DNA nucleotidylexotransferase - Bos taurus (Bovine)

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P06526 (TDT_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names 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

Name:	DNTT
Synonyms:	TDT

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	Nucleus.
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 nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA nucleotidylexotransferase activity Inferred from electronic annotation. Source: UniProtKB-KW DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred 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

BRCT

Region

151 – 509

359

Mediates interaction with DNTTIP2 By similarity

Region

336 – 345

Involved in ssDNA binding By similarity

Sites

Metal binding

253

Sodium; via carbonyl oxygen By similarity

Metal binding

255

Sodium; via carbonyl oxygen By similarity

Metal binding

343

Magnesium By similarity

Metal binding

345

Magnesium By similarity

Metal binding

433

Magnesium By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P06526 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: EE5262617BA5D207
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FASTA

509

58,296

        10         20         30         40         50         60 
MDPLCTASSG PRKKRPRQVG ASMASPPHDI KFQNLVLFIL EKKMGTTRRN FLMELARRKG 

        70         80         90        100        110        120 
FRVENELSDS VTHIVAENNS GSEVLEWLQV QNIRASSQLE LLDVSWLIES MGAGKPVEIT 

       130        140        150        160        170        180 
GKHQLVVRTD YSATPNPGFQ KTPPLAVKKI SQYACQRKTT LNNYNHIFTD AFEILAENSE 

       190        200        210        220        230        240 
FKENEVSYVT FMRAASVLKS LPFTIISMKD TEGIPCLGDK VKCIIEEIIE DGESSEVKAV 

       250        260        270        280        290        300 
LNDERYQSFK LFTSVFGVGL KTSEKWFRMG FRSLSKIMSD KTLKFTKMQK AGFLYYEDLV 

       310        320        330        340        350        360 
SCVTRAEAEA VGVLVKEAVW AFLPDAFVTM TGGFRRGKKI GHDVDFLITS PGSAEDEEQL 

       370        380        390        400        410        420 
LPKVINLWEK KGLLLYYDLV ESTFEKFKLP SRQVDTLDHF QKCFLILKLH HQRVDSSKSN 

       430        440        450        460        470        480 
QQEGKTWKAI RVDLVMCPYE NRAFALLGWT GSRQFERDIR RYATHERKMM LDNHALYDKT 

       490        500 
KRVFLKAESE EEIFAHLGLD YIEPWERNA

« Hide

References

	« Hide 'large scale' referencesShow '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

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents