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Protein

DNA nucleotidylexotransferase

Gene

DNTT

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 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. 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.By similarity

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).By similarity

Cofactori

Mg2+By similarityNote: Can also utilize other divalent cations, such as Mn2+ and Co2+ (in vitro).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi343 – 3431MagnesiumBy similarity
Metal bindingi345 – 3451MagnesiumBy similarity
Metal bindingi433 – 4331MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

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. 908.

Names & Taxonomyi

Protein namesi
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 namesi
Name:DNTT
Synonyms:TDT
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 26

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5289.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 509509DNA nucleotidylexotransferasePRO_0000218790Add
BLAST

Proteomic databases

PaxDbiP06526.
PRIDEiP06526.

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

BioGridi158482. 1 interaction.
STRINGi9913.ENSBTAP00000051460.

Chemistry

BindingDBiP06526.

Structurei

3D structure databases

ProteinModelPortaliP06526.
SMRiP06526. Positions 21-125, 148-509.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 12498BRCTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni151 – 509359Mediates interaction with DNTTIP2By similarityAdd
BLAST
Regioni258 – 2625Involved in DNA bindingBy similarity
Regioni333 – 3386Deoxynucleoside triphosphate bindingBy similarity
Regioni342 – 3454Deoxynucleoside triphosphate bindingBy similarity
Regioni448 – 4492Deoxynucleoside triphosphate bindingBy similarity

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.
InParanoidiP06526.
KOiK00977.
OrthoDBiEOG7BS4BH.
TreeFamiTF103012.

Family and domain databases

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]

Sequencei

Sequence statusi: Complete.

P06526-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPLCTASSG PRKKRPRQVG ASMASPPHDI KFQNLVLFIL EKKMGTTRRN
60 70 80 90 100
FLMELARRKG FRVENELSDS VTHIVAENNS GSEVLEWLQV QNIRASSQLE
110 120 130 140 150
LLDVSWLIES MGAGKPVEIT GKHQLVVRTD YSATPNPGFQ KTPPLAVKKI
160 170 180 190 200
SQYACQRKTT LNNYNHIFTD AFEILAENSE FKENEVSYVT FMRAASVLKS
210 220 230 240 250
LPFTIISMKD TEGIPCLGDK VKCIIEEIIE DGESSEVKAV LNDERYQSFK
260 270 280 290 300
LFTSVFGVGL KTSEKWFRMG FRSLSKIMSD KTLKFTKMQK AGFLYYEDLV
310 320 330 340 350
SCVTRAEAEA VGVLVKEAVW AFLPDAFVTM TGGFRRGKKI GHDVDFLITS
360 370 380 390 400
PGSAEDEEQL LPKVINLWEK KGLLLYYDLV ESTFEKFKLP SRQVDTLDHF
410 420 430 440 450
QKCFLILKLH HQRVDSSKSN QQEGKTWKAI RVDLVMCPYE NRAFALLGWT
460 470 480 490 500
GSRQFERDIR RYATHERKMM LDNHALYDKT KRVFLKAESE EEIFAHLGLD

YIEPWERNA
Length:509
Mass (Da):58,296
Last modified:May 1, 2007 - v2
Checksum:iEE5262617BA5D207
GO

Sequence cautioni

The sequence AAA87354.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA27734.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04122 mRNA. Translation: CAA27734.1. Different initiation.
BC114820 mRNA. Translation: AAI14821.1.
M26146 mRNA. Translation: AAA87354.1. Different initiation.
PIRiA23595.
RefSeqiNP_803461.1. NM_177495.2.
XP_005225486.1. XM_005225429.2.
UniGeneiBt.329.

Genome annotation databases

EnsembliENSBTAT00000027223; ENSBTAP00000027223; ENSBTAG00000020427.
GeneIDi281120.
KEGGibta:281120.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04122 mRNA. Translation: CAA27734.1. Different initiation.
BC114820 mRNA. Translation: AAI14821.1.
M26146 mRNA. Translation: AAA87354.1. Different initiation.
PIRiA23595.
RefSeqiNP_803461.1. NM_177495.2.
XP_005225486.1. XM_005225429.2.
UniGeneiBt.329.

3D structure databases

ProteinModelPortaliP06526.
SMRiP06526. Positions 21-125, 148-509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi158482. 1 interaction.
STRINGi9913.ENSBTAP00000051460.

Chemistry

BindingDBiP06526.
ChEMBLiCHEMBL5289.

Proteomic databases

PaxDbiP06526.
PRIDEiP06526.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000027223; ENSBTAP00000027223; ENSBTAG00000020427.
GeneIDi281120.
KEGGibta:281120.

Organism-specific databases

CTDi1791.

Phylogenomic databases

eggNOGiKOG2534. Eukaryota.
COG1796. LUCA.
GeneTreeiENSGT00530000063002.
HOGENOMiHOG000263600.
HOVERGENiHBG003670.
InParanoidiP06526.
KOiK00977.
OrthoDBiEOG7BS4BH.
TreeFamiTF103012.

Enzyme and pathway databases

BRENDAi2.7.7.31. 908.

Miscellaneous databases

PROiP06526.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: PROTEIN SEQUENCE OF 306-326; 337-357 AND 483-506.

Entry informationi

Entry nameiTDT_BOVIN
AccessioniPrimary (citable) accession number: P06526
Secondary accession number(s): A4FUF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: May 1, 2007
Last modified: June 8, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.