ID A0A0A2VE68_BEABA Unreviewed; 587 AA.
AC A0A0A2VE68;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU366014};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU366014};
GN ORFNames=BBAD15_g8907 {ECO:0000313|EMBL:KGQ05853.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ05853.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ05853.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ05853.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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=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|RuleBase:RU366014};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU366014}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family.
CC {ECO:0000256|RuleBase:RU366014}.
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:KGQ05853.1}.
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DR EMBL; ANFO01000909; KGQ05853.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VE68; -.
DR STRING; 1245745.A0A0A2VE68; -.
DR HOGENOM; CLU_008698_4_1_1; -.
DR Proteomes; UP000030106; 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: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; 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; IPR002054; DNA-dir_DNA_pol_X.
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; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR PANTHER; PTHR11276:SF29; DNA POLYMERASE TYPE-X FAMILY PROTEIN POL4; 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 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.
DR PROSITE; PS50172; BRCT; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|RuleBase:RU366014};
KW DNA repair {ECO:0000256|RuleBase:RU366014};
KW DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU366014};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU366014}; Nucleus {ECO:0000256|RuleBase:RU366014};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366014}.
FT DOMAIN 103..128
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 69..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 66055 MW; 9087B15C1BAC401F CRC64;
MSLSLPVIFL LQTNLKPAEL HELGKSIPTL TYDVHEAEVV LGRVSHKQRA QFELRRLKLN
TDSIEAGAMG HEAAEDGSPA GRYPKRQKLE LPASSSEADS SVVRVVHLSW LTESLEKHEL
LPMSSYIVYE GRKRTHSTSM LVDSQVDSGK TTTSGILERV ADEKSGLGER LTSQIEGGEK
VEQHMTKYPP AGAIAKPGLT RESTSEHDIQ LPLIPYHLHT TYSCQRPTPI NPPNASFIDE
LKSIRTIRLL QGDKIGKPQG TAFTLIPEAL ISMLDSNYLA EVSRLPGCGS KIAELYQEWH
ATGQTEEMRE SKADPKIDVL RIFYDIWGVG DTTARHFYQK GWRDLDDIVE HGWKSLSRVQ
QIGVKYYEEF QKKIGRDEVA RIADVILDHA HRLDQAYELI VVGGYRRGRE ENGDVDVILS
HKEEHKTSRL VEKLVLSIEN DNYITHTLSL STRNSERGQV PLQWKGEGST SGAGFDTLDK
AMVVWLDPKD AKALHRRVDI IVSPWKTVGC AILGWSGETT FQRDLRRYCK KEKGLKFDSS
GIRNRANGSW VDLERGDASA DSMEEAERRV FDGLNIPWRP PWDRCTG
//
