ID TDT_MOUSE Reviewed; 510 AA. AC P09838; Q99PD0; Q99PD1; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2018, sequence version 4. DT 05-DEC-2018, entry version 183. DE RecName: Full=DNA nucleotidylexotransferase; DE EC=2.7.7.31 {ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:23856622, ECO:0000269|PubMed:23968551}; DE EC=3.1.11.- {ECO:0000269|PubMed:11938351}; DE AltName: Full=Terminal addition enzyme; DE AltName: Full=Terminal deoxynucleotidyltransferase {ECO:0000303|PubMed:3755527}; DE Short=TDT; DE Short=Terminal transferase; GN Name=Dntt; Synonyms=Tdt; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TDT-L). RC TISSUE=Lymphoma; RX PubMed=3755527; DOI=10.1093/nar/14.14.5777; RA Koiwai O., Yokota T., Kageyama T., Hirose T., Yoshida S., Arai K.; RT "Isolation and characterization of bovine and mouse terminal RT deoxynucleotidyltransferase cDNAs expressible in mammalian cells."; RL Nucleic Acids Res. 14:5777-5792(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TDT-S), FUNCTION, ALTERNATIVE RP SPLICING, AND TISSUE SPECIFICITY. RC STRAIN=BALB/cJ; TISSUE=Thymus; RX PubMed=8464703; DOI=10.1093/nar/21.5.1187; RA Doyen N., Fanton D'Andon M., Bentolila L.A., Nguyen T.Q., Rougeon F.; RT "Differential splicing in mouse thymus generates two forms of terminal RT deoxynucleotidyl transferase."; RL Nucleic Acids Res. 21:1187-1191(1993). RN [3] RP SEQUENCE REVISION TO 443-445. RA Doyen N.; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TDT-L AND TDT-S), FUNCTION, AND RP TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; TISSUE=Thymus; RX PubMed=11136823; DOI=10.1084/jem.193.1.89; RA Benedict C.L., Gilfillan S., Kearney J.F.; RT "The long isoform of terminal deoxynucleotidyl transferase (TdtL) RT enters the nucleus and, rather than catalyzing N addition, modulates RT the catalytic activity of the short isoform."; RL J. Exp. Med. 193:89-99(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TDT-L). RC STRAIN=NOD; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP PROTEIN SEQUENCE OF 388-393, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [7] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ALTERNATIVE RP SPLICING. RX PubMed=7556063; RA Bentolila L.A., Fanton D'Andon M., Nguyen T.Q., Martinez O., RA Rougeon F., Doyen N.; RT "The two isoforms of mouse terminal deoxynucleotidyl transferase RT differ in both the ability to add N regions and subcellular RT localization."; RL EMBO J. 14:4221-4229(1995). RN [8] RP FUNCTION, ALTERNATIVE SPLICING, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10878023; DOI=10.1074/jbc.M005544200; RA Boule J.-B., Rougeon F., Papanicolaou C.; RT "Comparison of the two murine terminal deoxynucleotidyltransferase RT isoforms. A 20-amino acid insertion in the highly conserved carboxyl- RT terminal region modifies the thermosensitivity but not the catalytic RT activity."; RL J. Biol. Chem. 275:28984-28988(2000). RN [9] RP ERRATUM. RX PubMed=11032847; RA Boule J.-B., Rougeon F., Papanicolaou C.; RL J. Biol. Chem. 275:33184-33184(2000). RN [10] RP FUNCTION, TISSUE SPECIFICITY, CHARACTERIZATION OF ISOFORMS TDT-L AND RP TDT-S, AND MUTAGENESIS OF ASP-29; ASP-170 AND ASP-473. RX PubMed=11938351; DOI=10.1038/ni788; RA Thai T.H., Purugganan M.M., Roth D.B., Kearney J.F.; RT "Distinct and opposite diversifying activities of terminal transferase RT splice variants."; RL Nat. Immunol. 3:457-462(2002). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Lung; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 130-510 (ISOFORM TDT-S) IN RP COMPLEXES WITH MAGNESIUM; COBALT AND ATP ANALOG. RX PubMed=11823435; DOI=10.1093/emboj/21.3.427; RA Delarue M., Boule J.-B., Lescar J., Expert-Bezancon N., Jourdan N., RA Sukumar N., Rougeon F., Papanicolaou C.; RT "Crystal structures of a template-independent DNA polymerase: murine RT terminal deoxynucleotidyltransferase."; RL EMBO J. 21:427-439(2002). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 132-510 (ISOFORM TDT-S) IN RP COMPLEXES WITH SYNTHETIC INHIBITORS AND NUCLEOTIDE, AND CATALYTIC RP ACTIVITY. RX PubMed=23968551; DOI=10.1021/jm4010187; RA Costi R., Crucitti G.C., Pescatori L., Messore A., Scipione L., RA Tortorella S., Amoroso A., Crespan E., Campiglia P., Maresca B., RA Porta A., Granata I., Novellino E., Gouge J., Delarue M., Maga G., RA Di Santo R.; RT "New nucleotide-competitive non-nucleoside inhibitors of terminal RT deoxynucleotidyl transferase: discovery, characterization, and crystal RT structure in complex with the target."; RL J. Med. Chem. 56:7431-7441(2013). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 132-510 (ISOFORM TDT-S) IN RP COMPLEXES WITH ATP; CTP; TTP; NUCLEOTIDE; MAGNESIUM; MANGANESE AND RP ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF RP HIS-342; LEU-398; ASP-399; HIS-400; LYS-403; ASP-473 AND HIS-475. RX PubMed=23856622; DOI=10.1016/j.jmb.2013.07.009; RA Gouge J., Rosario S., Romain F., Beguin P., Delarue M.; RT "Structures of intermediates along the catalytic cycle of terminal RT deoxynucleotidyltransferase: dynamical aspects of the two-metal ion RT mechanism."; RL J. Mol. Biol. 425:4334-4352(2013). CC -!- FUNCTION: Isoform TDT-S: Transferase that catalyzes the CC nontemplated addition of nucleoside triphosphate to coding ends CC during V(D)J recombination (N addition). Involved in the CC generation of diversity in the antigen-binding region of CC immunoglobulin heavy and light chains and T-cell receptors during CC B-and T-cell development. Does not act on double-stranded DNA with CC blunt ends. {ECO:0000269|PubMed:11136823, CC ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:23856622, CC ECO:0000269|PubMed:7556063, ECO:0000269|PubMed:8464703}. CC -!- FUNCTION: Isoform TDT-L: 3'-to-5' DNA exonuclease. Involved in the CC generation of diversity in the antigen-binding region of CC immunoglobulin heavy and light chains and T-cell receptors during CC B-and T-cell development. Acts on single-stranded and double- CC stranded DNA with 3' or 5' extensions, but not on double-stranded CC DNA with blunt ends. Attenuates not only isoform TDT-S-catalyzed N CC addition, but also P (palindromic) addition in coding joins CC (PubMed:11938351). Lacks terminal transferase activity CC (PubMed:11136823, PubMed:7556063). {ECO:0000269|PubMed:11136823, CC ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:7556063}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA- CC COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.31; CC Evidence={ECO:0000269|PubMed:23856622, CC ECO:0000269|PubMed:23968551}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:23856622}; CC Note=Can also utilize other divalent cations, such as Mn(2+) and CC Co(2+) (in vitro). {ECO:0000269|PubMed:23856622, ECO:0000305}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=300 uM for dATP (at 35 degrees Celsius) CC {ECO:0000269|PubMed:10878023}; CC Note=In assays with isoform TDT-S. CC {ECO:0000269|PubMed:10878023}; CC -!- SUBUNIT: Interacts with PRP19 and DNTTIP1. Forms a ternary complex CC with DNTTIP2 and core histone. Released from this complex by PCNA. CC Interacts with TRERF1. {ECO:0000250|UniProtKB:P04053}. CC -!- SUBCELLULAR LOCATION: Isoform TDT-S: Nucleus CC {ECO:0000269|PubMed:7556063}. CC -!- SUBCELLULAR LOCATION: Isoform TDT-L: Nucleus CC {ECO:0000269|PubMed:11136823}. Cytoplasm CC {ECO:0000269|PubMed:7556063}. Note=The subcellular location is CC controversial. Detected in the nucleus (PubMed:11136823). Found CC mainly in the cytoplasm (PubMed:7556063). CC {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:7556063}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=TDT-S; Synonyms=TDT-Small, TdtS {ECO:0000303|PubMed:8464703}; CC IsoId=P09838-2; Sequence=Displayed; CC Note=Major form in the thymus and the bone marrow (Ref.2, CC Ref.4). Catalyzes the nontemplated addition of nucleoside CC triphosphate to coding ends during V(D)J recombination (Ref.14). CC May have a longer half-life than isoform TDT-L (Ref.7). CC {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:11938351, CC ECO:0000269|PubMed:7556063, ECO:0000269|PubMed:8464703}; CC Name=TDT-L; Synonyms=TDT-Large, TdtL {ECO:0000303|PubMed:8464703}; CC IsoId=P09838-1; Sequence=VSP_059967; CC Note=Exhibits 3'-to-5' DNA exonuclease activity (EC=3.1.11.-) CC (Ref.14). May have a shorter half-life than isoform TDT-S CC (Ref.7, Ref.8). {ECO:0000269|PubMed:10878023, CC ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:7556063}; CC -!- TISSUE SPECIFICITY: Isoform TDT-L: Expressed in the thymus, and, CC at lower levels, in the bone marrow (PubMed:8464703, CC PubMed:11136823, PubMed:7556063). Detected in both cycling and CC noncycling pro-B and pre-B cells (at protein level) CC (PubMed:11938351). Isoform TDT-S: Expressed in both cycling and CC noncycling pro-B, but not pre-B, cells (at protein level) CC (PubMed:11938351). Not detected in mature peripheral or germinal CC center B cells (PubMed:11938351). {ECO:0000269|PubMed:11136823, CC ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:7556063, CC ECO:0000269|PubMed:8464703}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04123; CAA27735.1; -; mRNA. DR EMBL; X68670; CAA48634.2; -; mRNA. DR EMBL; AF316014; AAK07884.1; -; mRNA. DR EMBL; AF316015; AAK07885.1; -; mRNA. DR EMBL; AK087978; BAC40071.1; -; mRNA. DR EMBL; AK088709; BAC40518.1; -; mRNA. DR CCDS; CCDS29807.1; -. [P09838-1] DR CCDS; CCDS37984.1; -. [P09838-2] DR PIR; B23595; B23595. DR RefSeq; NP_001036693.1; NM_001043228.1. [P09838-2] DR RefSeq; NP_033371.2; NM_009345.2. [P09838-1] DR UniGene; Mm.25620; -. DR PDB; 1JMS; X-ray; 2.36 A; A=130-510. DR PDB; 1KDH; X-ray; 3.00 A; A=148-510. DR PDB; 1KEJ; X-ray; 3.00 A; A=148-510. DR PDB; 4I27; X-ray; 2.60 A; A=132-510. DR PDB; 4I28; X-ray; 2.15 A; A=132-510. DR PDB; 4I29; X-ray; 2.20 A; A=132-510. DR PDB; 4I2A; X-ray; 1.90 A; A=132-510. DR PDB; 4I2B; X-ray; 2.20 A; A=132-510. DR PDB; 4I2C; X-ray; 2.10 A; A=132-510. DR PDB; 4I2D; X-ray; 2.30 A; A=132-510. DR PDB; 4I2E; X-ray; 2.00 A; A=132-510. DR PDB; 4I2F; X-ray; 2.10 A; A=132-510. DR PDB; 4I2G; X-ray; 2.50 A; A=132-510. DR PDB; 4I2H; X-ray; 2.75 A; A=132-510. DR PDB; 4I2I; X-ray; 2.50 A; A=132-510. DR PDB; 4I2J; X-ray; 2.70 A; A=132-510. DR PDB; 4IQT; X-ray; 2.60 A; A=132-510. DR PDB; 4IQU; X-ray; 2.40 A; A=132-510. DR PDB; 4IQV; X-ray; 2.90 A; A=132-510. DR PDB; 4IQW; X-ray; 2.60 A; A=132-510. DR PDB; 4QZ8; X-ray; 2.70 A; A=132-510. DR PDB; 4QZ9; X-ray; 2.05 A; A=132-510. DR PDB; 4QZA; X-ray; 2.15 A; A=132-510. DR PDB; 4QZB; X-ray; 2.15 A; A=132-510. DR PDB; 4QZC; X-ray; 2.75 A; A=132-510. DR PDB; 4QZD; X-ray; 2.70 A; A=132-510. DR PDB; 4QZE; X-ray; 2.25 A; A=132-510. DR PDB; 4QZF; X-ray; 2.60 A; A=132-510. DR PDB; 4QZG; X-ray; 2.75 A; A=132-510. DR PDB; 4QZH; X-ray; 2.60 A; A=132-510. DR PDB; 4QZI; X-ray; 2.65 A; A=132-510. DR PDB; 5D46; X-ray; 2.80 A; A=132-510. DR PDB; 5D49; X-ray; 1.99 A; A=132-510. DR PDB; 5D4B; X-ray; 2.66 A; A/B=132-510. DR PDBsum; 1JMS; -. DR PDBsum; 1KDH; -. DR PDBsum; 1KEJ; -. DR PDBsum; 4I27; -. DR PDBsum; 4I28; -. DR PDBsum; 4I29; -. DR PDBsum; 4I2A; -. DR PDBsum; 4I2B; -. DR PDBsum; 4I2C; -. DR PDBsum; 4I2D; -. DR PDBsum; 4I2E; -. DR PDBsum; 4I2F; -. DR PDBsum; 4I2G; -. DR PDBsum; 4I2H; -. DR PDBsum; 4I2I; -. DR PDBsum; 4I2J; -. DR PDBsum; 4IQT; -. DR PDBsum; 4IQU; -. DR PDBsum; 4IQV; -. DR PDBsum; 4IQW; -. DR PDBsum; 4QZ8; -. DR PDBsum; 4QZ9; -. DR PDBsum; 4QZA; -. DR PDBsum; 4QZB; -. DR PDBsum; 4QZC; -. DR PDBsum; 4QZD; -. DR PDBsum; 4QZE; -. DR PDBsum; 4QZF; -. DR PDBsum; 4QZG; -. DR PDBsum; 4QZH; -. DR PDBsum; 4QZI; -. DR PDBsum; 5D46; -. DR PDBsum; 5D49; -. DR PDBsum; 5D4B; -. DR ProteinModelPortal; P09838; -. DR SMR; P09838; -. DR STRING; 10090.ENSMUSP00000062078; -. DR iPTMnet; P09838; -. DR PhosphoSitePlus; P09838; -. DR MaxQB; P09838; -. DR PaxDb; P09838; -. DR PRIDE; P09838; -. DR DNASU; 21673; -. DR Ensembl; ENSMUST00000051806; ENSMUSP00000062078; ENSMUSG00000025014. [P09838-1] DR Ensembl; ENSMUST00000112200; ENSMUSP00000107819; ENSMUSG00000025014. [P09838-2] DR GeneID; 21673; -. DR KEGG; mmu:21673; -. DR UCSC; uc008hlo.1; mouse. [P09838-1] DR CTD; 1791; -. DR MGI; MGI:98659; Dntt. DR eggNOG; KOG2534; Eukaryota. DR eggNOG; COG1796; LUCA. DR GeneTree; ENSGT00940000158584; -. DR HOGENOM; HOG000263600; -. DR HOVERGEN; HBG003670; -. DR InParanoid; P09838; -. DR KO; K00977; -. DR OMA; KTWKAIR; -. DR OrthoDB; EOG091G073W; -. DR PhylomeDB; P09838; -. DR TreeFam; TF103012; -. DR BRENDA; 2.7.7.31; 3474. DR EvolutionaryTrace; P09838; -. DR PRO; PR:P09838; -. DR Proteomes; UP000000589; Chromosome 19. DR Bgee; ENSMUSG00000025014; Expressed in 27 organ(s), highest expression level in thymus. DR CleanEx; MM_DNTT; -. DR ExpressionAtlas; P09838; baseline and differential. DR Genevisible; P09838; MM. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0000791; C:euchromatin; ISO:MGI. DR GO; GO:0000790; C:nuclear chromatin; ISO:MGI. DR GO; GO:0016363; C:nuclear matrix; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003912; F:DNA nucleotidylexotransferase activity; IDA:MGI. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006259; P:DNA metabolic process; IDA:MGI. DR GO; GO:0006304; P:DNA modification; IEA:UniProtKB-KW. DR GO; GO:0033198; P:response to ATP; ISO:MGI. DR CDD; cd00027; BRCT; 1. DR CDD; cd00141; NT_POLXc; 1. DR Gene3D; 1.10.150.110; -; 1. DR Gene3D; 3.30.210.10; -; 1. DR Gene3D; 3.40.50.10190; -; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR002054; DNA-dir_DNA_pol_X. DR InterPro; IPR019843; DNA_pol-X_BS. DR InterPro; IPR010996; DNA_pol_b-like_N. DR InterPro; IPR028207; DNA_pol_B_palm_palm. DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain. DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf. DR InterPro; IPR037160; DNA_Pol_thumb_sf. DR InterPro; IPR022312; DNA_pol_X. DR InterPro; IPR029398; PolB_thumb. DR InterPro; IPR027292; TdT. DR InterPro; IPR001726; TdT/Mu. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF14792; DNA_pol_B_palm; 1. DR Pfam; PF14791; DNA_pol_B_thumb; 1. DR Pfam; PF10391; DNA_pol_lambd_f; 1. DR Pfam; PF14716; HHH_8; 1. DR PIRSF; PIRSF000817; DNA_NT; 1. DR PIRSF; PIRSF501175; TDT; 1. DR PRINTS; PR00869; DNAPOLX. DR PRINTS; PR00871; DNAPOLXTDT. DR SMART; SM00292; BRCT; 1. DR SMART; SM00483; POLXc; 1. DR SUPFAM; SSF47802; SSF47802; 1. DR SUPFAM; SSF52113; SSF52113; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS00522; DNA_POLYMERASE_X; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW Direct protein sequencing; Hydrolase; Magnesium; Metal-binding; KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome; KW Terminal addition; Transferase. FT CHAIN 1 510 DNA nucleotidylexotransferase. FT /FTId=PRO_0000218792. FT DOMAIN 27 124 BRCT. {ECO:0000255|PROSITE- FT ProRule:PRU00033}. FT REGION 151 510 Mediates interaction with DNTTIP2. FT {ECO:0000250|UniProtKB:P04053}. FT REGION 258 262 Involved in DNA binding. FT {ECO:0000269|PubMed:11823435, FT ECO:0000269|PubMed:23856622}. FT REGION 333 338 Deoxynucleoside triphosphate binding. FT {ECO:0000244|PDB:4I2B, FT ECO:0000244|PDB:4I2C, FT ECO:0000244|PDB:4I2D, FT ECO:0000244|PDB:4I2E, ECO:0000305}. FT REGION 342 345 Deoxynucleoside triphosphate binding. FT {ECO:0000244|PDB:4I2B, FT ECO:0000244|PDB:4I2C, FT ECO:0000244|PDB:4I2D, FT ECO:0000244|PDB:4I2E, ECO:0000305}. FT REGION 449 450 Deoxynucleoside triphosphate binding. FT {ECO:0000244|PDB:4I2B, FT ECO:0000244|PDB:4I2C, FT ECO:0000244|PDB:4I2D, FT ECO:0000244|PDB:4I2E, ECO:0000305}. FT MOTIF 11 17 Nuclear localization signal. FT {ECO:0000250|UniProtKB:P06526}. FT METAL 343 343 Magnesium. {ECO:0000244|PDB:1JMS, FT ECO:0000244|PDB:4I2B, ECO:0000305}. FT METAL 345 345 Magnesium. {ECO:0000244|PDB:1JMS, FT ECO:0000244|PDB:4I2B, ECO:0000305}. FT METAL 434 434 Magnesium. {ECO:0000244|PDB:1JMS, FT ECO:0000244|PDB:4I2B, ECO:0000305}. FT MOD_RES 134 134 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT VAR_SEQ 482 482 K -> KGKTVTISPLDGKVSKLQKAL (in isoform FT TDT-L). {ECO:0000303|PubMed:11136823, FT ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:3755527}. FT /FTId=VSP_059967. FT MUTAGEN 29 29 D->A: Almost complete loss of exonuclease FT activity in TDT-L; when associated with FT A-170 and A-473. Decreased transferase FT activity in TDT-S; when associated with FT A-170 and A-473. FT {ECO:0000269|PubMed:11938351}. FT MUTAGEN 170 170 D->A: Almost complete loss of exonuclease FT activity in TDT-L; when associated with FT A-29 and A-473. Decreased transferase FT activity in TDT-S; when associated with FT A-29 and A-473. FT {ECO:0000269|PubMed:11938351}. FT MUTAGEN 342 342 H->A: Nearly abolishes enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT MUTAGEN 398 398 L->A: Nearly abolishes enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT MUTAGEN 399 399 D->A: Nearly abolishes enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT MUTAGEN 400 400 H->A: Reduces enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT MUTAGEN 403 403 K->A: Nearly abolishes enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT MUTAGEN 473 473 D->A: Almost complete loss of exonuclease FT activity in TDT-L; when associated with FT A-29 and A-170. Decreased transferase FT activity in TDT-S; when associated with FT A-29 and A-170. FT {ECO:0000269|PubMed:11938351}. FT MUTAGEN 473 473 D->A: Nearly abolishes enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT MUTAGEN 475 475 H->A: Nearly abolishes enzyme activity. FT {ECO:0000269|PubMed:23856622}. FT CONFLICT 26 26 T -> M (in Ref. 2; CAA48634). FT {ECO:0000305}. FT CONFLICT 99 99 L -> F (in Ref. 2; CAA48634). FT {ECO:0000305}. FT CONFLICT 193 193 R -> G (in Ref. 1; CAA27735). FT {ECO:0000305}. FT CONFLICT 287 287 Q -> K (in Ref. 1; CAA27735). FT {ECO:0000305}. FT CONFLICT 309 309 E -> Q (in Ref. 1; CAA27735). FT {ECO:0000305}. FT CONFLICT 367 367 D -> H (in Ref. 1; CAA27735). FT {ECO:0000305}. FT CONFLICT 441 445 DRRAF -> ECAC (in Ref. 1; CAA27735). FT {ECO:0000305}. FT HELIX 154 156 {ECO:0000244|PDB:4I2A}. FT HELIX 166 181 {ECO:0000244|PDB:4I2A}. FT HELIX 185 199 {ECO:0000244|PDB:4I2A}. FT HELIX 208 211 {ECO:0000244|PDB:4I2A}. FT HELIX 219 231 {ECO:0000244|PDB:4I2A}. FT HELIX 235 242 {ECO:0000244|PDB:4I2A}. FT HELIX 244 253 {ECO:0000244|PDB:4I2A}. FT HELIX 260 268 {ECO:0000244|PDB:4I2A}. FT HELIX 274 279 {ECO:0000244|PDB:4I2A}. FT HELIX 287 294 {ECO:0000244|PDB:4I2A}. FT HELIX 296 300 {ECO:0000244|PDB:4I2A}. FT HELIX 305 322 {ECO:0000244|PDB:4I2A}. FT STRAND 327 330 {ECO:0000244|PDB:4I2A}. FT HELIX 332 335 {ECO:0000244|PDB:4I2A}. FT STRAND 339 342 {ECO:0000244|PDB:4I2A}. FT STRAND 344 349 {ECO:0000244|PDB:4I2A}. FT HELIX 355 372 {ECO:0000244|PDB:4I2A}. FT STRAND 375 381 {ECO:0000244|PDB:4I2A}. FT HELIX 387 389 {ECO:0000244|PDB:5D49}. FT STRAND 394 396 {ECO:0000244|PDB:4I2A}. FT STRAND 401 411 {ECO:0000244|PDB:4I2A}. FT HELIX 412 414 {ECO:0000244|PDB:4I2A}. FT STRAND 425 437 {ECO:0000244|PDB:4I2A}. FT HELIX 440 442 {ECO:0000244|PDB:4I2A}. FT HELIX 443 451 {ECO:0000244|PDB:4I2A}. FT HELIX 454 468 {ECO:0000244|PDB:4I2A}. FT STRAND 470 472 {ECO:0000244|PDB:4I2A}. FT STRAND 477 479 {ECO:0000244|PDB:4I2A}. FT TURN 480 482 {ECO:0000244|PDB:4I2A}. FT STRAND 484 486 {ECO:0000244|PDB:4I2E}. FT HELIX 491 498 {ECO:0000244|PDB:4I2A}. FT HELIX 505 507 {ECO:0000244|PDB:4I2A}. SQ SEQUENCE 510 AA; 58266 MW; CF6E850EE36EE3BF CRC64; MDPLQAVHLG PRKKRPRQLG TPVASTPYDI RFRDLVLFIL EKKMGTTRRA FLMELARRKG FRVENELSDS VTHIVAENNS GSDVLEWLQL QNIKASSELE LLDISWLIEC MGAGKPVEMM GRHQLVVNRN SSPSPVPGSQ NVPAPAVKKI SQYACQRRTT LNNYNQLFTD ALDILAENDE LRENEGSCLA FMRASSVLKS LPFPITSMKD TEGIPCLGDK VKSIIEGIIE DGESSEAKAV LNDERYKSFK LFTSVFGVGL KTAEKWFRMG FRTLSKIQSD KSLRFTQMQK AGFLYYEDLV SCVNRPEAEA VSMLVKEAVV TFLPDALVTM TGGFRRGKMT GHDVDFLITS PEATEDEEQQ LLHKVTDFWK QQGLLLYCDI LESTFEKFKQ PSRKVDALDH FQKCFLILKL DHGRVHSEKS GQQEGKGWKA IRVDLVMCPY DRRAFALLGW TGSRQFERDL RRYATHERKM MLDNHALYDR TKRVFLEAES EEEIFAHLGL DYIEPWERNA //