ID A0A0D2FIM0_9EURO Unreviewed; 1107 AA.
AC A0A0D2FIM0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=Z517_01905 {ECO:0000313|EMBL:KIW86507.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW86507.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW86507.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW86507.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:RU000442};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR EMBL; KN846969; KIW86507.1; -; Genomic_DNA.
DR RefSeq; XP_013290315.1; XM_013434861.1.
DR AlphaFoldDB; A0A0D2FIM0; -.
DR STRING; 1442368.A0A0D2FIM0; -.
DR GeneID; 25301395; -.
DR VEuPathDB; FungiDB:Z517_01905; -.
DR HOGENOM; CLU_000203_2_0_1; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000053029; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd05777; DNA_polB_delta_exo; 1.
DR CDD; cd05533; POLBc_delta; 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; 1.10.287.690; Helix hairpin bin; 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; IPR017964; DNA-dir_DNA_pol_B_CS.
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; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF14260; zf-C4pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU000442};
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000442}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000053029};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 176..475
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 539..970
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1008..1082
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1107 AA; 125831 MW; CD4D8402A0D39A24 CRC64;
MPGRVLDQPK KRVLTDTTNT HNVLKSPPSA KKRKLNGDRP NVSFHSSQPG PNRFKSKLGS
SQPKSQFETE VLEKMTQDIA GLKENNSEKD QQWERPSLDN FNADSNPLRF QQIEIEEGTL
HGGKIALKMF GVSETGHSIL LHVTDFLHYL YVAAPVNFQR SDVEGYKAYL EAQLAQHQPA
IHSVQMVLRE NLFGFQGNQK SPYLKITVTD PKFINRLRTA IEDGHANYKG MWKGVESKIL
TFDNIQYVLR FMIDTGITGM SWVEVPPQKY HVLPQHDRQS NCQIEAYCHY RDLVAHGHDG
EWAKMAPLRI LSFDIECAGR KGIFPEANQD PVIQIANVVT KYGESKPFIR NVFVLDTCSL
IVNTKIYEHR SESDMLMAWR QFLEEVDPDV IIGYNIANFD FPYLLDRAKH LKLTKFPYWS
RLKSVASHAK DTNFSSKQMG NRDTKSTNTN GRIQLDLLQL VQRDHQLRSY TLNSVCAHFL
GEQKEDVHHT MITELYNGTP DSRRRLAVYC LKDAYLPQRL MDKLMCLVNY TEMARVTGVP
FNYLLARGQQ VKFISQLFRK ALEQQLVIPN LRNESTDEQY EGATVIEPIR GYYDVPVATL
DFASLYPSII QAHNLCYTTL LNKNIIEKLN LKKDEDYILT PNGDLFCTAK VRKGLLSQIL
EELLSARKRA KKELAVETDP FKKAVLNGRQ LALKISANSV YGITGATVGK LPCLAIASST
TAYGRQMIEK TKHEVEQKYT MANGYSHDAQ VIYGDTDSVM VKFGEKDLRK TMELGEEAAN
FVSSKFIKPI KLEFEKVYFP YLLINKKRYA GLYWTNPEKH DKMDSKGIET VRRDNCRLVQ
VVIETVLKKI LIDRDLDGAQ DYVKETIANL LQNKIDLSML VITKALSKSD YTAKQAHVEL
AERMKKRDAG SAPALGDRVA YVMVKGASGS KNYENSEDPI YVLENNVPID TKYYLDNQLA
NPLGRIFEPI LGERRANSLL AGDHTRSISV AAPTLGGLMK FAKKTQTCMG CKKPLVSAQE
SKGAVCENCR PRIGELYTKQ IKKVGELEVR FARLWTQCQR CQGSMHSEVL CSSRDCPIFY
MRMKARKEVE ESGKELARFD ADVGAIW
//