TDT_CHICK
ID TDT_CHICK Reviewed; 506 AA.
AC P36195;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 134.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=7596835; DOI=10.1093/nar/23.11.2041;
RA Yang B., Gathy K.N., Coleman M.S.;
RT "T-cell specific avian TdT: characterization of the cDNA and recombinant
RT enzyme.";
RL Nucleic Acids Res. 23:2041-2048(1995).
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 -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
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DR EMBL; U06938; AAA75280.1; -; mRNA.
DR PIR; S55786; S55786.
DR RefSeq; NP_990720.1; NM_205389.1.
DR AlphaFoldDB; P36195; -.
DR SMR; P36195; -.
DR STRING; 9031.ENSGALP00000032645; -.
DR PaxDb; P36195; -.
DR PRIDE; P36195; -.
DR GeneID; 396351; -.
DR KEGG; gga:396351; -.
DR CTD; 1791; -.
DR VEuPathDB; HostDB:geneid_396351; -.
DR eggNOG; KOG2534; Eukaryota.
DR InParanoid; P36195; -.
DR OrthoDB; 1212057at2759; -.
DR PhylomeDB; P36195; -.
DR PRO; PR:P36195; -.
DR Proteomes; UP000000539; 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: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 Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Terminal addition; Transferase.
FT CHAIN 1..506
FT /note="DNA nucleotidylexotransferase"
FT /id="PRO_0000218795"
FT DOMAIN 27..124
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
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 430
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 445..446
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P09838"
SQ SEQUENCE 506 AA; 58447 MW; 92B2BFD87B30E94E CRC64;
MERIRPPTVV SQRKRQKGMY SPKLSCGYEI KFNKLVIFIM QRKMGMTRRT FLMELARSKG
FRVESELSDS VTHIVAENNS YPEVLDWLKG QAVGDSSRFE ILDISWLTAC MEMGRPVDLE
KKYHLVEQAG QYPTLKTPES EVSSFTASKV SQYSCQRKTT LNNCNKKFTD AFEIMAENYE
FKENEIFCLE FLRAASVLKS LPFPVTRMKD IQGLPCMGDR VRDVIEEIIE EGESSRAKDV
LNDERYKSFK EFTSVFGVGV KTSEKWFRMG LRTVEEVKAD KTLKLSKMQR AGFLYYEDLV
SCVSKAEADA VSSIVKNTVC TFLPDALVTI TGGFRRGKKI GHDIDFLITS PGQREDDELL
HKGLLLYCDI IESTFVKEQI PSRHVDAMDH FQKCFAILKL YQPRVDNSSY NMSKKCDMAE
VKDWKAIRVD LVITPFEQYA YALLGWTGSR QFGRDLRRYA THERKMMLDN HALYDKRKRV
FLKAGSEEEI FAHLGLDYVE PWERNA
