TDT_XENLA
ID TDT_XENLA Reviewed; 507 AA.
AC P42118;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=8157965;
RA Lee A., Hsu E.;
RT "Isolation and characterization of the Xenopus terminal deoxynucleotidyl
RT transferase.";
RL J. Immunol. 152:4500-4507(1994).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P04053}.
CC -!- TISSUE SPECIFICITY: Found in the thymus and not in the spleen, kidney,
CC intestine, or liver.
CC -!- DEVELOPMENTAL STAGE: During ontogeny TDT appears in significant amounts
CC in the thymus of tadpoles at metamorphic climax but little in the
CC earlier midlarval stages.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
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DR EMBL; U07803; AAA18493.1; -; mRNA.
DR PIR; I51658; I51658.
DR RefSeq; NP_001079251.1; NM_001085782.1.
DR AlphaFoldDB; P42118; -.
DR SMR; P42118; -.
DR GeneID; 378525; -.
DR KEGG; xla:378525; -.
DR CTD; 378525; -.
DR Xenbase; XB-GENE-6252658; dntt.L.
DR OMA; PKVINLW; -.
DR OrthoDB; 1212057at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
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; 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; 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..507
FT /note="DNA nucleotidylexotransferase"
FT /id="PRO_0000218797"
FT DOMAIN 27..124
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 254..258
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 329..334
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 338..341
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 446..447
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P09838"
SQ SEQUENCE 507 AA; 58846 MW; 4B57F91C96E8B6D1 CRC64;
MNPLSQSALV PLRKKAKMAP ISQSFCQHNV KFKEIVLFLV ERKMGSSRRT FLMELARKRG
FQTEIELSDS VTHIVAENNS GAEVLEWLQS KKLGFTVKTH ILDISWFTEC MEAGRPVEIQ
NRHLLPVQQD CSANFNPPLS SSCVQVSQYA CQRCTTLQDT NRIFTDAFDI LAEHFEFCEN
KGRTVAFLRA SSLIKSLPFP ITAMKELEGL PWLGDQMKGI IEEILEEGKS YKVLEVMNEE
RYKSFKQFTS VFGVGLKTSD KWFRMGFRTL EEIKNEKELK LTKMQKCGLL YYEDITSYVS
RAEAETTEQL IKSIVWKFVP DAIVTLTGGF RRGKKKGHDV DILITCARKG KEKNILHNTM
SVLKNRGLLL FYNIIESTFD ETKLPSRHVD ALDHFQKCFT ILKLPKRQMD IGNIIDPHEC
ERKNWKAVRL DLVITPYEQY PYALLGWTGS RQFERDLRRY ATHEKRMMLD NHGLYDKTKN
NFLKANNEED IFKQLGLDYL EPWERNA
