DPOE_EMENI
ID DPOE_EMENI Reviewed; 2207 AA.
AC O93845; C8VIQ6; Q5B8R3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 120.
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; Synonyms=nimP; ORFNames=AN3067;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA James S.W., Crawford G.E., Wexler A.N.;
RT "nimP DNA pol epsilon gene of Aspergillus nidulans.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AF019254; AAD01637.1; -; Genomic_DNA.
DR EMBL; AACD01000051; EAA63638.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF83469.1; -; Genomic_DNA.
DR RefSeq; XP_660671.1; XM_655579.1.
DR AlphaFoldDB; O93845; -.
DR SMR; O93845; -.
DR STRING; 162425.CADANIAP00010012; -.
DR PRIDE; O93845; -.
DR EnsemblFungi; CBF83469; CBF83469; ANIA_03067.
DR EnsemblFungi; EAA63638; EAA63638; AN3067.2.
DR GeneID; 2874392; -.
DR KEGG; ani:AN3067.2; -.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_1_1; -.
DR InParanoid; O93845; -.
DR OMA; MLDQCRY; -.
DR OrthoDB; 39650at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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..2207
FT /note="DNA polymerase epsilon catalytic subunit A"
FT /id="PRO_0000046462"
FT ZN_FING 2075..2116
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1934..1961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2147..2164
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2075
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2078
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2147
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2150
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2164
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT CONFLICT 1368
FT /note="F -> N (in Ref. 1; AAD01637)"
FT /evidence="ECO:0000305"
FT CONFLICT 1607
FT /note="V -> G (in Ref. 1; AAD01637)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2207 AA; 252726 MW; C3615E5299DCF12A CRC64;
MPSRKPSKYG NKFRSGAASF NPKRTKTVEF SSLRSSEATS QDEKFEAIRL ANSIDESLGF
PRFEAGEKRV GWLINMHSTS IEDPNVPGGR AGVDYYFLDD DGGSFKATVE YDPYFLIAVK
TGHEAEVEEW CRRMFEGLIK KIKRVVKEDL KLPNHLLGHR RTFLQLDFAN VSHLLEVRKT
LLPLAEKNRK NARPNGTTNA SDFIIDIREY DVPYHVRVAI DKDIRIGKWY TVEATHGIIS
LTCLEERLTR ADPVVLAFDI ETTKLPLKFP DSVIDQIMMI SYMIDGQGFL ITNREIVSED
IDDFEYTPKP EYSGPFMIFN EPNERAVIER FFEHIKEAKP TVIATYNGDF FDWPFVEARA
SVLGIDMYKE IGFRKNSEDI YQSDHCAHMD CFAWVNRDSY LPQGSRGLKA VTVAKLGYDP
DELDPELMTP YASERPQTLA EYSVSDAVAT YYLYMKYIHP FIFSLCTILP LNPDDTLRKG
TGTLCEMLLM VQAYKGNIVL PNKHKDPPEA FYEGHLLESE TYVGGHVESI EAGVFRSDIP
VPFNIDPTAV DELLRDLDAA LKFSIEVEEK KSLDDVTNYE EVKGQIAKLL TDLRENPHRN
EVPFIYHLDV ASMYPNIMIT NRLQPDSLIQ ESNCAACDFN RPGKTCDRRL PWAWRGEFLP
AKRDEYNMIR QAVQNERFPG RTKKSPMRAF TELSAEEQAA IVKKRLQDYS KKIYHKIHDS
KTMVREAIIC QRENPFYVDT VRSFRDRRYD FKGKQKVWKG KTESLKSSGA PAAEIEEAKK
MIVLYDSLQL AHKVILNSFY GYVMRKGSRW YSMEMAGVTC LTGARIIQMA RELVERIGRP
LELDTDGIWC MLPGTFPENF SFTLKNGKKL GISYPCVMLN HLVHGSYTNH QYQSLANPAT
FRYETHSENS IFFEVDGPYR AMILPTSKEE DKNLKKRYAV FNDDGSLAEL KGFEVKRRGE
LKLIKIFQTQ IFKFFLEGTT LAETYAAVAR VADRWLDVLY EHGATLADEE LIELISENRS
MTKTLEEYGN QKSTSITTAR RLAEFLGEQM VKDKGLNCKY IISARPRNTP VTERAIPVTI
FSAEDSIKRH FLRKWLKDDP GDMDPRSVID WDYYLERLGS VVQKLITIPA ALQKIRNPVP
RVAHPEWLQR RINKQDDRFK QVKMTDMFGK SEKNPLSDIS TNIIDHRVQH ADNLDEAMAD
SMEKLKSSSP QKASGKRKHP ENQTKTSLDP FASLPAKMPS IDDDYVGFLK YQKQKWKIQK
QARLRRRQLF GERANTGGDS LSHLFRNQAE LLYISTWQVL QLAETSRPGI VRAFVLIDRK
IHALTIKVPR CVYINLKQDS LPDVEVPECE VEKVNHTLPN GHPSVHLFKL TLSEETFLRE
ADKIHVLLQH PSVEGVYERN IPLNLRAVLK LGSICTFDEA QRGVLGDGLE RGFDLSTLCR
TSSEQQYLQD SPLAYHFLYH VSSGEKQIFA IFSSTKNEAH IVILNRARDV QGLPNVDKIY
SELLARKLQG QGDQAEGAFQ YQEKIHFRTT QITTRRKAYL EVSDLIKKLR NDESLPAIMI
IQSQQRSRLC HDIPILKEYP ILSVKPEVSD MNLPPLGWQS FIAKRLVTHY LYLSSWVQHL
TMLARYGDVP LCNLESDDPR FLIDISYARR LQQNNVVLWW SSTAKPDHAG YEKDDITGPL
ERVGMPCVNV PGSYTTVCVE LEVRNLAINT ILTSSIINEA EGADSLLAPS DPSAESSGSG
VLYSEKAFAS AGAVVLREMV KHWWSEACQG NNMADIMVQH LIRWVESPAS CLYDRSLHQY
VRMLSRKSFQ QLMAEFRRVG SNVVFASPTR LLLQTSKTEV GNAYAYSQYV LKSIRANPSF
HFIDLDIKEY WDYLVWYDEY NYGGKGCQEV AETEEQPLET VMHWQLSRFL PTPMQTIFHD
WVVEYIELMH SFKRPESDDS STPRLTQIPI GQPEPGQENE ELSAALSDRF SKPLKKQISG
LIRRQREELL HPELASDYVF PILPGVLTDP NEEKRNPVLE LVKLLMQVLS LSKTTALETR
LLRRELLALF EVREFSKEGR FENPGSSLKI PELTCSACCL IRDLDLCRDE DVLPERGSGS
GPDSATSSRP WCCPFCQTEY DRLAQEEMLI GQVWGMVVAW QTQDLKCSKC GTLKISEFME
HCSCSGQWTE TMNRADIEKR LKVLESVAKF HELKLLQVVV EEVLSQT
