DPOE_ASPFU
ID DPOE_ASPFU Reviewed; 2230 AA.
AC Q4WXH8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=AFUA_3G09560;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000002; EAL92625.1; -; Genomic_DNA.
DR RefSeq; XP_754663.1; XM_749570.1.
DR AlphaFoldDB; Q4WXH8; -.
DR SMR; Q4WXH8; -.
DR STRING; 746128.CADAFUBP00003880; -.
DR EnsemblFungi; EAL92625; EAL92625; AFUA_3G09560.
DR GeneID; 3511701; -.
DR KEGG; afm:AFUA_3G09560; -.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_1_1; -.
DR InParanoid; Q4WXH8; -.
DR OMA; MLDQCRY; -.
DR OrthoDB; 39650at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
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..2230
FT /note="DNA polymerase epsilon catalytic subunit A"
FT /id="PRO_0000046458"
FT ZN_FING 2101..2139
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2170..2187
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2170
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2173
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2185
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2187
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
SQ SEQUENCE 2230 AA; 255652 MW; 43721C297919429F CRC64;
MPTRQPSKYG NKFRSSSASF KPKRTKTVEF SSLRSTEATS QDEKFEAIRL ANSIDEALGF
PRFESGEKRV GWLINMHSTS IEDPNVPGGR AGVDYYFLED GGGSFKATVE YDPYFLLAVK
KGHEAEVEEW CRRMFEGLIK TIKRVEKEDL QLPNHLLGHR RTFLQLNFAN VSHLLDVRKT
LLPLAEKNKK NVNVMDTYAE ISSANAGFDL FDDELINESR PNSNMNASDY IIDIREYDVP
YHVRVAIDKD IRIGKWYTVE AKHGVISLTC LEERLQRADP VILAFDIETT KLPLKFPDSV
IDQIMMISYM IDGQGFLITN REIVSEDIRD FEYTPKPEYS GPFMIFNEPN ERSVIERFFE
HIKEAKPTVI ATYNGDFFDW PFVEARASVL GIDMYKEIGF RKNSEDIYQS DHCVHMDCFA
WVNRDSYLPQ GSRGLKAVTV AKLGYDPDEL DPELMTPYAS ERPQTLAEYS VSDAVATYYL
YMKYVHPFIF SLCTIIPLNP DDTLRKGTGT LCEMLLMVQA YKGEIVLPNK HKDPPESFYE
GHLLESETYV GGHVESIEAG VFRSDIPVTF NIDTTAIDEL LRDLDAALKF SIEVEEKKSM
DDVVNYEDVK AQIAERLVNL REKPHRDEVP SIYHLDVASM YPNIMITNRL QPDSMIQESD
CAACDFNRPG KTCDRRLPWA WRGEFLPAKR DEYNMIRQAV ANELFPGRTK NSPMRSFGEM
SAEEQAAIIK KRLQDYSKKI YHKIHDSKTI VREAIICQRE NPFYVDTVRS FRDRRYDFKG
KQKVWKGKTE ALKAAGASAA EIEEAKKMIV LFDSLQLAHK VILNSFYGYV MRKGSRWYSM
EMAGVTCLTG AHIIQMAREL VERIGRPLEL DTDGIWCMLP GSFPEDFSFT LKNGKKLGIS
YPCVMLNHLV HGKYTNHQYQ TLVDPKTFRY ETHSDNSIFF EVDGPYKAMI LPTSKEEDKN
LKKRYAVFNH DGSLAELKGF EVKRRGELKL IKIFQTQIFR FFLEGSTLEE TYAAVARVAD
RWLDVLYDHG ATLADEELIE LISENRSMTK TLEEYGNQKS TSITTARRLA EFLGEQMVKD
KGLNCKYIIS AKPKNTPVTE RAIPVTIFSA EEPVKRFFLR KWLKDDPGDM DPRSVIDWDY
YLERLGSVVQ KLITIPAALQ KVRNPVPRVA HPDWLQRRIN MKEDKFKQTK MTDMFGKTEK
NPLSNISTNI LDHRVQHHGD IGEAVANSTQ KLKSSPNGKI SQKRKHPEGL TKTLLDPFAS
LPAIMPSLND DYVGFLKYQK QKWKIQKQAR ARRRQLFGER VNVATDSLSN LFRNQAELLY
INTWQILQLC ETGRPGLVRA FVLIDRKIHA LTIKVPRQIY VNLKRDSLPD VDVPDCEVEK
VNHTLPNGHP SVHLFKLTLS EDTYLRETDK IDALLQHPSI EGVYEKNIPL SVRAVLKLGS
VCTFDEEQRG VLGEGLDRGF NLSTLCHTTP DEPYLLNSPL VYHYLYHVLS GDRQIFALFS
TTKSEAHIVI LNRTRDVQGL PNVDKIYAEL RARTMENMGG DQSQNAFEYQ EKIHFKTTQV
TTRRKAYLEI GDLIKKLKGE ETQPVIMVIQ SHQRHRLCHD IPILKEYPVL PVKPEVSDMD
LPPLGWQSFI AKRLVTHYLY LASWIHHLTM LARYGDVPLC NLENDDPRYL IDISYARRLQ
QNNVVLWWSN GPRPDHAGYE KDDVTGSLER VSMPSVNVPS AYNTVCIELE VRNLSINTIL
TSSIINELEG ADTLLASSEP SADANGSGVL YSEKAFASAG AVVLREMVKH WWSEACEGNN
MADIMVQHLI RWVESPVSCL YDRSLHDYVR MLSRKSFQRL MAEFRRVGSN VIFASPTRLL
LQTTKTEVGN AYAYSQYVLK SIRANASFHF IDLEIKEYWD YLVWYDEYNY GGKGCRKVTG
SEDQELETVM HWQLSRFLPA PMQTIFHDWV VEYIELMHGL KRTDSDDSST PRLTQLPVGN
HNEDNDEITS ILAEKFSKPL KKQISGLIRR QRDELLHPEL ASDYVFPVLP GVLVDPNNDK
RNPVLELVKL LMQVLSLSKT TTLETRLLRR ELLAMFEVRE FSKEGRFENP GASLKLPELS
CNACCLIRDL DLCRDEDVLP EMGSDPNKAA PKPWRCPFCQ TEYDRLAQEE ALIGQVQGLI
VGWQTQDLKC SKCGGLKISD FMEHCSCSGH WVETMDRNEV EKKLLLLSSV SKFHGLKLLE
SVVQGVLEQM
