ID A0A3Q7SPT3_VULVU Unreviewed; 548 AA.
AC A0A3Q7SPT3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA-directed DNA/RNA polymerase mu {ECO:0000256|PIRNR:PIRNR000817};
DE EC=2.7.7.7 {ECO:0000256|PIRNR:PIRNR000817};
GN Name=POLM {ECO:0000313|RefSeq:XP_025844135.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025844135.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025844135.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025844135.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025844135.1};
RG RefSeq;
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|ARBA:ARBA00024632,
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|PIRNR:PIRNR000817}.
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DR RefSeq; XP_025844135.1; XM_025988350.1.
DR AlphaFoldDB; A0A3Q7SPT3; -.
DR Proteomes; UP000286640; Unplaced.
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:UniProtKB-KW.
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 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; IPR022312; DNA_pol_X.
DR InterPro; IPR043519; NT_sf.
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; PF10391; DNA_pol_lambd_f; 1.
DR Pfam; PF14716; HHH_8; 1.
DR PIRSF; PIRSF000817; DNA_NT; 2.
DR PIRSF; PIRSF501176; DNApol_mu; 2.
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 damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
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|PIRNR:PIRNR000817};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR000817};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Transferase {ECO:0000256|PIRNR:PIRNR000817}.
FT DOMAIN 57..154
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
FT BINDING 488
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
SQ SEQUENCE 548 AA; 59467 MW; 240B266F6F3A1F28 CRC64;
MGEACSPGPP GAASPSSGLR RLSSDFRVPF PAPARGRDRM LPKRRRAQVG APGDPASSEA
RFPGVAIYLA EPHMGRSRRA FLTRLALSKG FRVLDAYSSE VTHVVMEQTS AEEASHWQEH
RAAAASPQRC SRPALLDISW FTESMAAGQP VPVECRHRLE VAAPRKGLPC PARMLPYACQ
RPTPLTHHNS SLSEALEMLA EAAGFEGSEG RFLSFRRAAA VLKALPSPVT ALSQLQGLPH
FGEHSRRVVQ ELLEQGVCEE VERVRLSERY QTMKLFTGIF GVGVKTADRW YQEGLRTLDS
LQEQPQRLTQ QQKAGLQHYQ DLSTPVQRPD AEALMQLVKA AVAPVLPGAT VTLAGGFRRG
KLQGHDVDLL ISHPQEGREA GLLPRVMQCL EKQVRGSQAC PECAAWPWLL APSPMPRWPP
CLLSPQGLVL YQQHHRGGCG HAEPPPRQSH PMDAFERTFC ILGLPQPSGV PVGSTQGPCP
TRKAVRVDLV AVPISRLPFA LLGWTGSKVG CVLRGRPGAR ERCCHSCSPH STSRGSCAAS
AGRRGGCG
//
