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 24-JAN-2024, entry version 69.
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; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 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; 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; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR027292; TdT.
DR InterPro; IPR001726; TdT/Mu.
DR PANTHER; PTHR11276:SF21; DNA NUCLEOTIDYLEXOTRANSFERASE; 1.
DR PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR Pfam; PF10391; DNA_pol_lambd_f; 1.
DR Pfam; PF01909; NTP_transf_2; 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; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81585; PsbU/PolX domain-like; 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
//
