TDT_BOVIN
ID TDT_BOVIN Reviewed; 509 AA.
AC P06526; A4FUF8;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=DNA nucleotidylexotransferase;
DE EC=2.7.7.31;
DE AltName: Full=Terminal addition enzyme;
DE AltName: Full=Terminal deoxynucleotidyltransferase;
DE Short=TDT;
DE Short=Terminal transferase;
GN Name=DNTT; Synonyms=TDT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Thymus;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-2.
RX PubMed=3579900; DOI=10.1016/s0006-291x(87)80493-x;
RA Koiwai O., Kaneda T., Morishita R.;
RT "Analysis of human terminal deoxynucleotidyl transferase cDNA expressible
RT in mammalian cells.";
RL Biochem. Biophys. Res. Commun. 144:185-190(1987).
RN [4]
RP PROTEIN SEQUENCE OF 132-168; 169-176; 183-188; 191-219; 223-334; 336-415
RP AND 421-509.
RX PubMed=2713339; DOI=10.1021/bi00428a045;
RA Evans R.K., Beach C.M., Coleman M.S.;
RT "Photoaffinity labeling of terminal deoxynucleotidyl transferase. 2.
RT Identification of peptides in the nucleotide binding domain.";
RL Biochemistry 28:713-720(1989).
RN [5]
RP PROTEIN SEQUENCE OF 210-238.
RX PubMed=3346221; DOI=10.1016/s0021-9258(18)68987-2;
RA Pandey V.N., Modak M.J.;
RT "Biochemistry of terminal deoxynucleotidyltransferase. Affinity labeling
RT and identification of the deoxynucleoside triphosphate binding domain of
RT terminal deoxynucleotidyltransferase.";
RL J. Biol. Chem. 263:3744-3751(1988).
RN [6]
RP PROTEIN SEQUENCE OF 210-221 AND 224-238, AND ATP- AND DTTP-BINDING SITES
RP CYS-216 AND CYS-224.
RX PubMed=2910867; DOI=10.1016/s0021-9258(19)85023-8;
RA Pandey V.N., Modak M.J.;
RT "Biochemistry of terminal deoxynucleotidyltransferase. Identification and
RT unity of ribo- and deoxyribonucleoside triphosphate binding site in
RT terminal deoxynucleotidyltransferase.";
RL J. Biol. Chem. 264:867-871(1989).
RN [7]
RP PROTEIN SEQUENCE OF 306-326; 337-357 AND 483-506.
RX PubMed=6087320; DOI=10.1073/pnas.81.14.4363;
RA Peterson R.C., Cheung L.C., Mattaliano R.J., Chang L.M.S., Bollum F.J.;
RT "Molecular cloning of human terminal deoxynucleotidyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4363-4367(1984).
CC -!- FUNCTION: Template-independent DNA polymerase which catalyzes the
CC random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a
CC DNA initiator (PubMed:3755527). One of the in vivo functions of this
CC enzyme is the addition of nucleotides at the junction (N region) of
CC rearranged Ig heavy chain and T-cell receptor gene segments during the
CC maturation of B- and T-cells. {ECO:0000250|UniProtKB:P09838,
CC ECO:0000269|PubMed:3755527}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.31;
CC Evidence={ECO:0000250|UniProtKB:P09838};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P09838};
CC Note=Can also utilize other divalent cations, such as Mn(2+) and Co(2+)
CC (in vitro). {ECO:0000250|UniProtKB:P09838};
CC -!- SUBUNIT: Interacts with PRP19 and DNTTIP1. Forms a ternary complex with
CC DNTTIP2 and core histone. Released from this complex by PCNA. Interacts
CC with TRERF1. {ECO:0000250|UniProtKB:P04053}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:3755527}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA87354.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA27734.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X04122; CAA27734.1; ALT_INIT; mRNA.
DR EMBL; BC114820; AAI14821.1; -; mRNA.
DR EMBL; M26146; AAA87354.1; ALT_INIT; mRNA.
DR PIR; A23595; A23595.
DR RefSeq; NP_803461.1; NM_177495.2.
DR RefSeq; XP_005225486.1; XM_005225429.2.
DR AlphaFoldDB; P06526; -.
DR SMR; P06526; -.
DR BioGRID; 158482; 1.
DR STRING; 9913.ENSBTAP00000051460; -.
DR BindingDB; P06526; -.
DR ChEMBL; CHEMBL5289; -.
DR PaxDb; P06526; -.
DR PRIDE; P06526; -.
DR Ensembl; ENSBTAT00000027223; ENSBTAP00000027223; ENSBTAG00000020427.
DR GeneID; 281120; -.
DR KEGG; bta:281120; -.
DR CTD; 1791; -.
DR VEuPathDB; HostDB:ENSBTAG00000020427; -.
DR VGNC; VGNC:28150; DNTT.
DR eggNOG; KOG2534; Eukaryota.
DR GeneTree; ENSGT00940000158584; -.
DR HOGENOM; CLU_008698_0_0_1; -.
DR InParanoid; P06526; -.
DR OMA; PKVINLW; -.
DR OrthoDB; 1212057at2759; -.
DR TreeFam; TF103012; -.
DR BRENDA; 2.7.7.31; 908.
DR PRO; PR:P06526; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000020427; Expressed in thymus and 15 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0006304; P:DNA modification; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 1.10.150.110; -; 1.
DR Gene3D; 3.30.210.10; -; 1.
DR Gene3D; 3.30.460.10; -; 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; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR InterPro; IPR027292; TdT.
DR InterPro; IPR001726; TdT/Mu.
DR PANTHER; PTHR11276; PTHR11276; 1.
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 SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Terminal addition;
KW Transferase.
FT CHAIN 1..509
FT /note="DNA nucleotidylexotransferase"
FT /id="PRO_0000218790"
FT DOMAIN 27..124
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..509
FT /note="Mediates interaction with DNTTIP2"
FT /evidence="ECO:0000250|UniProtKB:P04053"
FT REGION 258..262
FT /note="Involved in DNA binding"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT MOTIF 11..17
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:3755527"
FT BINDING 333..338
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 342..345
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 433
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 448..449
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P09838"
SQ SEQUENCE 509 AA; 58296 MW; EE5262617BA5D207 CRC64;
MDPLCTASSG PRKKRPRQVG ASMASPPHDI KFQNLVLFIL EKKMGTTRRN FLMELARRKG
FRVENELSDS VTHIVAENNS GSEVLEWLQV QNIRASSQLE LLDVSWLIES MGAGKPVEIT
GKHQLVVRTD YSATPNPGFQ KTPPLAVKKI SQYACQRKTT LNNYNHIFTD AFEILAENSE
FKENEVSYVT FMRAASVLKS LPFTIISMKD TEGIPCLGDK VKCIIEEIIE DGESSEVKAV
LNDERYQSFK LFTSVFGVGL KTSEKWFRMG FRSLSKIMSD KTLKFTKMQK AGFLYYEDLV
SCVTRAEAEA VGVLVKEAVW AFLPDAFVTM TGGFRRGKKI GHDVDFLITS PGSAEDEEQL
LPKVINLWEK KGLLLYYDLV ESTFEKFKLP SRQVDTLDHF QKCFLILKLH HQRVDSSKSN
QQEGKTWKAI RVDLVMCPYE NRAFALLGWT GSRQFERDIR RYATHERKMM LDNHALYDKT
KRVFLKAESE EEIFAHLGLD YIEPWERNA
