ID D8LQC0_ECTSI Unreviewed; 1416 AA.
AC D8LQC0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN ORFNames=Esi_0006_0016 {ECO:0000313|EMBL:CBN78684.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBN78684.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBN78684.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
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|ARBA:ARBA00001966,
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN648818; CBN78684.1; -; Genomic_DNA.
DR STRING; 2880.D8LQC0; -.
DR EnsemblProtists; CBN78684; CBN78684; Esi_0006_0016.
DR eggNOG; KOG1798; Eukaryota.
DR InParanoid; D8LQC0; -.
DR OrthoDB; 5475218at2759; -.
DR Proteomes; UP000002630; Chromosome LG04.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide 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; 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; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR029703; POL2.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10670:SF0; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT 1; 1.
DR PANTHER; PTHR10670; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 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|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}; Nucleus {ECO:0000256|RuleBase:RU365029};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365029};
KW Zinc {ECO:0000256|RuleBase:RU365029};
KW Zinc-finger {ECO:0000256|RuleBase:RU365029}.
FT DOMAIN 155..446
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 807..992
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1416 AA; 158200 MW; 9137999B99830BDA CRC64;
MAPARGRGKG DWKRNGGGGG GGGGGGKGSR YQRQQSKGGG GSGGKRSYAD SSQAARLSGG
GRKESAVKAA LREQGDALDK RFGYDRYSEG PPRLGWIFNM LPTSIPDASG NEKSGLDMYF
LEQDGGTFKA TVFYKPYFYV LVKEERYIQD CIQCIRRRFE DSAVEVTVVD KEDLDMPNHL
SGKLRRFLKL SFHSVADLME VKRALMPTIQ ANKTRAEAQD AYMHAEAREQ QPSDFLSVLV
DAREYDVPYY VRCSIDLDIR VGAWYMVTPQ EEGVDVAWQK EMVDKAEPKV LAYDIECTKA
PLKFPNVEID QVFMISYMVD GQGYLIISRE VVSEDVENFE YTPKPSFPGP FHIFNEPNEE
AVIRRFFKHV AELRPQIIVT YNGDFFDWPF VDERAKGYGL DMEKEIGVGL QANGEYRGRC
VAHMDAIYWV KRDSYLPQGS HGLKAVTKYK LGYDPVEVDP EDMVRYASER PTEMAAYSVS
DAVATYYLYQ TYVHMFVFSL CTIIPMGPDD VLRKGSGTLC EALLMVEAYR GNIVCPNKHS
EPLTKFHDGH LVESETYIGG HVECLETGVF RSDLPEKFRL VPSALQALID NVDRDLTFAI
EVESGVQRDT VSNYDEVRSE IIEQLEMLRD SPLREEEPFI YHLDVAAMYP NIILSNRLQP
GAIVNKAMCA SCDFNQDSNN CKRSLTWKWR GDMTPASRTE YQSVKMQLTY ENVDGKPFVE
LDEADQATNV RARLKNYAHK VYKKTKITKE EERVDTVCMR ENPFYVNTVR AFRDRRYDYK
ILTKKAKKAK SKAAEEGDAV GAKEAGDRAQ VFDSLQLAHK CILNSFYGYV MRKGARWRSM
EMAGIVTYTG AMLIKQAREL VEQIGRPLEL DTDGIWCILP SSFPENFTFT TKSGGKIRIS
YPCVMLNADV HENYTNHQYQ DLQDPATRKY NTKSECSIFF EVDGPYRCMV LPSSTEEGKL
LKKRYAVFNH DGSLAELKGF ELKRRGELEV IKVFQSQGTS QTTARRLADF LGAEMVKDKG
LNCRMILSNR PHGAPVTDRA VPTAIFSAEP AVKKHYLRKW LKDPAMEDFD IRSILDWDYY
LDRLGNCIRK IITIPAAMQK VENPCPRVKH PDWLRKIVRE INDGYRQTKI DQLFKAAPPG
TPQLTNAGAS TKAKPTPAPA ATDIEDMAGG GGGGGGAAGR SILGARARVT KRIGNGAAAG
GALAPDGSPG KENADVGGGG QEEEEEEEEE AVPIRREDDF QGWLAQQKAG WKKRREQNRL
KRRTEARSQA MASFRGSGSS GARGGTAGLG AAGAAEKRRR TAAMGKSGLQ GYLTSAQDAL
LRGFWQVVEI RPSDNPGSFT VFAMTGPGEL QVIPITIPRV FYVNCLEDKG PAGSSAMGRR
VARTLPNGHG SPFLYEVAMD EAKFQRNEKQ PVAPVV
//
