ID G3NEP2_GASAC Unreviewed; 481 AA.
AC G3NEP2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=DNA-directed DNA/RNA polymerase mu {ECO:0000256|PIRNR:PIRNR000817};
DE EC=2.7.7.7 {ECO:0000256|PIRNR:PIRNR000817};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000003793.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000003793.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000003793.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Gap-filling polymerase involved in repair of DNA double-
CC strand breaks by non-homologous end joining (NHEJ).
CC {ECO:0000256|PIRNR:PIRNR000817}.
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=2.7.7.7;
CC Evidence={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 AlphaFoldDB; G3NEP2; -.
DR STRING; 69293.ENSGACP00000003793; -.
DR Ensembl; ENSGACT00000003806.1; ENSGACP00000003793.1; ENSGACG00000002880.1.
DR eggNOG; KOG2534; Eukaryota.
DR GeneTree; ENSGT00940000158584; -.
DR InParanoid; G3NEP2; -.
DR OMA; PKVINLW; -.
DR TreeFam; TF103012; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000002880; Expressed in head kidney and 1 other cell type or tissue.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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: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; IPR027249; DNA/RNApol_mu.
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; 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; PIRSF501176; DNApol_mu; 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:UP000007635};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000817}.
FT DOMAIN 32..124
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
SQ SEQUENCE 481 AA; 54154 MW; 7EC1AC1ECCAD04BA CRC64;
SEEMFQSAVA PRARKRSRPA EAGVSRCNEV KFEDVRVFLV ERKMGRSRRS FLTQLATSKG
FIVENVLSDK VTHVVSEDSQ AASLWKWLRE CAPADPPGVH VLDISWFTDS MREGKPVAVE
TRHLIQQIYD DAVATPPEGS KPASMATVSQ FACQRRTTTE NSNKKITDAF EVLAENYEFN
EMDGSCLAFR RAASVLKSLP MAVRSLRETQ DLPCLGEHTK AVMEEVLRCG RSFEVEKLLS
DERYQTFKLF TSVFGVGPKT ADKWYRGGLR SFSEVLADRS IHLNQMQQIG FLHYGDISGV
VSKAEARSLR NIIDEAARAT TPAAKVALTG GFCREKEFGH DVDFIVTTPE LGGEETLLPK
IIDELKKQGM LLYCDYHPST FDINKLPSPK FEAMDHYAKC FLILRLEGSR VEGGLHIAEG
DNRGWRAVRV DLVSPPVDRY AFALLGWSGS RQFERDLRRF ARAKRGMLLD NHALYDKNKV
V
//
