ID   TDT_EULMA               Reviewed;         511 AA.
AC   A4PCD4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=DNA nucleotidylexotransferase;
DE            EC=2.7.7.31;
DE   AltName: Full=Terminal addition enzyme;
DE   AltName: Full=Terminal deoxynucleotidyltransferase;
DE            Short=Terminal transferase;
GN   Name=DNTT;
OS   Eulemur macaco (Black lemur) (Petterus macaco).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Lemuridae; Eulemur.
OX   NCBI_TaxID=30602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Aruga J., Toyoda A., Yoshikawa F., Nozaki Y., Sakaki Y., Furuichi T.;
RT   "Analysis of a phylogenetically conserved oligodendrocyte-enhancer in a
RT   mammalian gene, Opalin.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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. One of the in vivo functions of this enzyme is the
CC       addition of nucleotides at the junction (N region) of rearranged Ig
CC       heavy chain and T-cell receptor gene segments during the maturation of
CC       B- and T-cells. {ECO:0000250|UniProtKB:P09838}.
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:0000250|UniProtKB:P04053}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
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DR   EMBL; AB265806; BAF51669.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4PCD4; -.
DR   SMR; A4PCD4; -.
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:0006281; P:DNA repair; IEA:InterPro.
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; 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   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   3: Inferred from homology;
KW   Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW   Terminal addition; Transferase.
FT   CHAIN           1..511
FT                   /note="DNA nucleotidylexotransferase"
FT                   /id="PRO_0000288558"
FT   DOMAIN          27..124
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..511
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:0000250|UniProtKB:P06526"
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         435
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P09838"
FT   BINDING         450..451
FT                   /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61560"
FT                   /evidence="ECO:0000250|UniProtKB:P09838"
FT   MOD_RES         134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09838"
SQ   SEQUENCE   511 AA;  58585 MW;  AD54690A90E31E56 CRC64;
     MDPLQTAHAG PRKKRPRQTG ASMASTPQDV RFQDLVLFIL EKKMGSTRRT FLTELARRKG
     FRVENEFSDS VTHIVAENNS GSDVLEWLQV QKIKASSQLE VLDVSWLIEC MRTGKPVETT
     GKHQLVARSD CSASPNPGPQ KTPPLAVQKI SQYACQRRTT LNNCNHVFTD AFEILAENYE
     FKENEGCAVT FLRAASVLKS LPFTIITMRD TEGIPCLEDK VKCIIEEIIE DGESSEVKAV
     LNDERYQSFK LFTSVFGVGL KTSEKWFRMG FRTLSKIRSD KSLTFTRMQR AGFHYYEDLV
     SCVTRAEAEA VSVLVKEAVW AFLPDAFVTM TGGFRRGKKI GHDVDFLITS PGSTEEEEEQ
     LLHKVMNLWE KKGLLLYCDL VESTFEKLKL PSRKVDALDH FQKCFLILKL HHQRVVDSQK
     SSQQDGKTWK AIRVDLVMCP YERRAFALLG WTGSRQFERD LRRYATHERR MMLDNHGLWD
     KTKRIFLKAE SEEEIFAHLG LDYIEPSERN A