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Database: UniProt
Entry: A0A452FR23_CAPHI
LinkDB: A0A452FR23_CAPHI
Original site: A0A452FR23_CAPHI 
ID   A0A452FR23_CAPHI        Unreviewed;       334 AA.
AC   A0A452FR23;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
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|Ensembl:ENSCHIP00000026655.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000026655.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000026655.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000026655.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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};
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   EMBL; LWLT01000003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A452FR23; -.
DR   Ensembl; ENSCHIT00000034520.1; ENSCHIP00000026655.1; ENSCHIG00000022903.1.
DR   GeneTree; ENSGT00940000158490; -.
DR   Proteomes; UP000291000; Chromosome 4.
DR   Bgee; ENSCHIG00000022903; Expressed in thymus and 18 other cell types or tissues.
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   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; IPR010996; DNA_pol_b-like_N.
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; 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; SSF81585; PsbU/PolX domain-like; 1.
DR   PROSITE; PS50172; BRCT; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|PIRNR:PIRNR000817};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000817};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000817};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR000817};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000817}.
FT   DOMAIN          18..114
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
SQ   SEQUENCE   334 AA;  36789 MW;  95DFB15EB8967F26 CRC64;
     MLPKRRRARV ASPRAAPSSA ARFPGVTIYL AEPHMGRSRQ AFLTRLAVSK GFRVLSTYSP
     EVTHVVMEGT SAEEAVCWQK RKTSALPPGC TRPVLLDISW FTESMAAGQP VPVECRHRLE
     VAVPKKKMPS PAWMLPYACQ RPTPLVHHNA SLSEALETLA EAAGFDGSEG RQISFYRAAS
     VLKALPSPVT ALSQLQGLPH FGEHSCRVVQ ELLEHGVCDE VERIRLSERY QTMKLFTQIF
     GVGVRTADQW YQKGLRTLDD LQEESHRLTQ QQKAGLQHHQ DLSALILRSE VEALQQVVEA
     AVTQALPGAT VTLAGGFRRA LSCTTSTSTA SRET
//
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