ID A0A9D3XBX5_9SAUR Unreviewed; 485 AA.
AC A0A9D3XBX5;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 18-JUN-2025, entry version 10.
DE RecName: Full=DNA-directed DNA/RNA polymerase mu {ECO:0000256|ARBA:ARBA00071509, ECO:0000256|PIRNR:PIRNR000817};
DE EC=2.7.7.7 {ECO:0000256|PIRNR:PIRNR000817};
GN ORFNames=KIL84_010434 {ECO:0000313|EMBL:KAH1176732.1};
OS Mauremys mutica (yellowpond turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Geoemydidae; Geoemydinae; Mauremys.
OX NCBI_TaxID=74926 {ECO:0000313|EMBL:KAH1176732.1, ECO:0000313|Proteomes:UP000827986};
RN [1] {ECO:0000313|EMBL:KAH1176732.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MM-2020 {ECO:0000313|EMBL:KAH1176732.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAH1176732.1};
RA Gong S., Gao Y.;
RT "The genome of Mauremys mutica provides insights into the evolution of
RT semi-aquatic lifestyle.";
RL Submitted (SEP-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Gap-filling polymerase involved in repair of DNA double-
CC strand breaks by non-homologous end joining (NHEJ). Participates in
CC immunoglobulin (Ig) light chain gene rearrangement in V(D)J
CC recombination. {ECO:0000256|ARBA:ARBA00054461}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC EC=2.7.7.7; 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAH1176732.1}.
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DR EMBL; JAHDVG010000474; KAH1176732.1; -; Genomic_DNA.
DR OrthoDB; 205514at2759; -.
DR Proteomes; UP000827986; 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:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:TreeGrafter.
DR CDD; cd00141; NT_POLXc; 1.
DR FunFam; 1.10.150.20:FF:000010; DNA polymerase lambda; 1.
DR FunFam; 1.10.150.110:FF:000003; DNA polymerase mu; 1.
DR FunFam; 3.30.210.10:FF:000004; DNA-directed DNA/RNA polymerase mu; 1.
DR FunFam; 3.40.50.10190:FF:000035; DNA-directed DNA/RNA polymerase mu; 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; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR PANTHER; PTHR11276:SF24; DNA-DIRECTED DNA_RNA POLYMERASE MU; 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; 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 DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000817};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000817};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR000817};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR000817};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000827986};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000817}.
FT DOMAIN 20..119
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
FT BINDING 409
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
SQ SEQUENCE 485 AA; 53817 MW; CE73CDF643EEB4E6 CRC64;
MALVPLKRRR RAPSPSDGPP GAGRFPAVVL CLVEKRMGAS RRAFLTQLAR AKGFRVDGAY
SAAVTHVVSE QNSGDEVARW LEQQREECGA GGDPALLDIS WFTESMGAGR PVEIESRHRL
RVTVLAPLGQ QMAPYACQRR TPLLHSNQPL TEALETLAEE AGFSGSEGRS LAFTRAASVL
KALPGRLSTL EELGPLPGIG EHSRRVIQDV LEDGVSVEVE RVKLSERYRT MKLFTKIFGV
GVRTASRWYQ EGLRTLGDLQ ERNTKLTRQQ QAGLRHYEDL NTPVERGEAE SIGQMVQEAV
QRFLPGASVT LAGGFRRGKP HGHDVDLLLT HPEAGREAGL LTRVVSWLDS QGLILYQHSQ
ENSFTLHEGP EAPGGRDVLD RFERCFSIFR LEVQGGPGAA RGWKAVRVDL VVAPVSQFPF
ALLGWTGSRH FERELRRFAS HERRMVLNSH TLYDTRQNLF LPAASEEEIF QLLGLEYVPP
AQRNA
//
