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TDT_AMBME
ID   TDT_AMBME               Reviewed;         510 AA.
AC   O57486; Q800C6;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 104.
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; Synonyms=TDT;
OS   Ambystoma mexicanum (Axolotl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Caudata; Salamandroidea; Ambystomatidae; Ambystoma.
OX   NCBI_TaxID=8296;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=15146297; DOI=10.1007/s00251-004-0681-2;
RA   Golub R., Andre S., Hassanin A., Affaticati P., Larijani M., Fellah J.S.;
RT   "Early expression of two TdT isoforms in the hematopoietic system of the
RT   Mexican axolotl. Implications for the evolutionary origin of the N-
RT   nucleotide addition.";
RL   Immunogenetics 56:204-213(2004).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O57486-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O57486-2; Sequence=VSP_007952;
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
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DR   EMBL; AF039209; AAB92673.2; -; mRNA.
DR   EMBL; AY248700; AAO92254.1; -; mRNA.
DR   AlphaFoldDB; O57486; -.
DR   SMR; O57486; -.
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; 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   Alternative splicing; Magnesium; Metal-binding; Nucleotidyltransferase;
KW   Nucleus; Terminal addition; Transferase.
FT   CHAIN           1..510
FT                   /note="DNA nucleotidylexotransferase"
FT                   /id="PRO_0000218794"
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         434
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P09838"
FT   BINDING         449..450
FT                   /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61560"
FT                   /evidence="ECO:0000250|UniProtKB:P09838"
FT   VAR_SEQ         166..222
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15146297"
FT                   /id="VSP_007952"
SQ   SEQUENCE   510 AA;  58244 MW;  BA83394777EFA6D0 CRC64;
     MYAFPTTRIA PRRKQPKCIK PPKCTSKYDI KFKDIAIYIL ERKMGASRRY FLMELARKKG
     FRVEPDLSEY VTHVVSEKNS GAEVLEWLQA KKAGSIPNVA ILDISWFTDC MGAGQPVEIE
     RKHRLTLQKI CVCKSPSPVV PSRVGVSQYA CQRKTTLDNK NTLFTDAFEI LAENYEFREN
     ERSCLSFRQA ASVLKSLTFT IAGMADVDGL PGFGDHIRAV IEDLIEDGES SKVSEVLNDE
     VYRSLKLFTT IFGVGLRTAE KWHRLGIRTL EEIKSNENLK FSKMQIAGLQ HYEDILGGVR
     KAEADAVAMV VRDAVWTFLP DAVVTLTGGF RRGNKTGHDV DMLITSPIQG KEKELLHKVI
     NLWKKQDLLL CHTIHESTMD EDNLPSKSVN LLDHFQKCFA ILKSNQHRGE ISSCDGPHDS
     RERGKRIWKA IRVDLVFCPF EQYAFALLGW TGSRQFERDL RRYASHEKKM MIDNHALYDK
     TKRVFVKCES EEEIFGHLGL EYIDPVERNA
 
 
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