ID A0A428P002_9HYPO Unreviewed; 629 AA.
AC A0A428P002;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU366014};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU366014};
GN ORFNames=CEP54_013921 {ECO:0000313|EMBL:RSL46291.1};
OS Fusarium duplospermum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL46291.1, ECO:0000313|Proteomes:UP000288168};
RN [1] {ECO:0000313|EMBL:RSL46291.1, ECO:0000313|Proteomes:UP000288168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL46291.1,
RC ECO:0000313|Proteomes:UP000288168};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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|ARBA:ARBA00024632,
CC 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:RSL46291.1}.
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DR EMBL; NKCI01000241; RSL46291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428P002; -.
DR STRING; 1325734.A0A428P002; -.
DR Proteomes; UP000288168; 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; 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; 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 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.
DR PROSITE; PS50172; BRCT; 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};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU366014}; Nucleus {ECO:0000256|RuleBase:RU366014};
KW Reference proteome {ECO:0000313|Proteomes:UP000288168};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366014}.
FT DOMAIN 153..178
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 70908 MW; 72E38E1086CEDA21 CRC64;
MAVNQTSPQS VSNHSDTSVA NRPELSSTSP IELDQSDASS FVMAPDFPRI FLLSTHLNVN
ELHELENRTP TLTYDINEAQ VVVGNISRAE RAKFELRKAK LETVPIERPQ TREDESQQTY
ITTGTQERGP EDPPSPKRRR VAEPTTPDDV DIIKVVKLAW LKNSFEHGTV LPVEKYLLYQ
GKKVYPKDAR PTLATVQHSS TTSILERAKQ DQQAQPASGS PRDRFKHRSH PPETSTEHVP
SLLHQTTSEH DITLPPVPDF LETPYSCQRP TPMNPPNEAF VEALVEVRTI RQLQGDEVGV
RAYSTSIATV SAYPRGLQNT QEVERLPGCG AKIAELWREW NETGGLKEVR KADADPMVSV
LRLFYNIWGV GDTTAREFYR KGWRDLNDLV DFTWDSLSRS QQVGVKFYDE FLLKIPRHEV
EFIGAVILKH AREIDPGFEM AITGGYRRGK LQCGDVDVIL SHRDEDKTLR FVGKLIKSLE
QAHFITHNLV MSLHNSERGQ RPVSWKGEGV SGSGFDTLDK AMAAWQDPNK EDAPHRRVDI
IISPWKTVGC ALLGWSGGTT FQRDLRRYCK KVKGLKFDSS GIRRRSDGMW VNLEKGPAGD
GAPDMETAER RVFEGLGLTW RPPEERCTG
//
