ID D6WSX8_TRICA Unreviewed; 2164 AA.
AC D6WSX8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN Name=AUGUSTUS-3.0.2_09600 {ECO:0000313|EMBL:EFA06672.2};
GN ORFNames=TcasGA2_TC009600 {ECO:0000313|EMBL:EFA06672.2};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA06672.2, ECO:0000313|Proteomes:UP000007266};
RN [1] {ECO:0000313|EMBL:EFA06672.2, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA06672.2,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [2] {ECO:0000313|EMBL:EFA06672.2, ECO:0000313|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA06672.2,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(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}.
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DR EMBL; KQ971352; EFA06672.2; -; Genomic_DNA.
DR STRING; 7070.D6WSX8; -.
DR EnsemblMetazoa; TC009600_001; TC009600_001; TC009600.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_0_1; -.
DR InParanoid; D6WSX8; -.
DR OMA; MLDQCRY; -.
DR Proteomes; UP000007266; Linkage group 7.
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' DNA exonuclease 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 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: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 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:UP000007266};
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 1500..1896
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2164 AA; 247872 MW; DD25A6EBF26CA25F CRC64;
MDEINEKFRP QRDPKLAKKP TDFSREETSE VRLRQVIEND AIDAKYGFER VRDNLERTGF
LLNMHASEIL DEDKRLVAAV DFYFMEEDGA RFKVSYCYMP YFYILTKIEL IQEVSQFLTK
KFSGTIGKIE VVTKEDLDLP NHLIGLQQKY IKLSFFNQTD LIKVRKEILK VVKKNKERES
SNTYYTEMLT DILADKAAQT TKTNTDQMEN ILDIREYDVP YHVRVSIDLK IFCGLWYTVK
CKGATTEPPV ITLRPDLIER PEPIVLAFDI ETTKLPLKFP DAQTDQIMMI SYMIDGQGFL
ITNREILSSD IEDFEYTPKP EFEGKFTIFN EPNELALIQK FFDHIMDVRP HVFVTYNGDF
FDWPFVETRA AVYDLDMKQE IGFAKDRNDV YSCRPAIHMD CLCWVKRDSY LPVGSHNLKA
VAKAKLRYDP VELDPEEMCP LAASQPQVLS NYSVSDAVAT YYLYMQYVHP FIFALCTIIP
CEPDEVLRKG SGTLCEALLM VEAFHCNIIF PNKEETVLNK LTDDGHVLHQ ETYVGGHVEA
LESGVFRADI PCRFRLETDA LNKLIEQVPK TLAHAIEIEE GVPLTDVTNL EEVTNEIVAK
LTSLKEQPMR LERPLIYHLD VGAMYPNIIL TNRLQPCAIV DETICAACDY NKLGARCQRN
MAWMWRAEYM PASRNEYHRI QQQLETEKFP PQYPGGPQRA FHQLTKQEQA DLEKKRLTVY
CRKVYKKAKV TKIEERTTTI CQKENSFYVD TVRAFRDRRY EYKGLSKKAK QAVAAAIKGG
DASEIKSAKN REVLYDSLQL AHKCILNSFY GYVMRRGARW HSMEMAGIVC YTGANIIMRA
REIIEKVGRP LELDTDGIWC ILPASFPENF VVRTNHEKKN KIVVSYPNAV LNAMVKEHFT
NDQYHELVDA QSLKYEERSE NSIFFEVDGP YKAMVLPASK EEGKKLKKRY AVFNFDGTLA
ELKGFEVKRR GELQLIKNFQ SSVFEAFLKG DTLESCYAAV AQIADYWLDV LFSHGRNMPD
SELFDLISEN RSMSKKLEEY GGQKSTSIST AKRLAEFLGD QMVKDAGLAC KYVISKKPDG
APVTERAIPL AIFQSEVSVQ RYYLRKWLKD NSINEVDIRE ILDWNYYIER LGGAIQKIIT
IPAAMQGVPN PVPRVRHPDW LHKKMLEKND TFKQRRITDM FAACPKPQTL PDIEDFGGTS
STDKRPIVTT IKRKRDSDKE SESGFTEEDL SKTWREVMGN PPPYGTTKEE HLAWITFQKR
KWLFQAMQRA QGTRNRKKAK SSASVLRSTV TGTLSGFLQK AQKTLLTVPW QVIQVAPTPV
AGEYKLWALI LNELHQIKLV VPRIFYANLK ESKVVEEGAL FKKCNRTLPR TRQVYNLYMY
SVPEEVFQEH GRKLYLDQTD PNVEGVYETQ VPPLFRTFVQ IGCLCKVVGQ VSSLESFPLD
NLELCTARNQ YLVKDSVKRL FFYNHRHPTK PQQIFGLFLT PLKKALVVVV DTVKTNLMPN
LNKLYQAERM AKKEKGTEDD SLPPASVTFE IRVESDLGQV YKTLQKALQF YKDEKKGPTL
LAVQSALEPA TLRSRIPLFS DFPQVQIHIT DEEELYNVMD WQKIGGRALV RHYLNSEKVL
DLMIEQSRYF HLPVGNMPPD PALFGSDLFY ARHLTKHNHV LWCSPTDKPD LGGVEENDSR
LLAENQEGSS EVCNVPGWYS SVCIELDVDC LAINTLLQSH HVTDIEGTSS ATAFDGVGAT
SLDDLVGDNP TVYDETARCA EAFKILRTMA SIWMRDISLY QNIFADFQVV HFYRWLRAPK
ALLYDPALLR TLQNLMKKLF LQLVAEFKRL GCTIIYANFN KIVICSKKKS VEDAMENVEF
VVTSIRNKEL FHSLDISFRQ CWETLVWLDP ANYAGVQGKL PEDLREEGNE EEKGQSNIVM
SWNLAQRLPE AGGCRTNFSA VIAGYINATF TKMKETENST IARAVSSQPT FGIGANEDVR
QYAKEILSGE ITQELFQITE RINNRLKPLP DGTSPALEFV KAVCQVLGLD AALKDTVSHL
KANLLRLVGV GEFSEKAEWR DTSVSYVIPQ VICKSCNHCR DIDLGRDTHR SEAAWVCPLC
DFAYDNGEIE LFLLDTINRK FLAYNLQDLQ CKKCAQIKLE NLVFHCQCAG DFKCLISRSE
LGKY
//
