Reviewed, UniProtKB/Swiss-Prot P06526 (TDT_BOVIN)

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)

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.
Sequence processing	The displayed sequence is not processed.
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.

Ontologies

Keywords
Biological process	Terminal addition
Cellular component	Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA modification Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: InterPro
Cellular component	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 magnesium 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	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

	Sequence		Length	Mass (Da)
	P06526-1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: EE5262617BA5D207	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

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: 3755527] [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: 3579900] [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: 2713339] [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: 3346221] [Abstract] Cited for: PARTIAL 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: 2910867] [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: 6087320] [Abstract] Cited for: PROTEIN SEQUENCE OF 306-326; 337-357 AND 483-506.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
UniGene	Bt.329
3D structure databases
HSSP	HSSP built from PDB template 1JMS based on UniProtKB P09838.
SMR	P06526. Positions 21-125, 148-509.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000020427. Bos taurus. [Contig view]
GeneID	281120.
KEGG	bta:281120.
Phylogenomic databases
HOVERGEN	P06526.
Enzyme and pathway databases
BRENDA	2.7.7.31. 251.
Family and domain databases
InterPro	IPR001357. BRCT. IPR002054. DNA-dir_DNA_pol_X. IPR010996. DNA-dir_DNA_pol_X_beta-like_N. IPR001726. DNA_nucleotidylexotransferase. IPR019843. DNA_pol-X_BS. IPR018944. DNA_pol_lambd_fingers_domain. IPR002934. Nucleotidyltransferase. [Graphical view]
Gene3D	G3DSA:1.10.150.110. DNA_pol_b_N-like. 1 hit.
PANTHER	PTHR11276:SF6. DNA_polXtrans. 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.
PRINTS	PR00869. DNAPOLX. PR00871. DNAPOLXTDT.
SMART	SM00292. BRCT. 1 hit. SM00483. POLXc. 1 hit. [Graphical view]
PROSITE	PS50172. BRCT. 1 hit. PS00522. DNA_POLYMERASE_X. 1 hit. [Graphical view]
ProtoNet	Search...

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:	June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)