DPOE1_DICDI
ID DPOE1_DICDI Reviewed; 2380 AA.
AC Q54RD4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=pole; Synonyms=pol2; ORFNames=DDB_G0283189;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(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: Consists of three subunits: pole, pole2 and pole3.
CC {ECO:0000305}.
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; AAFI02000051; EAL65833.1; -; Genomic_DNA.
DR RefSeq; XP_639211.1; XM_634119.1.
DR AlphaFoldDB; Q54RD4; -.
DR SMR; Q54RD4; -.
DR STRING; 44689.DDB0216320; -.
DR PaxDb; Q54RD4; -.
DR EnsemblProtists; EAL65833; EAL65833; DDB_G0283189.
DR GeneID; 8623984; -.
DR KEGG; ddi:DDB_G0283189; -.
DR dictyBase; DDB_G0283189; -.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_1_1; -.
DR InParanoid; Q54RD4; -.
DR OMA; MLDQCRY; -.
DR PhylomeDB; Q54RD4; -.
DR Reactome; R-DDI-6782135; Dual incision in TC-NER.
DR Reactome; R-DDI-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DDI-68952; DNA replication initiation.
DR Reactome; R-DDI-68962; Activation of the pre-replicative complex.
DR PRO; PR:Q54RD4; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; ISS:dictyBase.
DR GO; GO:0005657; C:replication fork; ISS:dictyBase.
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; ISS:dictyBase.
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; ISS:dictyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:dictyBase.
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..2380
FT /note="DNA polymerase epsilon catalytic subunit A"
FT /id="PRO_0000328349"
FT ZN_FING 2225..2288
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT REGION 169..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1766..1787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1967..1998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2059..2120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2245..2275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2319..2337
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT COMPBIAS 1974..1988
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2059..2084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2085..2100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2261..2275
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2319
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2322
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2334
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2337
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
SQ SEQUENCE 2380 AA; 275442 MW; B4DC5FAA0542994B CRC64;
MSQKWNENKK NKDEKDENDK YVGFKNYEKE GWLLNMQPGS SKDGLDIEKA SLELFFIQDD
ATSFRVWIPY NPYFYIYVKE GHQSEVESYL KSTYEKDIAG IDIMDKEDLD LENHLSGLKR
KYLKIRFHNV STLLSVRNDL FPIIKRNKQK SNTSEAYEDE SLNKILNSYY NKGNNNNNNH
QNYNNNNNQN NNNFNKELNK DDNNNNNSKL NKQATEYILD IREYDVPYYV RAAIDLNIRV
GLWYTVIKNG RLTTVNELTT RVDRPDPKVL AYDIETTKLP LKFPDSSIDS IMMISYMLDK
QGYLIVNREI VSEDIKDFEY TPKPEYYGPF TVFNEPDEKS VLERFFSEIK REKPHIFVSY
NGDMFDWPFV ESRAEYHGLS MFHQIGFRND NGEYRSKINP HMDAFCWVKR DSYLPHGSHG
LKAVTREKLR YDPLELDPEL MLKSAQEDPE TLANYSVSDA VATYYLYMNY VHPFIFSLCT
IIPMNPDDVL RKGSGTLCEA LLMTQAFKAD VIFPNKHKDD INSMYKGHLL ESETYVGGHV
ECLESGVFRS DIPTNFSLDP ASIEKHMGNI DQVLKFALKE GGIPLDTVSN YQEVKEDVLK
KFTLLKENPK QQSHPLIYHL DVSAMYPNII LTNKLQPTAV VNDEVCATCV YNKPESQCQR
TLDWQWRGDY SPSNQSEYRL ILQQLESEKF GDGDERKSFL SLSEEKRNEL LRKRLKEYSR
KVYRKTHQIT QEIRSDTICM RENSFYVDTV RLFRDRRYVF KNHHRDWKIK YDQAMQESGG
TNSVAVVAAQ GMVVLYESLQ LAHKCILNSF YGYVMRKGAR WYSMQMAGIV THTGSNIIKE
AREVVEQMGR PLEIDTDGIW CILPSHFPEN YTLKSASTGK KVTFSYICEM LNEKVAKSFT
NHQYQDYNAE TNTYTIRDEC SILFECDGPY RCMLIPTSKE KDVKLKKRYA VFNREGRICE
LKGFEIKRRG ELKLIKLFQS EVFKEFLGGD SLEGCYQSVG AVANRWLDIL DSHAENYEEK
DLIELITESS NMSRKLEEYG TQKSSAISTA KKLAEFLGDD MIKDKGLSCQ YIISNKPAGS
PITERALPVA IFDADFETRC HYLRRWTKSP SGDLDIRELI DWDYYRQRLS GVIQKIITIP
AALQNVTNPV PRVIHPDWIL KEIRRNEDGR QQTSITSFFE KTEDNDQDND NDNDNDNDND
NDNSKPQQTD DIENMFSSRF KDLPAFNPKV TKFKRSKQSS SDVSSLLIKK SKSSIETFTN
EQEKQIMETK TPSIDKDFQG WLSISKKKWK IQRLLKKRRQ RLGGSLFDSD SFRIGSKLTN
RESSSSSFFK SQSDIIKKGY WNIISIEPIY GGEPGIYQMW SLIEDQLIPI KVDIGRVFYL
NSIDTDPYED AQKNTNVIPP RGKQRFNVFS VTMSESQFLE QSKELNTLFT NPMIEGVYET
KVPLDIKAII QCGCVATLSR VSPFFTKIVN SNTRFSLEDI ASKPDKQFHY LAEHNFNQLF
LYHNSRDGKD GYFVLFNMNT QQCSVIFSNP YMAANKIDAR VLNSIKEKLP EITFTMDQKS
SMSLAKKEIG SLIMEYQRKG LPTIILLQVP NAIGILEQIP ILREFPRVPV PYHDNDSMYS
PFNWDVHSLK PLPLRLMDAP KLWVYYANMS RYANIPIGNI PTDNASFMCD ILYARSLVEQ
KHLLWMSDSN FPDLGGSEED DAKFYEELNN VEINNSDCYN QVCFELDIEN LATNTILESI
HLAEIEGILG NELGDESNVA MFDDIKNTSN NSNTKNGANQ NTTNDTTSSF DKLSITNKFR
SAINHQISGC EKEFNILRNL VSKWKLDLVS GSNSKRNEIS SRYSNYLLLH FYRWISSTNS
KLYDPILYRT LHQLMKKVFI QLIFEFKKLG SKIVYANFNK IIICSQKDSI EDARSYCNYI
LAVIKKKELF SWINFKQTNY YHNLLWLNNS NYSGILYFNP LINKNQQQQQ QQQDNADDDD
DDDVSENEEE QQQNKNKKLK KIKNGKIITN WNIAEFLPPQ IQTSFIIIIS DYIYKLHTER
DELNRIQKEQ QQRYLLKQKI STTSSSSNND STAATTTTTK DTINEPTKPD LRKSSTWNEE
EDEDISIPPS SSSSTTTTTS KTKKATSKFD LLIDVNRIFT LLDHFQVNQS SLEFPQLPGG
YLKLNNPPLE FIKFVCHVLS IDKSISSRVS RLRMKLMTSM KVREFSDEAK FKDPCVSFTL
PDVICSSCHS CRDIDLLRNT NTTSISSRLS SQQKSNNNDS DDSDDDNEEN EGDDDNIIRV
PELSCIQCKG HYSKNTIESQ LVEIIQRRSL SYQLQDLRCS KCNDVKSDNL GDICPQCSGQ
WECTQSNNLF SKDLIIFKSI AEYHNFEWLG ETVDSLSKFI
