ID A0A2S4PPC2_9PEZI Unreviewed; 2221 AA.
AC A0A2S4PPC2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN ORFNames=EPUL_004023 {ECO:0000313|EMBL:POS83854.1};
OS Erysiphe pulchra.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=225359 {ECO:0000313|EMBL:POS83854.1, ECO:0000313|Proteomes:UP000237438};
RN [1] {ECO:0000313|EMBL:POS83854.1, ECO:0000313|Proteomes:UP000237438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cflorida {ECO:0000313|EMBL:POS83854.1};
RA Wadl P.A., Mack B.M., Moore G., Beltz S.B.;
RT "Development of genomic resources for the powdery mildew, Erysiphe
RT pulchra.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase II participates in chromosomal DNA
CC replication. {ECO:0000256|RuleBase:RU365029}.
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:RU365029};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU365029};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365029}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU365029}.
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:POS83854.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PEDP01001312; POS83854.1; -; Genomic_DNA.
DR STRING; 225359.A0A2S4PPC2; -.
DR OrthoDB; 5475218at2759; -.
DR Proteomes; UP000237438; Unassembled WGS sequence.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd05779; DNA_polB_epsilon_exo; 1.
DR CDD; cd05535; POLBc_epsilon; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR013697; DNA_pol_e_suA_C.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR029703; POL2.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10670:SF0; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT 1; 1.
DR PANTHER; PTHR10670; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1.
DR Pfam; PF00136; DNA_pol_B; 2.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08490; DUF1744; 1.
DR SMART; SM01159; DUF1744; 1.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU365029};
KW DNA replication {ECO:0000256|RuleBase:RU365029};
KW DNA-binding {ECO:0000256|RuleBase:RU365029};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU365029};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365029};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU365029};
KW Metal-binding {ECO:0000256|RuleBase:RU365029};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU365029};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365029};
KW Reference proteome {ECO:0000313|Proteomes:UP000237438};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365029};
KW Zinc {ECO:0000256|RuleBase:RU365029};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU365029}.
FT DOMAIN 1513..1907
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
SQ SEQUENCE 2221 AA; 255449 MW; FEB9F9432B2407A0 CRC64;
MPNRVYGNGG KQAYQGPRGL KKFSATNRNE KTSVHEKRDA VKLADSIDEA HGFMRYESGK
KKIGWLVNIK STSIEDDKVP EGRAAVDCYL IEEDGGTFKA TIQYEPYFLV AVRRGYETEA
EEWLKRIPGG GVVKTIKKVE KEDLKMPNHL MGYRRSFFEL RFNNIGNLLA ARKDIMPIVE
RNKKTVSMMD MYAEVASANN AVDLYQEDHD DRRLHVSTID AGDLIVDIRE WDVPYHVRVM
IDMGIRTGKW YSVEVKHGNT NLVCLEERLQ RADPVVMAYD IETTKLPLKF PDASIDQIMM
ISYMIDGQGF LITNREIVAQ EIDDFEYTPK PEYEGPFIIF NEPDEKSAIE RFFLHIKESR
PTVIATYNGD FFDWPFVDAR ASINGIDMYK EIGWRKSQED QYCCDYSAHM DCFHWVNRDS
YLPQGSRGLK AVTTAKLGYD PDELDPELML RYASERPQVL AEYSVSDAVA TYYLYMKYVH
PFIFSLCTII PLGPDAVLRK GTGTLCEMLL MVQAYEKEIV LPNKHVSPKE SFWEGHLLES
ETYVGGHVES IEAGVFRADI PVQFSIDTSA IDELLLDLDL ALKFCIEIEE NKSLDNVVNY
EDVKKQITDR LMILKENANE SDYPLIYHLD VASMYPNIMT TNRLQPDSMI DESSCAACDF
NRPGKKCDRR LPWSWRGEFL PPKRDEYNMI KSSLENERFP GKFPNSPFRT FQDLSTTEQA
DLIRKRLQIY SQKIYHKIRE TKTIEREAII CQRENPFYID TVRAFRDRRY EYKGKQKDWK
IKTETLKASG APSSDIENAE KMIVLFDSLQ LAHKVILNSF YGYVMRKGSR WYSMEMAGVT
CLTGAHIIQV ARQLIERIGR PLELDTDGIW CMLPAKFPEN YSFELNSGKK LGFSYPCVML
NYLIHGKFTN HQYQTLIEPK SFKYETHSEN TIFFEVDGPY RAMILPTSKE EDKNLKKRYA
VFNHDGSLAE LKGFEVKRRG ELKLIKIFQQ SIFKFFLEGQ TLAATYEAVA RVANQWLDVL
HSKGETLVDE ELIDLICENR SMSKPLDQYG NQKSTSITTA KRLADFLGDQ MVKDKGLNCK
YIICSRPKNA PVTERAIPVA IFSAEPMTKK TYLSRWLKET PTNLDPKALI DWEYYIERLG
SVIQKLITIP AALQKISNPV PRVSHPEWLQ RRLNIKDDRL KQRKLTDHFK ASIPGELNNE
FSRMKDIEDF GVKLLTPKTI GIALSQASKK QLKRKSPEPL ISVSTNPYAS LPEKMPDPTT
DYRGFLDYQK QKWKIQKHQR IRRRHLFGET KINAQNNIGV QFRNQAEITF RNTWHILQLS
ESTSPGVVSA FVLIDSKIHK LMINVPRQIY LNLKEKELPQ IEIDGCDAQK VTHTLPNGHP
SVHLFKLTMS EKTYIDEAQK LSLLFNHPSI EGVYERQISP STRAILQLGN LSTINEAKSG
VLGKGLEDGF DLSGLKTVTT KIPYLSISNI TYLYLYHITF GDRQIFALFS TAKDLAHVIV
LRKGRDSDKE FPNFGKIYVE ALEKKRLEAE TQVQEDNFIY QDKLQFKISQ VTFRRKALIE
VGDLLKKVRK DETKPFVLVI QSPQRRLLVH EMPILSELPL LSMDYIISDG NLPSLGWQTY
FAKRLVNRYL SLSSWIQHLT ELAKYGDIPL CNLERDDPKF LIDIAYARRL QKSNVVLWWS
AGPRPDHAGY EKDDILSPLE TIQVPNVNNP GAYSSVCIDI ELRNLTVNTI LTSSLINELE
GSGLTSFNSV TPSNDVTGDG NSILYSDEAF ATAGISVLRE MVKAWWAEAC KGSGMADIMV
QHLVRWVGSP DSFLYDRKLH YYVQFMSLRA FRQLMADFRR VGSHIIFAST NRLLLQTTKS
EVGNAYAFSQ YIIKAIKAKP HFYFLDLEIS EYWDYLIWYD EFNYGGKACT KVVGAENQEL
DCVMHWQLSK FLPIPLQSIF HDWIVEFIEL MHKYKVNLSS EGVNTTFSTS FFIKNLSEEL
ESKNILGKSF EKPIKRQITS LIRKQKEEIL HPQLASDYTF PNLPGSYLNL TNPVLELVKS
LMHILSLDSN ITLEARLLRK ELLALFDIRE FSTEANFRNP SQSLKLAQVI CDNCTLSRDL
DFCRDEDLIL SGSIDNKTPN NSYAWKCSFC DVEYNRLSIE ERLIAMVYGM YTEWCGQDLK
CIKCGALRVN DFMEHCACSG TWGEILQRDK VVTKLEVLYR VAKAYDLKML IDVVSEITAG
L
//
