DPOE_USTMA
ID DPOE_USTMA Reviewed; 2305 AA.
AC Q4PFV5; A0A0D1CDD6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA polymerase epsilon catalytic subunit A;
DE EC=2.7.7.7 {ECO:0000250|UniProtKB:P15436};
DE AltName: Full=DNA polymerase II subunit A;
GN Name=POL2; ORFNames=UMAG_01008;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase II participates in chromosomal DNA
CC replication. {ECO:0000250}.
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:0000250|UniProtKB:P15436};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P15436};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P15436};
CC -!- SUBUNIT: Heterotetramer. Consists of 4 subunits: POL2, DPB2, DPB3 and
CC DPB4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The CysA-type zinc finger is required for PCNA-binding.
CC {ECO:0000250|UniProtKB:P15436}.
CC -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC formation of polymerase complexes. {ECO:0000250|UniProtKB:P15436}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR EMBL; CM003141; KIS71097.1; -; Genomic_DNA.
DR RefSeq; XP_011386988.1; XM_011388686.1.
DR AlphaFoldDB; Q4PFV5; -.
DR SMR; Q4PFV5; -.
DR STRING; 5270.UM01008P0; -.
DR EnsemblFungi; KIS71097; KIS71097; UMAG_01008.
DR GeneID; 23562144; -.
DR KEGG; uma:UMAG_01008; -.
DR VEuPathDB; FungiDB:UMAG_01008; -.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_1_1; -.
DR InParanoid; Q4PFV5; -.
DR OMA; MLDQCRY; -.
DR OrthoDB; 39650at2759; -.
DR Proteomes; UP000000561; Chromosome 2.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006287; P:base-excision repair, gap-filling; IBA:GO_Central.
DR GO; GO:0045004; P:DNA replication proofreading; IBA:GO_Central.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 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; PTHR10670; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
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; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; DNA replication; DNA-binding; DNA-directed DNA polymerase; Iron;
KW Iron-sulfur; Metal-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..2305
FT /note="DNA polymerase epsilon catalytic subunit A"
FT /id="PRO_0000046465"
FT ZN_FING 2178..2214
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2245..2262
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2245
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2248
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2260
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2262
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
SQ SEQUENCE 2305 AA; 260483 MW; 21402B8B2B56B116 CRC64;
MPSTFGLTSR ASNVRSRGTF RKRGGGPRSG SFKSATEKAI ANAAAQLVKG VEDGSAVEER
FQELKERDEI DEKLGFHRLE QGQTRQAWLV NMHPTLLRDP DHPTGKSGVD FYFIEDDASM
FKATVLYQPY FLVGCRPGTE SSVEEWLRRR YEGLVQSIQR DRKEDLKLPN HLLGNQRLYL
RLTFLNVQDL LSVRKELLPI AKAAQKKLSA VDTYADVLSA ASAAASASLG IQLDSDGHNA
ALDPDDGWTG ARKRAAASAL DPAECLVDIR EYDIPYYLRV AIDQDVRVGL WYDVSFEDGI
VSLNMVKDRV KRADPVVMAF DIETTKQPLK FPDAETDAVM MISYMIDGQG FLITNREIVS
EDIEDFEYTP RDEYEGPFII FNEPDELGVL QRFFSHFREA RPTVVATYNG DLFDFPFIDA
RARAHGLNMM SEIGFAKDSD NEYKSRATAH LDCFRWVQRD SYLPQGSQGL KAVTVAKLGY
DPMELDPELM TPYAIEQPQT LAQYSVSDAV ATYYLYMKYV HPFIFSLCNI IPLNPDEVLR
KGSGTLCETL LMVQAFKGNI IMPNRHEDPV GNTYKGHLLE SETYVGGHVE ALEAGVFRSD
IETDFRVDPA AIQQLIDDLD AALQFSIREE GKLDLDDIEN YDEVKAEIRT MLEVMRDQPV
RKDCPLIYHL DVAAMYPNIM LSYRLQPDSM VSEAMCATCD YNRPGMKCDK RMDWAWRGEY
FPAKRDEVNM IRNALSNETF PPKAAHLARR TYDDLDPNER TALLHKRLGD YSRKVYRKTH
ESKTVIREAV ICQRENPFYI NTVRDFRDRR YEYKGLHKTW KKNLDKADSL NDTIEAKKMI
VLYDSLQLAH KCILNSFYGY VMRKGARWYS MEMAGITCLT GASIIQMAKE LVDRIGRPLE
LDTDGIWCML PGVFPENFNF KVKGGKKFGI SYPCTMLNHL VHEKFTNHQY HELVDKQTGK
YEVRSENSIF FELDGPYKAM ILPSSKEEDK LLKKRYAVFN TDGSLAELKG FEVKRRGELQ
LIKDFQKQIF EKFLLGTTLN ECYAAVAKVA NQWLDVLYSK GSTLHDEELI DLIAENKSMS
KTLQEYGSLK STAITTAKRL AEFLGAQMIK DKGLACKFII SAKPFGAPVT ERAVPVALFN
AEPSVKHYYL KKFLRDNSIT DFDIRNILDW NYYIERFGGV IQKLITIPAA MQKVSNPVPR
VRHPDWLHKR VAAREDKFKQ RKLTDVFRPA AKPTSIEACT TLKPAAAVAS ADIVENEPEV
EEVAPDITVD YSGWVAVMKK KWRKQRLQRA KERKARANGG GAFISSSLGK GTVGSMFSKR
SANMATAVWD IVQICATSRP GEYRLWISID QHLQSLKLKV PRQFYVNFKS QPSESVFLSG
VYRAERLVKT LPRDAPCRHL YRITVDEDVY QEQESHFSNL IHHPNVEGVY EKQLPLDVRA
LIQLGSTCVY GRNSQAPKLS RALDTGFHLQ DLSAPTSVDI SPNHKYLSGG AGIRYFYLYH
AHRDGRHVIS LFSPEGEIKM HIVDSAGLRQ VPNVETMYAD RVAHMRKRGK LEEGSGVFEY
SDTMRVDVRV HTSTTRAFKA ITKELGSLKA AKQGSAMLAL CTSKDQAYYE SHIPSVAEFP
IIKIAAAALE DELPALGWQL YSARRMLQCY LRASNWIRGW IDLASHFDLP LCNMEKDFTI
FGADIDFARR LVKQDMVLWW SPHPRPDLGG REQDIHAQSR WDEQESLEIS HAGAYSTVCL
EVGLVDLAVD SVLQSGSVNE MEGSTSGFAF EGASHNLDEY SRGTVETATI LGDSVLTSAV
FAAVKGMVKA WYTTKRRNRS PYAALLSDNF WRWASSDGSA LFEPALQRFL FGLMKKTLLQ
LLAEFKRLGA SIVYASFNRL FLLTSKPTAA NAMAYSRYLL TAVTSRELFK HVQLDIIHYW
EYLLWMDTAN FGGVIADTDS LVAPTDEQAQ EASAANQVAT FNVEMNWNIQ TFLPLAVQEK
FSVAVGSFIY SLYEYKRRAA LAGEHERTPL RAVVEPNTPA DPVTLHGDGG QVNGDGGKDD
RTALAPAAKF TSDLINHTMT RKLLKHLSEL KSSMQTSSDE INAAIARDED EEYIDMLTTE
HRRMWSFPVL PGSWLTPSNP LLEFIKTTNA VLSLAKDHAI EVSILKRNLL DMIKVREFSP
EAEFRNPCEP FKLPLVICTF CNDDRTLDLC RDADLMPSAA SNGGGAPKWK CAKCQFPYNI
AALEMRLVNT ANAYLESFHL QDLRCNKCGA LKQTNLQPHC ECSGSFGLMV TRKETLKRLK
SLKTIAEFHG LETTAMAVES MLAMV
