DPOE2_ARATH
ID DPOE2_ARATH Reviewed; 2138 AA.
AC F4IFN6; Q9ZVC8;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=DNA polymerase epsilon catalytic subunit B;
DE EC=2.7.7.7 {ECO:0000250|UniProtKB:P15436};
DE AltName: Full=DNA polymerase 2 b;
DE Short=AtPOL2b;
DE AltName: Full=DNA polymerase II subunit b;
DE AltName: Full=Protein TILTED 2;
GN Name=POL2B; Synonyms=TIL2; OrderedLocusNames=At2g27120; ORFNames=T20P8.17;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=16278345; DOI=10.1105/tpc.105.036889;
RA Jenik P.D., Jurkuta R.E.J., Barton M.K.;
RT "Interactions between the cell cycle and embryonic patterning in
RT Arabidopsis uncovered by a mutation in DNA polymerase epsilon.";
RL Plant Cell 17:3362-3377(2005).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16212602; DOI=10.1111/j.1365-313x.2005.02521.x;
RA Ronceret A., Guilleminot J., Lincker F., Gadea-Vacas J., Delorme V.,
RA Bechtold N., Pelletier G., Delseny M., Chaboute M.-E., Devic M.;
RT "Genetic analysis of two Arabidopsis DNA polymerase epsilon subunits during
RT early embryogenesis.";
RL Plant J. 44:223-236(2005).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19947980; DOI=10.1111/j.1365-313x.2009.04093.x;
RA del Olmo I., Lopez-Gonzalez L., Martin-Trillo M.M., Martinez-Zapater J.M.,
RA Pineiro M., Jarillo J.A.;
RT "EARLY IN SHORT DAYS 7 (ESD7) encodes the catalytic subunit of DNA
RT polymerase epsilon and is required for flowering repression through a
RT mechanism involving epigenetic gene silencing.";
RL Plant J. 61:623-636(2010).
CC -!- FUNCTION: DNA polymerase II, which participates in chromosomal DNA
CC replication (By similarity). Involved in the determination of cell fate
CC during plant embryogenesis. Contributes to the flowering time
CC repression. {ECO:0000250, ECO:0000269|PubMed:16212602,
CC ECO:0000269|PubMed:16278345, ECO:0000269|PubMed:19947980}.
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,
CC ECO:0000250|UniProtKB:P15436};
CC -!- SUBUNIT: Heterotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed at low levels in inflorescence
CC (floral meristem and flowers until anthesis), and, to a lower extent,
CC in seeds. {ECO:0000269|PubMed:16278345}.
CC -!- DOMAIN: The DNA polymerase activity domain resides in the N-terminal
CC half of the protein, while the C-terminus is necessary for maintenance
CC of the complex. {ECO:0000250|UniProtKB:P21951}.
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 -!- DISRUPTION PHENOTYPE: No visible effects. When associated with
CC heterozygote POL2A disruption; lethal, with sporophytic embryo-
CC defective with an arrest at the globular stage during embryo
CC development. When associated with esd7-1 mutation of POL2A; very early
CC flowering. {ECO:0000269|PubMed:16212602, ECO:0000269|PubMed:16278345,
CC ECO:0000269|PubMed:19947980}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC77870.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005623; AAC77870.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07940.1; -; Genomic_DNA.
DR PIR; A84669; A84669.
DR RefSeq; NP_180280.2; NM_128270.3.
DR AlphaFoldDB; F4IFN6; -.
DR SMR; F4IFN6; -.
DR STRING; 3702.AT2G27120.1; -.
DR iPTMnet; F4IFN6; -.
DR PaxDb; F4IFN6; -.
DR PRIDE; F4IFN6; -.
DR EnsemblPlants; AT2G27120.1; AT2G27120.1; AT2G27120.
DR GeneID; 817254; -.
DR Gramene; AT2G27120.1; AT2G27120.1; AT2G27120.
DR KEGG; ath:AT2G27120; -.
DR Araport; AT2G27120; -.
DR TAIR; locus:2059314; AT2G27120.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_1_1; -.
DR InParanoid; F4IFN6; -.
DR PRO; PR:F4IFN6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IFN6; baseline and differential.
DR Genevisible; F4IFN6; AT.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; ISS:UniProtKB.
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 2: Evidence at transcript level;
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..2138
FT /note="DNA polymerase epsilon catalytic subunit B"
FT /id="PRO_0000420241"
FT ZN_FING 2015..2045
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MOTIF 1224..1231
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 2076..2093
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MOTIF 2107..2114
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT BINDING 2015
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2018
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2040
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2045
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2076
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2079
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2091
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2093
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
SQ SEQUENCE 2138 AA; 244993 MW; DC8C343A54645B23 CRC64;
MSGRRCDRRL NVQKVSAADE LETKLGFGLF SQGETRLGWL LTFASSSWED ADTGKTFSCV
DLFFVTQDGS SFKTKYKFRP YLYAATKDNM ELEVEAYLRR RYERQVADIQ IVHKEDLYLK
NHLSGLQKKY LKVSFDTVQQ LVEVKRDLLH IVERNLAKFN ALEAYESILS GKREQRPQDC
LDSVVDLREY DVPYHVRFAI DNDVRSGQWY NVSISSTDVI LEKRTDLLQR AEVRVCAFDI
ETVKLPLKFP DAEYDQIMMI SYMVDGQGFL ITNRECVGKD IEDLEYTPKP EFEGYFKVTN
VTNEVELLRK WFSHMQELKP GIYVTYNGDF FDWPFIERRA SHHGIKMNEE LGFRCDQNQG
ECRAKFVCHL DCFSWVKRDS YLPQGSQGLK AVTKVKLGYD PLEVNPEDMV RFAMEKPQTM
ASYSVSDAVA TYYLYMTYVH PFVFSLATII PMVPDEVLRK GSGTLCEMLL MVEAYKANVV
CPNKNQADPE KFYQGKLLES ETYIGGHVEC LQSGVFRSDI PTSFKLDASA YQQLIDNLGR
DLEYAITVEG KMRMDSVSNF DEVKEVIREK LEKLRDDPIR EEGPLIYHLD VAAMYPNIIL
TNRLQPPSIV TDEVCTACDF NGPEKTCLRK LEWVWRGVTF KGNKSEYYHL KKQIESESVD
AGANMQSSKP FLDLPKVEQQ SKLKERLKKY CQKAYSRVLD KPITEVREAG ICMRENPFYV
DTVRSFRDRR YEYKTLNKVW KGKLSEAKAS GNLIKIQEAH DMVVVYDSLQ LAHKCILNSF
YGYVMRKGAR WYSMEMAGVV TYTGAKIIQN ARLLIERIGK PLELDTDGIW CALPGSFPEN
FTFKTIDMKK FTISYPCVIL NVDVAKNNSN DQYQTLVDPV RKTYNSRSEC SIEFEVDGPY
KAMIIPASKE EGILIKKRYA VFNHDGTIAE LKGFEMKRRG ELKLIKVFQA ELFDKFLHGS
TLEECYSAVA AVANRWLDLL EGQGKDIADS ELLDYISESS TMSKSLADYG QQKSCAVTTA
KRLADFLGDT MVKDKGLRCQ YIVAREPEGT PVSERAVPVA IFQTDDPEKK FYLQKWCKIS
SYTGIRSIID WMYYKQRLHS AIQKVITIPA AMQKVANPVL RVRHPYWLEK KVCDKFRQGK
IVDMFSSANK DHSTTQDNVV ADIEEFCKEN RPSVKGPKPV ARSFEVDRNH SEGKQQESWD
PEFHDISLQN VDKNVDYQGW LELEKRKWKM TLTNKKKRRY SSSLFGFDLE QNINKKVCKG
RVGVGSYFRR PEEALTSSYL QIIQLVQSPQ SGQFFAWVVV EGLMLKIPLT IPRVFYINSK
ASIAGNFTGK CINKILPHGK PCYNLMEVNI QEDQFIKESK KLAALLADPE IEGIYETKMP
LEFSAICQIG CVCKIEDTAK HRNTQDGWKL GELHRITTTE CRYLENSIPL VYLYHSTSTG
RAVYVLYCHA SKLMSVVVVN PYGDKELLSS ALERQFRDRC QELSPEPFSW DGILFQVEYV
DHPEAATKFL QKALCEYREE NCGATVAVIE CPDFNTTKEG VKALEDFPCV RIPFNDDDNS
YQPVSWQRPA AKIAVLRCAS AIQWLDRRIA QSRYAHVPLG NFGRDWLTFT VDIFLSRALR
DQQQVLWVSD NGVPDLGDIN NEETFLADET SLLFPGAYRK VSVELKVHRL AVNALLKSDL
VSEMEGGGFL GVNSRGSSLN DNGSFDENNG CAQAFRVLKQ LIKRLLHDAC NSGNIYADSI
LQHLSWWLRS PSSKLHDPAL HLMLHKVMQK VFALLLTDLR RLGAIIIYAD FSKVIIDTGK
FDLSAAKTYC ESLLTVMGSR DIFKLILLEP VHYWHSLLFM DQHNYAGIRA TGDEISGNEV
TIEPKWSVAR HLPEYIQKDF IIIVATFIFG PWKFALEKKR GSAESLEAEM VEYLKEQIGT
RFISMIVEKI GNIRSHIKDI NVSDASWASG QAPKGDYTFE FIQIITAVLA LDQNVQQDVL
VMRKILLKYI KVKECAAEAE FIDPGPSFIL PNVACSNCGA YRDLDFCRDS ALLTEKEWSC
ADPQCVKIYD KEQIESSIIQ MVRQRERMYQ LQDLVCNRCN QVKAAHLTEQ CECSGSFRCK
ESGSDFHKRI EIFLDIAKRQ KFRLLEECIS WILFATSC
