ID F7FZT0_CALJA Unreviewed; 2258 AA.
AC F7FZT0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN Name=POLE {ECO:0000313|Ensembl:ENSCJAP00000023741.5};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000023741.5, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000023741.5}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000023741.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: DNA polymerase II participates in chromosomal DNA
CC replication. {ECO:0000256|RuleBase:RU365029}.
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:0000256|RuleBase:RU365029};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU365029};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365029}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU365029}.
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DR Ensembl; ENSCJAT00000025115.5; ENSCJAP00000023741.5; ENSCJAG00000012853.5.
DR eggNOG; KOG1798; Eukaryota.
DR GeneTree; ENSGT00390000010194; -.
DR TreeFam; TF105017; -.
DR Proteomes; UP000008225; Chromosome 9.
DR Bgee; ENSCJAG00000012853; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd05779; DNA_polB_epsilon_exo; 1.
DR CDD; cd05535; POLBc_epsilon; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1.
DR PANTHER; PTHR10670:SF1; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 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; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU365029};
KW DNA replication {ECO:0000256|RuleBase:RU365029};
KW DNA-binding {ECO:0000256|RuleBase:RU365029};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU365029};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365029};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU365029};
KW Metal-binding {ECO:0000256|RuleBase:RU365029};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU365029};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365029};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365029};
KW Zinc {ECO:0000256|RuleBase:RU365029};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU365029}.
FT DOMAIN 1498..1898
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1912..1943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1921..1943
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2258 AA; 258737 MW; 7D74B45C1D759A38 CRC64;
MALRSGGRRR ADPGADGEAG RDDGPTSSVS ALKRLERSQW TDKMDLRFGF ERLKEPGEKT
GWLINMHPVA LPYKPYFYIA TRKGCEREVS SFLSKKFQGK IAKVETVPKE DLDLPNHLVG
LKRNYIKLSF HTVEDLVKVR KEIFPAVKKN REQDHASDTY TAMLSSVLQR TSVITDEEEA
SKKIADQLDN IVDMREYDVP YHIRLSIDLK IHVAHWYNVR YRGNAFPVEI TRRDDLVERP
DPVVLAFDIE TTKLPLKFPD AETDQIMMVS YMIDGQGYLI TNREIVSEDI EDFEFTPKPE
YEGPFCVFNE PDEAHLIQRW FEHVQETRPT VMVTYNGDFF DWPFVEARAA VHGLSMQQEI
GFQKDSQGEY KAPQCIHMDC LRWVKRDSYL PVGSHNLKAA AKAKLGYDPV ELDPEDMCRM
ATEQPQTLAT YSVSDAVATY YLYMKYVHPF IFALCTIIPM EPDEVLRKGS GTLCEALLMV
QAFHANIIFP NKQEQEFNKL TDDGHVLDSE TYVGGHVEAL ESGVFRSDIP CRFRMNPAAF
DFLLQRVEKT LRHAIEEEEK VPVEQVTNFQ ELCDQIKSKL ASLKEVPNRI ECPLIYHLDV
GAMYPNIILT NRLQPSAMVD EATCAACDFN KPGANCQRKM AWQWRGEFMP ASRSEYHRIQ
HQLESEKFPS LFPEGPARAF HELSREEQAK YEKRRLADYC RKAYKKIHIT KVEERLTTIC
QRENSFYVDT VRAFRDRRYE FKGLHKVWKK KLSAAVEVGD AAEVKRCKNM EVLYDSLQLA
HKCILNSFYG YVMRKGARWY SMEMAGIVCF TGANIITQAR ELIEQIGRPL ELDTDGIWCV
LPNSFPENFV FKTTNVKKPK VTISYPGAML NLMVKEGFTN DQYQELAEPS SLTYVTRSEN
SIFFEVDGPY LAMILPASKE EGKKLKKRYA VFNEDGSLAE LKGFEVKRRG ELQLIKIFQS
SVFEAFLKGS TLEEVYASVA KVADYWLDVL YSKAANMPDS ELFELISENR SMSRKLEDYG
EQKSTSISTA KRLAEFLGDQ MVKDAGLSCR YIISRKPEGS PVTERAIPLA IFQAEPTVRK
HFLRKWLKSS SLQDFDIRAI LDWDYYIERL GSAIQKIITI PAALQQVKNP VPRVKHPDWL
HKKLLEKNDV YKQKKISELF TLEGRRQVMM AQAPGDSLRP SAPDMEDFGL VKPPHPPAHI
AVKRKRVLWE SQEESQDLTP TVPWQEILGQ PPALGTTQEE WLVWLRFHKK KWQLQARQRL
ARRKRQRLES AEGVPRPGAI RDGPATGLGS FLRRTARSIL DLPWQIVQIS ETSQPGLFRL
WALIGSDLHC IRLSIPRVFY VNQRVAKAEE GASYRKVNRV LPRSNVVYNL YEYSVPEDMY
QEHINEINTE LSAPDIEGVY ETQVPLLFRA LVHLGCVCVV NKQLVRHLSG WEAETFALEH
LEMRSLAQFS YLEPGSIRHI YLYHHMQGHK ALFGIFIPSQ HRASVFVLDT VRSNQMPSLG
ALYSAEHGLL LEKVGPELLP PPKHTFEVRA ETDLKTICRA IQRFLLAYKE ERRGPTLIAV
QSNWELKRLA REIPVLEEFP LVPICVADKI NYGVLDWQRH GARRMIRHYL NLDTCLSQAF
EMSRYFHIPI GNLPEDISTF GSDLFFARHL QRHNHLLWLS PTARPDLGGK EADDNRLVME
FDDQATVEIN SSGCYSTVCM ELDLQNLAVN TILQSHHVND MEGADSMGIS FDVIQQASLE
DMITGGQAAS APASYDETAL CSNTFRILKS MVVGWVKEIT QYHNIYADNQ VMHFYRWLRS
PSSLLYDPAL HRTLHNMMKK LFLQLIAEFK RLGSSVIYAN FNRIILCTKK RRVEDAIAYV
EYITSSIHSK EIFHSLTISF SRCWEFLLWM DPSNYGGIKG KVSSRIHCGL QDSQKAGGAA
DEQEDEDEEE EREGEEEDAE ESDVEDLLEN SWNILQFLPQ AASCQSYFLM IVSAYIVAVY
HCMKDGLRRS APGSTPVRRR GASQLSQEAE ETAGALPGMI TFSQDYVANE LTQSFFTITQ
KIQKKVTGSR NSAELSEMFP VLPGSHLLLN NPALEFIKYV CKVLSLDTNI TNQVNKLNRD
LLRLVDVGEF SEEAQFRDPC RSYVLPEVIC RSCNFCRDLD LCKDSSFSED GVVLPQWLCP
NCQAAYDSSA IEMALVEVLQ KKLMAFTLQD LVCLKCRGVK ETHMPVYCSC AGDFALTIHT
KVFMEQIRIF QNIAQHYGMS YLLETLEWLL QKNPQLGH
//