P06526 (TDT_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 111.
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: DNA nucleotidylexotransferase EC=2.7.7.31 Alternative name(s): Terminal addition enzyme Terminal deoxynucleotidyltransferase Short name=TDT Short name=Terminal transferase | ||||
| Gene names |
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| Organism | Bos taurus (Bovine) [Reference proteome] | ||||
| Taxonomic identifier | 9913 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 509 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. |
| Catalytic activity | Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). |
| Cofactor | Magnesium. |
| Subunit structure | Interacts with PRP19 and DNTTIP1. Forms a ternary complex with DNTTIP2 and core histone. Released from this complex by PCNA By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the DNA polymerase type-X family. Contains 1 BRCT domain. |
| Sequence caution | The sequence AAA87354.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA27734.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Terminal addition |
| Cellular component | Nucleus |
| Ligand | Magnesium Metal-binding |
| Molecular function | Nucleotidyltransferase Transferase |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | DNA modification Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: Compara nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | DNA binding Inferred from electronic annotation. Source: InterPro DNA nucleotidylexotransferase activityInferred from electronic annotation. Source: UniProtKB-KW DNA-directed DNA polymerase activityInferred from electronic annotation. Source: InterPro metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 509 | 509 | DNA nucleotidylexotransferase | PRO_0000218790 | |||||
Regions | |||||||||
| Domain | 27 – 124 | 98 | BRCT | ||||||
| Region | 151 – 509 | 359 | Mediates interaction with DNTTIP2 By similarity | ||||||
| Region | 336 – 345 | 10 | Involved in ssDNA binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 253 | 1 | Sodium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 255 | 1 | Sodium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 343 | 1 | Magnesium By similarity | ||||||
| Metal binding | 345 | 1 | Magnesium By similarity | ||||||
| Metal binding | 433 | 1 | Magnesium By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and characterization of bovine and mouse terminal deoxynucleotidyltransferase cDNAs expressible in mammalian cells." Koiwai O., Yokota T., Kageyama T., Hirose T., Yoshida S., Arai K. Nucleic Acids Res. 14:5777-5792(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Thymus. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Thymus. |
| [3] | "Analysis of human terminal deoxynucleotidyl transferase cDNA expressible in mammalian cells." Koiwai O., Kaneda T., Morishita R. Biochem. Biophys. Res. Commun. 144:185-190(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-2. |
| [4] | "Photoaffinity labeling of terminal deoxynucleotidyl transferase. 2. Identification of peptides in the nucleotide binding domain." Evans R.K., Beach C.M., Coleman M.S. Biochemistry 28:713-720(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 132-168; 169-176; 183-188; 191-219; 223-334; 336-415 AND 421-509. |
| [5] | "Biochemistry of terminal deoxynucleotidyltransferase. Affinity labeling and identification of the deoxynucleoside triphosphate binding domain of terminal deoxynucleotidyltransferase." Pandey V.N., Modak M.J. J. Biol. Chem. 263:3744-3751(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 210-238. |
| [6] | "Biochemistry of terminal deoxynucleotidyltransferase. Identification and unity of ribo- and deoxyribonucleoside triphosphate binding site in terminal deoxynucleotidyltransferase." Pandey V.N., Modak M.J. J. Biol. Chem. 264:867-871(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 210-221 AND 224-238, ATP- AND DTTP-BINDING SITES CYS-216 AND CYS-224. |
| [7] | "Molecular cloning of human terminal deoxynucleotidyltransferase." Peterson R.C., Cheung L.C., Mattaliano R.J., Chang L.M.S., Bollum F.J. Proc. Natl. Acad. Sci. U.S.A. 81:4363-4367(1984) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 306-326; 337-357 AND 483-506. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X04122 mRNA. Translation: CAA27734.1. Different initiation. BC114820 mRNA. Translation: AAI14821.1. M26146 mRNA. Translation: AAA87354.1. Different initiation. |
| IPI | IPI00709217. |
| PIR | A23595. |
| RefSeq | NP_803461.1. NM_177495.2. |
| UniGene | Bt.329. |
3D structure databases | |
| ProteinModelPortal | P06526. |
| SMR | P06526. Positions 21-125, 148-509. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P06526. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000027223; ENSBTAP00000027223; ENSBTAG00000020427. ENSBTAT00000052753; ENSBTAP00000051460; ENSBTAG00000020427. |
| GeneID | 281120. |
| KEGG | bta:281120. |
Organism-specific databases | |
| CTD | 1791. |
Phylogenomic databases | |
| eggNOG | COG1796. |
| GeneTree | ENSGT00530000063002. |
| HOGENOM | HOG000263600. |
| HOVERGEN | HBG003670. |
| InParanoid | P06526. |
| KO | K00977. |
| OrthoDB | EOG4SQWWN. |
Family and domain databases | |
| InterPro | IPR001357. BRCT_dom. IPR002054. DNA-dir_DNA_pol_X. IPR019843. DNA_pol-X_BS. IPR010996. DNA_pol_b-like_N. IPR018944. DNA_pol_lambd_fingers_domain. IPR022312. DNA_pol_X. IPR002934. Nucleotidyltransferase. IPR027292. TdT. IPR001726. TdT/Mu. [Graphical view] |
| PANTHER | PTHR11276:SF6. PTHR11276:SF6. 1 hit. |
| Pfam | PF00533. BRCT. 1 hit. PF10391. DNA_pol_lambd_f. 1 hit. PF01909. NTP_transf_2. 1 hit. [Graphical view] |
| PIRSF | PIRSF000817. DNA_NT. 1 hit. PIRSF501175. TDT. 1 hit. |
| PRINTS | PR00869. DNAPOLX. PR00871. DNAPOLXTDT. |
| SMART | SM00292. BRCT. 1 hit. SM00483. POLXc. 1 hit. [Graphical view] |
| SUPFAM | SSF52113. BRCT. 1 hit. SSF81585. DNA_pol_lambd_fingers_domain. 1 hit. SSF47802. DNApol_B_N_like. 1 hit. |
| PROSITE | PS50172. BRCT. 1 hit. PS00522. DNA_POLYMERASE_X. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| BindingDB | P06526. |
| ChEMBL | CHEMBL5289. |
| NextBio | 20805189. |
Entry information
| Entry name | TDT_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P06526 Secondary accession number(s): A4FUF8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
