Domain

The DNA-binding JBP1 domain (DB-JBP1) is necessary and sufficient for binding to J-DNA.

Sequence similarities

Belongs to the TET family. JBP1 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    827
  • Mass (Da)
    93,403
  • Last updated
    2000-05-01 v1
  • Checksum
    5A4B502DE70A4BFE
MEPDSKKVKLDIFNFPTTRETRTPEEVAESYAEAVKSHPFYDNVHSVVDFYDSGTIKDGRGQIIGVVLREALPKYAASMASELLTSAAVRTSLRSMMFGGEPPLSGIAGYFDYRGSPVELKSRKTSFTYEHEAAWPAVFPVVDYVSEIYRHVAPERWKAQNDAIPDLVRIHGTPFSTLTINSRFRTASHTDVGDFDAGYSCIACLDGQFKGLALSFDDFGINVLLQPRDVMIFDSHHFHSNTEVELSFSGEDWKRLTCVFYYRAALGEPASYAEYQRRLEKSKTDTRFTPVVHHVRVKENGTSVNRPSPVYPISQSPFWVPMVAHCLQHCASAAQCVHEAMTADGSRLAEMMFGESLSTSDGIPLRGEDEKVKANGDSTPRPLSRLGGFSETNLMVSTAVEKKKYLDSEFLLHCISAQLLDMWKQARARWLELVGKEWAHMLALNPERKDFLWKNQSEMNSAFFDLCEVGKQVMLGLLGKEVALPKEEQAFWIMYAVHLSAACAEELHMPEVAMSLRKLNVKLKDFNFGGTRYFKDMPPEEKKRRMERKQRIEEARRHGMPSGSHEKRANWLTNDSFDYQTEDCVIDYAQHKWVLPALHAKEVTKTVRTGELPTTERVVRVLVVIPDPQSKLENVDCKLEVPDMVGSSSEWERLMSSPAVHRVLSAAQRNLQLPDSVTHGNVQTHFAFHSTLPTDIYDFVVLQHVLSRIPDDAQASAYIRRAAALCSGCLFVVETDVQCRQYYTLKYSIRCSYDTVAPLFFQQLHRVCYGTKTARVRTKGELESLIPTVCCARYKLQGSPLNTTVHVVSPFPSCEVQNLSSALCDRA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias539-564Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF182401
EMBL· GenBank· DDBJ
AAF01743.1
EMBL· GenBank· DDBJ
Genomic DNA
AY842844
EMBL· GenBank· DDBJ
AAX81332.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp