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Database: UniProt
Entry: A0A1Y2LPU3_EPING
LinkDB: A0A1Y2LPU3_EPING
Original site: A0A1Y2LPU3_EPING 
ID   A0A1Y2LPU3_EPING        Unreviewed;       785 AA.
AC   A0A1Y2LPU3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=B5807_09555 {ECO:0000313|EMBL:OSS45750.1};
OS   Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX   NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS45750.1, ECO:0000313|Proteomes:UP000193240};
RN   [1] {ECO:0000313|EMBL:OSS45750.1, ECO:0000313|Proteomes:UP000193240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS45750.1,
RC   ECO:0000313|Proteomes:UP000193240};
RA   Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT   "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT   strain isolated from New Zealand.";
RL   Genome Announc. 0:0-0(2017).
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};
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DR   EMBL; KZ107853; OSS45750.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2LPU3; -.
DR   STRING; 105696.A0A1Y2LPU3; -.
DR   InParanoid; A0A1Y2LPU3; -.
DR   OMA; KWHGASA; -.
DR   OrthoDB; 49764at2759; -.
DR   Proteomes; UP000193240; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
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   Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1.
DR   InterPro; IPR036420; BRCT_dom_sf.
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:SF43; DNA POLYMERASE IV; 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   4: Predicted;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193240};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          456..784
FT                   /note="DNA-directed DNA polymerase X"
FT                   /evidence="ECO:0000259|SMART:SM00483"
FT   REGION          264..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        517
FT                   /note="Nucleophile; Schiff-base intermediate with DNA; for
FT                   5'-dRP lyase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622312-50"
SQ   SEQUENCE   785 AA;  87403 MW;  F7C2341720D742E8 CRC64;
     MPNDKLVAKQ AYFEDQKLLD LSNDETSDSN EALDEIESAM AEGERVKLVR QNSNFLGPTP
     KETKADFEAH AARRRAAKRD RNQSFVRSTT APEAELTQSF PVTKLRARQS SHIDNNASSK
     IKRITSLPDM TGLDQTPFYQ RMGVVPRELK NGKNVKPADN IKLEPESRQL LRGKVVYFYP
     NDDVSMVRRT RIHMVIRLGA AWVNKWRDDI THVFVDDASH TYTQLLRHLN KAGLPRKVVL
     AKFEPYVPQC IHFGSLMDPS ATRYSVKGAP QQSQASQKPE VSTVVSQTSG ESQTSLQIKP
     TRKQKDALSS RKTDSLPGES TSRQSAMDKA PENSTVERVE DSFAMPSSDS HNEPPEVEVH
     DAEFGYELQQ AIRETKAIAH LPIDDDEDEG SIAPSMVDAD GTDSGTDGEP SEIPSKSRKK
     NFANEKTTST GPTRKAFDQS GFQCMDPSTG GYSSQNPNAH TIKILEEMGR YHDQMQDQWR
     TLAYRRGVTT LKKQPTKIST AKQAAALPFI GTRLAEKIEE IVLTSRLRKL DNTKDDPLAE
     VLRLFLGVYG AGLVQANKWI QTGHRTLDDL QAKAKLTDSQ KIGIEHYADF NARIPRAEVA
     AHGAFVKNAL LEIDPAFEAT VMGSYRRRAA NSGDIDMLIS RPGASLAQLR TVVFNVLVPT
     LSKAGFLKVA LAASHSSDAS GTKWHGASCL PGSTVWRRID LLLVPEAEMG AALIYFTGND
     IFNRSMRLLA RKKGMRLNQK GLYKDVKRGW RGEKLNEGTL VEGRSERRIF EVLGVPWREP
     GERIC
//
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