Q4DBW3 (JBP1A_TRYCC) Reviewed, UniProtKB/Swiss-Prot
Last modified
February 6, 2013.
Version 23.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Thymine dioxygenase JBP1-A EC=1.14.11.6 Alternative name(s): J-binding protein 1A Thymidine hydroxylase JBP1-A | ||||
| Gene names |
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| Organism | Trypanosoma cruzi (strain CL Brener) [Complete proteome] | ||||
| Taxonomic identifier | 353153 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma › Schizotrypanum › ![]() |
Protein attributes
| Sequence length | 832 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| 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 By similarity. |
| Catalytic activity | Thymine + 2-oxoglutarate + O2 = 5-hydroxymethyluracil + succinate + CO2. |
| Cofactor | Binds 1 Fe2+ ion per subunit By similarity. |
| Subunit structure | Monomer. Binds to DNA as a monomer By similarity. |
| Subcellular location | Nucleus By similarity. |
| Domain | The DNA-binding JBP1 domain (DB-JBP1) is necessary and sufficient for binding to J-DNA By similarity. |
| Sequence similarities | Belongs to the TET family. JBP1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Nucleus |
| Ligand | DNA-binding Iron Metal-binding |
| Molecular function | Dioxygenase Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Cellular_component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygenInferred from electronic annotation. Source: UniProtKB-KW thymine dioxygenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 832 | 832 | Thymine dioxygenase JBP1-A | PRO_0000377556 | |||||
Regions | |||||||||
| Region | 80 – 282 | 203 | Thymine dioxygenase By similarity | ||||||
| Region | 409 – 578 | 170 | DNA-binding JBP1 domain By similarity | ||||||
Sites | |||||||||
| Metal binding | 207 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 209 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 257 | 1 | Iron; catalytic By similarity | ||||||
| Binding site | 273 | 1 | 2-oxoglutarate By similarity | ||||||
| Site | 542 | 1 | Involved in J base recognition, conferring specificity towards J-DNA By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease." El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G., Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G., Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B., Anupama A., Arner E., Aslund L. Andersson B.Science 309:409-415(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CL Brener. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AAHK01000683 Genomic DNA. Translation: EAN90000.1. |
| RefSeq | XP_811851.1. XM_806758.1. |
3D structure databases | |
| ProteinModelPortal | Q4DBW3. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3542898. |
| KEGG | tcr:510357.10. |
Phylogenomic databases | |
| ProtClustDB | CLSZ2441100. |
Family and domain databases | |
| InterPro | IPR024779. 2OGFeDO_nucleic_acid_mod. [Graphical view] |
| Pfam | PF12851. Tet_JBP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | JBP1A_TRYCC | ||||||||
| Accession | Primary (citable) accession number: Q4DBW3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
