ID A0A7H9B0Q0_ZYGMR Unreviewed; 591 AA.
AC A0A7H9B0Q0;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU366014};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU366014};
GN ORFNames=HG535_0B04020 {ECO:0000313|EMBL:QLG71362.1};
OS Zygotorulaspora mrakii (Zygosaccharomyces mrakii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygotorulaspora.
OX NCBI_TaxID=42260 {ECO:0000313|EMBL:QLG71362.1, ECO:0000313|Proteomes:UP000509704};
RN [1] {ECO:0000313|EMBL:QLG71362.1, ECO:0000313|Proteomes:UP000509704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-6702 {ECO:0000313|EMBL:QLG71362.1,
RC ECO:0000313|Proteomes:UP000509704};
RA Coughlan A.Y., Lombardi L., Braun-Galleani S., Martos A.R., Galeote V.,
RA Bigey F., Dequin S., Byrne K.P., Wolfe K.H.;
RT "The yeast mating-type switching endonuclease HO is a domesticated member
RT of an unorthodox homing genetic element family.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase that functions in several pathways of DNA
CC repair. Involved in base excision repair (BER) responsible for repair
CC of lesions that give rise to abasic (AP) sites in DNA. Also contributes
CC to DNA double-strand break repair by non-homologous end joining and
CC homologous recombination. Has both template-dependent and template-
CC independent (terminal transferase) DNA polymerase activities. Has also
CC a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
CC {ECO:0000256|RuleBase:RU366014}.
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|ARBA:ARBA00049244,
CC ECO:0000256|RuleBase:RU366014};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU366014}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family.
CC {ECO:0000256|RuleBase:RU366014}.
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DR EMBL; CP058605; QLG71362.1; -; Genomic_DNA.
DR RefSeq; XP_037143090.1; XM_037287195.1.
DR AlphaFoldDB; A0A7H9B0Q0; -.
DR GeneID; 59235023; -.
DR OrthoDB; 205514at2759; -.
DR Proteomes; UP000509704; Chromosome 2.
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:0006284; P:base-excision repair; IEA:TreeGrafter.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:TreeGrafter.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 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; IPR002054; DNA-dir_DNA_pol_X.
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; IPR002008; DNA_pol_X_beta-like.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR PANTHER; PTHR11276:SF42; DNA POLYMERASE BETA; 1.
DR PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 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 PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00870; DNAPOLXBETA.
DR SMART; SM00483; POLXc; 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.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU366014};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU366014};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU366014}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU366014}; Nucleus {ECO:0000256|RuleBase:RU366014};
KW Reference proteome {ECO:0000313|Proteomes:UP000509704};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366014}.
FT DOMAIN 205..582
FT /note="DNA-directed DNA polymerase X"
FT /evidence="ECO:0000259|SMART:SM00483"
FT REGION 160..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 267
FT /note="Nucleophile; Schiff-base intermediate with DNA; for
FT 5'-dRP lyase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR622312-50"
SQ SEQUENCE 591 AA; 68527 MW; AB2575A11D7CBA44 CRC64;
MLLFKGTKFV ILPNRNASSL KFLAELLVKE GGMLVNEEKE IDCDTIVLIN DSFITNTNTI
MKNELFFKEF DLDPSTVWNN VNTYKLKCVR ATCISEWLRK SSFQINPELV LSVEDNLEDN
SEDHSGVKFV THSATPLYNY DLITAKLLKN SEKAARQIPE VYSSSQNKSE NSELAGKSME
TEVSNKMGEE VKRTVDISQT TSVPKGNEKL IQALGRLAKR YEMKGDQFRA RGYKLARIGI
EQYPFKIESG AQAQEEISNV GASIAKKIQT LLDNGSLPGL QELFESEKRV DYFTRCHDIG
IYTAKKWEIM GLKSFSEACT IFPEDFTRDW PILFGWSYYE DWLKPIRRDE CEKLASVVQQ
ELHLIDPQMK VEILGSYHRG AEKCGDIDLF FYKAGCDDIS EIGRIMEDLS ISLYRKGYVQ
CFLQLTRKIY KAFNKIIINR LEKCHLKTTP TLQYTARDDN PRKFMLGVKL PDKEKRQFES
ITFVDNYKLK PEDMFMSLNS DRSPCRRMDF FCCKYSELGA ARLQWIGPKE FNRWIRLKAM
HNGLKLTQHG LYDNHNVLLE SFDEQRIFQL LNEDYISPSE RNHVVKKRRK V
//
