ID A0A091KGW0_9GRUI Unreviewed; 505 AA.
AC A0A091KGW0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=DNA nucleotidylexotransferase {ECO:0000256|ARBA:ARBA00015018, ECO:0000256|PIRNR:PIRNR000817};
DE EC=2.7.7.31 {ECO:0000256|ARBA:ARBA00012435, ECO:0000256|PIRNR:PIRNR000817};
GN ORFNames=N324_12983 {ECO:0000313|EMBL:KFP38678.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP38678.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP38678.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP38678.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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:0000256|ARBA:ARBA00037135}.
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:0000256|ARBA:ARBA00024522,
CC ECO:0000256|PIRNR:PIRNR000817};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000817, ECO:0000256|PIRSR:PIRSR000817-1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR000817}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family.
CC {ECO:0000256|ARBA:ARBA00008323, ECO:0000256|PIRNR:PIRNR000817}.
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DR EMBL; KK740816; KFP38678.1; -; Genomic_DNA.
DR RefSeq; XP_010127496.1; XM_010129194.1.
DR AlphaFoldDB; A0A091KGW0; -.
DR GeneID; 104486491; -.
DR KEGG; cmac:104486491; -.
DR CTD; 1791; -.
DR OrthoDB; 3019669at2759; -.
DR Proteomes; UP000053330; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003912; F:DNA nucleotidylexotransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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; 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:SF21; DNA NUCLEOTIDYLEXOTRANSFERASE; 1.
DR PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 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; 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 {ECO:0000256|PIRNR:PIRNR000817, ECO:0000256|PIRSR:PIRSR000817-1};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000817,
KW ECO:0000256|PIRSR:PIRSR000817-1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR000817};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR000817};
KW Reference proteome {ECO:0000313|Proteomes:UP000053330};
KW Terminal addition {ECO:0000256|ARBA:ARBA00022639};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000817}.
FT DOMAIN 27..124
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
SQ SEQUENCE 505 AA; 58442 MW; 21BA03AF92FCD5A2 CRC64;
MDGIRAPVVS SQRKRQKGMH SPNLSCSYEI KFSKFVIFIM QRKMGMTRRK FLMELARRKG
FRVESELSDS VTHIVAENNS YLEVLDWLRG QAVGDSSRFE LLDISWFTAC MEAGRPVASE
IKYRLMEQDQ SPPLNTPESE VPSFIASKVS QYSCQRKTTL NNYNKKFTDA FEIMAENYEF
KENEILCLEF LRAASVLKFL PFPVTRMKDI QGLPCMGDRV RDVIEEIIEE GESSRAKEVL
NDERYKSFKQ FTSVFGVGVK TSEKWYRMGL RTLEEVKVDK TLKLTKMQRA GFLYYEDLVS
CVTEAEAGAV SLIVKNTVCT FLPDALVTIT GGFRRGKKIG HDIDFLITNP GPREDDELLH
KGLLLYCDVI ESTFVKEHLP SRNVDVMDNF QKCFAILKLH QPRADNSSYN MSKEFDMAEV
KDWKAIRVDL VITPFEQYAY ALLGWTGSRQ FGRDLRRYAS HERKMLLDNH VLYDRRKRIF
LKAGSEEEIF AHLGLDYVEP WERNA
//
