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Protein

DNA nucleotidylexotransferase

Gene

Dntt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator (PubMed:23856622). 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.Curated1 Publication

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).2 Publications

Cofactori

Mg2+1 PublicationNote: Can also utilize other divalent cations, such as Mn2+ and Co2+ (in vitro).Curated1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi343MagnesiumCombined sourcesCurated1
Metal bindingi345MagnesiumCombined sourcesCurated1
Metal bindingi434MagnesiumCombined sourcesCurated1

GO - Molecular functioni

GO - Biological processi

  • DNA metabolic process Source: MGI
  • DNA modification Source: UniProtKB-KW
  • response to ATP Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Terminal addition

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi2.7.7.31. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA nucleotidylexotransferase (EC:2.7.7.312 Publications)
Alternative name(s):
Terminal addition enzyme
Terminal deoxynucleotidyltransferase1 Publication
Short name:
TDT
Short name:
Terminal transferase
Gene namesi
Name:Dntt
Synonyms:Tdt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:98659. Dntt.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi342H → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi398L → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi399D → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi400H → A: Reduces enzyme activity. 1 Publication1
Mutagenesisi403K → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi473D → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi475H → A: Nearly abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002187921 – 530DNA nucleotidylexotransferaseAdd BLAST530

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei134PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP09838.
PaxDbiP09838.
PRIDEiP09838.

PTM databases

iPTMnetiP09838.
PhosphoSitePlusiP09838.

Expressioni

Gene expression databases

BgeeiENSMUSG00000025014.
CleanExiMM_DNTT.
ExpressionAtlasiP09838. baseline and differential.
GenevisibleiP09838. MM.

Interactioni

Subunit structurei

Interacts with PRP19 and DNTTIP1. Forms a ternary complex with DNTTIP2 and core histone. Released from this complex by PCNA. Interacts with TRERF1.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000062078.

Structurei

Secondary structure

1530
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi154 – 156Combined sources3
Helixi166 – 181Combined sources16
Helixi185 – 199Combined sources15
Helixi208 – 211Combined sources4
Helixi219 – 231Combined sources13
Helixi235 – 242Combined sources8
Helixi244 – 253Combined sources10
Helixi260 – 268Combined sources9
Helixi274 – 279Combined sources6
Helixi287 – 294Combined sources8
Helixi296 – 300Combined sources5
Helixi305 – 322Combined sources18
Beta strandi327 – 330Combined sources4
Helixi332 – 335Combined sources4
Beta strandi339 – 342Combined sources4
Beta strandi344 – 349Combined sources6
Helixi355 – 372Combined sources18
Beta strandi375 – 381Combined sources7
Helixi387 – 389Combined sources3
Beta strandi394 – 396Combined sources3
Beta strandi401 – 411Combined sources11
Helixi412 – 414Combined sources3
Beta strandi425 – 437Combined sources13
Helixi440 – 442Combined sources3
Helixi443 – 451Combined sources9
Helixi454 – 468Combined sources15
Beta strandi470 – 472Combined sources3
Beta strandi477 – 479Combined sources3
Turni480 – 482Combined sources3
Beta strandi504 – 506Combined sources3
Helixi511 – 518Combined sources8
Helixi525 – 527Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JMSX-ray2.36A130-530[»]
1KDHX-ray3.00A148-530[»]
1KEJX-ray3.00A148-530[»]
4I27X-ray2.60A132-530[»]
4I28X-ray2.15A132-530[»]
4I29X-ray2.20A132-530[»]
4I2AX-ray1.90A132-530[»]
4I2BX-ray2.20A132-530[»]
4I2CX-ray2.10A132-530[»]
4I2DX-ray2.30A132-530[»]
4I2EX-ray2.00A132-530[»]
4I2FX-ray2.10A132-530[»]
4I2GX-ray2.50A132-530[»]
4I2HX-ray2.75A132-530[»]
4I2IX-ray2.50A132-530[»]
4I2JX-ray2.70A132-530[»]
4IQTX-ray2.60A132-530[»]
4IQUX-ray2.40A132-530[»]
4IQVX-ray2.90A132-530[»]
4IQWX-ray2.60A132-530[»]
4QZ8X-ray2.70A132-530[»]
4QZ9X-ray2.05A132-530[»]
4QZAX-ray2.15A132-530[»]
4QZBX-ray2.15A132-530[»]
4QZCX-ray2.75A132-530[»]
4QZDX-ray2.70A132-530[»]
4QZEX-ray2.25A132-530[»]
4QZFX-ray2.60A132-530[»]
4QZGX-ray2.75A132-530[»]
4QZHX-ray2.60A132-530[»]
4QZIX-ray2.65A132-530[»]
5D46X-ray2.80A132-530[»]
5D49X-ray1.99A132-530[»]
5D4BX-ray2.66A/B132-530[»]
ProteinModelPortaliP09838.
SMRiP09838.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09838.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 124BRCTPROSITE-ProRule annotationAdd BLAST98

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni151 – 530Mediates interaction with DNTTIP2By similarityAdd BLAST380
Regioni258 – 262Involved in DNA binding2 Publications5
Regioni333 – 338Deoxynucleoside triphosphate bindingCombined sourcesCurated6
Regioni342 – 345Deoxynucleoside triphosphate bindingCombined sourcesCurated4
Regioni449 – 450Deoxynucleoside triphosphate bindingCombined sourcesCurated2

Sequence similaritiesi

Belongs to the DNA polymerase type-X family.Curated
Contains 1 BRCT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2534. Eukaryota.
COG1796. LUCA.
GeneTreeiENSGT00530000063002.
HOGENOMiHOG000263600.
HOVERGENiHBG003670.
InParanoidiP09838.
KOiK00977.
OMAiKTWKAIR.
OrthoDBiEOG091G073W.
PhylomeDBiP09838.
TreeFamiTF103012.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
cd00141. NT_POLXc. 1 hit.
Gene3Di1.10.150.110. 1 hit.
3.30.210.10. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR002054. DNA-dir_DNA_pol_X.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR028207. DNA_pol_B_palm_palm.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR027421. DNA_pol_X_lyase_dom.
IPR029398. PolB_thumb.
IPR027292. TdT.
IPR001726. TdT/Mu.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF14792. DNA_pol_B_palm. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
PF14716. HHH_8. 1 hit.
[Graphical view]
PIRSFiPIRSF000817. DNA_NT. 1 hit.
PIRSF501175. TDT. 1 hit.
PRINTSiPR00869. DNAPOLX.
PR00871. DNAPOLXTDT.
SMARTiSM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]
SUPFAMiSSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform TDT-L (identifier: P09838-1) [UniParc]FASTAAdd to basket
Also known as: TDT-Large, TdtL

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDPLQAVHLG PRKKRPRQLG TPVASTPYDI RFRDLVLFIL EKKMGTTRRA
60 70 80 90 100
FLMELARRKG FRVENELSDS VTHIVAENNS GSDVLEWLQL QNIKASSELE
110 120 130 140 150
LLDISWLIEC MGAGKPVEMM GRHQLVVNRN SSPSPVPGSQ NVPAPAVKKI
160 170 180 190 200
SQYACQRRTT LNNYNQLFTD ALDILAENDE LRENEGSCLA FMRASSVLKS
210 220 230 240 250
LPFPITSMKD TEGIPCLGDK VKSIIEGIIE DGESSEAKAV LNDERYKSFK
260 270 280 290 300
LFTSVFGVGL KTAEKWFRMG FRTLSKIQSD KSLRFTQMQK AGFLYYEDLV
310 320 330 340 350
SCVNRPEAEA VSMLVKEAVV TFLPDALVTM TGGFRRGKMT GHDVDFLITS
360 370 380 390 400
PEATEDEEQQ LLHKVTDFWK QQGLLLYCDI LESTFEKFKQ PSRKVDALDH
410 420 430 440 450
FQKCFLILKL DHGRVHSEKS GQQEGKGWKA IRVDLVMCPY DRRAFALLGW
460 470 480 490 500
TGSRQFERDL RRYATHERKM MLDNHALYDR TKGKTVTISP LDGKVSKLQK
510 520 530
ALRVFLEAES EEEIFAHLGL DYIEPWERNA
Note: Inactivated at physiological temperature but is stable at lower temperatures.
Length:530
Mass (Da):60,331
Last modified:November 16, 2001 - v3
Checksum:iE6B109DCF39C8107
GO
Isoform TDT-S (identifier: P09838-2) [UniParc]FASTAAdd to basket
Also known as: TDT-Small, TdtS

The sequence of this isoform differs from the canonical sequence as follows:
     483-502: Missing.

Note: Major form.
Show »
Length:510
Mass (Da):58,266
Checksum:iCF6E850EE36EE3BF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti26T → M in CAA48634 (PubMed:8464703).Curated1
Sequence conflicti99L → F in CAA48634 (PubMed:8464703).Curated1
Sequence conflicti193R → G in CAA27735 (PubMed:3755527).Curated1
Sequence conflicti287Q → K in CAA27735 (PubMed:3755527).Curated1
Sequence conflicti309E → Q in CAA27735 (PubMed:3755527).Curated1
Sequence conflicti367D → H in CAA27735 (PubMed:3755527).Curated1
Sequence conflicti441 – 445DRRAF → ECAC in CAA27735 (PubMed:3755527).Curated5

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001309483 – 502Missing in isoform TDT-S. 1 PublicationAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04123 mRNA. Translation: CAA27735.1.
X68670 mRNA. Translation: CAA48634.2.
AF316014 mRNA. Translation: AAK07884.1.
AF316015 mRNA. Translation: AAK07885.1.
AK087978 mRNA. Translation: BAC40071.1.
AK088709 mRNA. Translation: BAC40518.1.
CCDSiCCDS29807.1. [P09838-1]
CCDS37984.1. [P09838-2]
PIRiB23595.
RefSeqiNP_001036693.1. NM_001043228.1. [P09838-2]
NP_033371.2. NM_009345.2. [P09838-1]
UniGeneiMm.25620.

Genome annotation databases

EnsembliENSMUST00000051806; ENSMUSP00000062078; ENSMUSG00000025014. [P09838-1]
ENSMUST00000112200; ENSMUSP00000107819; ENSMUSG00000025014. [P09838-2]
GeneIDi21673.
KEGGimmu:21673.
UCSCiuc008hlo.1. mouse. [P09838-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04123 mRNA. Translation: CAA27735.1.
X68670 mRNA. Translation: CAA48634.2.
AF316014 mRNA. Translation: AAK07884.1.
AF316015 mRNA. Translation: AAK07885.1.
AK087978 mRNA. Translation: BAC40071.1.
AK088709 mRNA. Translation: BAC40518.1.
CCDSiCCDS29807.1. [P09838-1]
CCDS37984.1. [P09838-2]
PIRiB23595.
RefSeqiNP_001036693.1. NM_001043228.1. [P09838-2]
NP_033371.2. NM_009345.2. [P09838-1]
UniGeneiMm.25620.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JMSX-ray2.36A130-530[»]
1KDHX-ray3.00A148-530[»]
1KEJX-ray3.00A148-530[»]
4I27X-ray2.60A132-530[»]
4I28X-ray2.15A132-530[»]
4I29X-ray2.20A132-530[»]
4I2AX-ray1.90A132-530[»]
4I2BX-ray2.20A132-530[»]
4I2CX-ray2.10A132-530[»]
4I2DX-ray2.30A132-530[»]
4I2EX-ray2.00A132-530[»]
4I2FX-ray2.10A132-530[»]
4I2GX-ray2.50A132-530[»]
4I2HX-ray2.75A132-530[»]
4I2IX-ray2.50A132-530[»]
4I2JX-ray2.70A132-530[»]
4IQTX-ray2.60A132-530[»]
4IQUX-ray2.40A132-530[»]
4IQVX-ray2.90A132-530[»]
4IQWX-ray2.60A132-530[»]
4QZ8X-ray2.70A132-530[»]
4QZ9X-ray2.05A132-530[»]
4QZAX-ray2.15A132-530[»]
4QZBX-ray2.15A132-530[»]
4QZCX-ray2.75A132-530[»]
4QZDX-ray2.70A132-530[»]
4QZEX-ray2.25A132-530[»]
4QZFX-ray2.60A132-530[»]
4QZGX-ray2.75A132-530[»]
4QZHX-ray2.60A132-530[»]
4QZIX-ray2.65A132-530[»]
5D46X-ray2.80A132-530[»]
5D49X-ray1.99A132-530[»]
5D4BX-ray2.66A/B132-530[»]
ProteinModelPortaliP09838.
SMRiP09838.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000062078.

PTM databases

iPTMnetiP09838.
PhosphoSitePlusiP09838.

Proteomic databases

MaxQBiP09838.
PaxDbiP09838.
PRIDEiP09838.

Protocols and materials databases

DNASUi21673.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000051806; ENSMUSP00000062078; ENSMUSG00000025014. [P09838-1]
ENSMUST00000112200; ENSMUSP00000107819; ENSMUSG00000025014. [P09838-2]
GeneIDi21673.
KEGGimmu:21673.
UCSCiuc008hlo.1. mouse. [P09838-1]

Organism-specific databases

CTDi1791.
MGIiMGI:98659. Dntt.

Phylogenomic databases

eggNOGiKOG2534. Eukaryota.
COG1796. LUCA.
GeneTreeiENSGT00530000063002.
HOGENOMiHOG000263600.
HOVERGENiHBG003670.
InParanoidiP09838.
KOiK00977.
OMAiKTWKAIR.
OrthoDBiEOG091G073W.
PhylomeDBiP09838.
TreeFamiTF103012.

Enzyme and pathway databases

BRENDAi2.7.7.31. 3474.

Miscellaneous databases

EvolutionaryTraceiP09838.
PROiP09838.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025014.
CleanExiMM_DNTT.
ExpressionAtlasiP09838. baseline and differential.
GenevisibleiP09838. MM.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
cd00141. NT_POLXc. 1 hit.
Gene3Di1.10.150.110. 1 hit.
3.30.210.10. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR002054. DNA-dir_DNA_pol_X.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR028207. DNA_pol_B_palm_palm.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR027421. DNA_pol_X_lyase_dom.
IPR029398. PolB_thumb.
IPR027292. TdT.
IPR001726. TdT/Mu.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF14792. DNA_pol_B_palm. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
PF14716. HHH_8. 1 hit.
[Graphical view]
PIRSFiPIRSF000817. DNA_NT. 1 hit.
PIRSF501175. TDT. 1 hit.
PRINTSiPR00869. DNAPOLX.
PR00871. DNAPOLXTDT.
SMARTiSM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]
SUPFAMiSSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTDT_MOUSE
AccessioniPrimary (citable) accession number: P09838
Secondary accession number(s): Q99PD0, Q99PD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 16, 2001
Last modified: November 30, 2016
This is version 172 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.