TDT_MONDO
ID TDT_MONDO Reviewed; 518 AA.
AC O02789;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 137.
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 Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9553155; DOI=10.1007/s002510050386;
RA Guth A.M., Rosenberg G.H., Miller R.D.;
RT "Opossum (Monodelphis domestica) terminal deoxynucleotidyl transferase
RT gene.";
RL Immunogenetics 47:483-486(1998).
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. Interacts with TRERF1. Forms
CC a ternary complex with DNTTIP2 and core histone. Released from this
CC complex by PCNA (By similarity). {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; U91571; AAC17587.1; -; mRNA.
DR RefSeq; NP_001028151.1; NM_001032979.1.
DR AlphaFoldDB; O02789; -.
DR SMR; O02789; -.
DR STRING; 13616.ENSMODP00000005738; -.
DR GeneID; 554183; -.
DR KEGG; mdo:554183; -.
DR CTD; 1791; -.
DR eggNOG; KOG2534; Eukaryota.
DR InParanoid; O02789; -.
DR OrthoDB; 1212057at2759; -.
DR Proteomes; UP000002280; Unplaced.
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 2: Evidence at transcript level;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Terminal addition; Transferase.
FT CHAIN 1..518
FT /note="DNA nucleotidylexotransferase"
FT /id="PRO_0000218793"
FT DOMAIN 27..124
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 153..518
FT /note="Mediates interaction with DNTTIP2"
FT /evidence="ECO:0000250|UniProtKB:P04053"
FT REGION 260..264
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 335..340
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 344..347
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
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 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 442
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 457..458
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P09838"
SQ SEQUENCE 518 AA; 60010 MW; 28E043428FEF3C42 CRC64;
MHRIRTIDSD FGKKRQKKMD NHISSMIYEI KFHEFVLFIL EKKMGATRRT FLTDLARKKG
FRVENELSNS VTHIVAENNS GSDVLAWLKT HKMEKTTQFE LLDISWLIEC MKVGKPVDTK
GKYQLMESRV DSANPDPTAG TLNILPPTTK TISQYACQRR TTINNHNQRF TDAFEILAKN
YEFKENDDTC LTFMRAISVL KCLPFEVVSL KDTEGLPWIG DEVKGIMEEI IEDGESLEVQ
AVLNDERYQS FKLFTSVFGV GLKTADKWYR MGFRTLNKIR SDKTLKLTKM QKAGLCYYED
LIDCVSKAEA DAVSLLVQDA VWTFLPDALV TITGGFRRGK EFGHDVDFLI TSPGAEKEQE
DQLLQKVTNL WKKQGLLLYC DLIESTFEDL KLPSRKIDAL DHFQKCFLIL KLYHHKEDKR
KWEMPTGSNE SEAKSWKAIR VDLVVCPYDR YAFALLGWSG SRQFERDLRR YATHEKKMML
DNHALYDKTK KIFLKAKSEE EIFAHLGLEY IQPSERNA
