ID B4LXF6_DROVI Unreviewed; 2259 AA.
AC B4LXF6;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 91.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN Name=Dvir\GJ24376 {ECO:0000313|EMBL:EDW67834.1};
GN ORFNames=Dvir_GJ24376 {ECO:0000313|EMBL:EDW67834.1};
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244 {ECO:0000313|EMBL:EDW67834.1, ECO:0000313|Proteomes:UP000008792};
RN [1] {ECO:0000313|EMBL:EDW67834.1, ECO:0000313|Proteomes:UP000008792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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 EMBL; CH940650; EDW67834.1; -; Genomic_DNA.
DR RefSeq; XP_002054314.1; XM_002054278.2.
DR SMR; B4LXF6; -.
DR STRING; 7244.B4LXF6; -.
DR EnsemblMetazoa; FBtr0240301; FBpp0238793; FBgn0211456.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_0_1; -.
DR InParanoid; B4LXF6; -.
DR OMA; MLDQCRY; -.
DR OrthoDB; 5475218at2759; -.
DR PhylomeDB; B4LXF6; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:EnsemblMetazoa.
DR GO; GO:0008296; F:3'-5'-DNA exonuclease activity; IEA:EnsemblMetazoa.
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:0045004; P:DNA replication proofreading; IEA:EnsemblMetazoa.
DR GO; GO:0090592; P:DNA synthesis involved in DNA replication; IEA:EnsemblMetazoa.
DR GO; GO:0007113; P:endomitotic cell cycle; IEA:EnsemblMetazoa.
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:SF0; 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:UP000008792};
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 1542..1945
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
FT REGION 1210..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1969..1988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2259 AA; 258737 MW; FE8FC9346DFB0A95 CRC64;
MAEAGKTKVL QNTGKFVSET RAEGDDFFNE AGYRQSREND KIDSKYGFDR VKDSQERTGY
LINMHTNEVL DDDRRLVAAL DLFFIQMDGS RFKCTVAYKP YLLIRPEVNM HLEVARFLGR
KYSGQIASLE HINKEDLDLA NHLSGLQQHY LKLSFLNQTA MTKVRRELMA AVRRNTEREK
SNTYYMQMLA NSLAQSASGS DDGSGKRQQD YMDCIMDIRE HDVPYHVRVS IDLRIFCGQW
YNIRCRSGVE LPVITCRPDI LDRPEPVVLA FDIETTKLPL KFPDAQTDQI MMISYMIDGQ
GYLITNREII SSNIEDFEYT PKPEFEGNFI IFNEENEMQL LQKFFDHIME VRPHIVVTYN
GDFFDWPFVE TRAAVYDLDM KQEIGFSKMR DGIYLSRPSI HMDCLCWVKR DSYLPVGSQG
LKAVAKAKLR YDPVELDPED MCRMAVEEPQ VLSNYSVSDA VATYYLYMKY VHPFIFALNT
IIPMEPDEIL RKGSGTLCET LLMVQAYHAN IVFPNKHQSE LNKLSNEGHV LDSETYVGGH
VEALESGVFR ADIPCRFRLD PNMVKQLMDQ VDAVLKHAIE VEESIPLQLV SNLDEVKQEI
VQALQGLHDI PNRLEQPVIY HLDVGAMYPN IILTNRLQPS AMVTELDCAA CDFNKPGVRC
KRSMDWLWRG EMLPASRNEF QRIQQQLETE KFPPLFPGGP ARAFHELSKE DQAAYEKKRL
SDYCRKAYKK TKITKLETRN STICQKENSF YVDTVRAFRD RRYEYKGLTK TAKASVNAAI
ASGDAAEIKA AKGREVLYDS LQLAHKCILN SFYGYVMRRG ARWHSMPMAG IVCLTGSNII
TKAREIIERV GRPLELDTDG IWCILPGSFP QEFTVHTTHE KKKKINISYP NAVLNTMVKD
HFTNDQYHEL RKAEKGEPPS YDIRDENSIF FEVDGPYLAM VLPAAKEEGK KLKKRYAVFN
FDGTLAELKG FEVKRRGELQ LIKNFQSSVF EAFLAGSTLE ECYASVAKVA DYWLDVLYSR
GSNLPDSELF ELIAENKSMS KKLEEYGAQK STSISTAKRL AEFLGEQMVK DAGLACKYII
SKKPEGAPVT ERAVPLAIFQ SEPSVRRHHL RRWLKDNTMG DADIRDVLDW NYYIERLGGT
IQKIITIPAA LQGLANPVPR VQHPDWLHKK MLEKNDVLKQ RRINEMFTSR PRPKPALATE
DKQLELGDME DLAGKEDAEA SGRPIVTKRK RVHLDDDDEE GNAAESTPQP KTWRQALGAP
PAIGETRKTI VEWVRFQKRK WAWQQEQRQR CRQQSKRQRN GTETAAGAAS AQAAARATTS
AATLGGFLRR AQRTLLDQPW QILQLVPVND LGQFTVWALI GEELHRIKLT VPRIFYVNQR
SAAPPEEGQL WRKVHRVLPR SRPVYNLYRY SVPEQLFRDN CLGMLADLAT PDIEGIYETQ
MTLEFRALMD MGCICGVERE EARRLALLST RELENFSIEQ LEQRPQSHIR YLQHASSKLR
KIYLYQHNIP TAKKEIWALF LLPSKKALVF ALDTVRANQM PNMKQLYVAE RLALIKNLQQ
AAQIEKLPAE DFSFEVLIEV DVKQIYRHIQ RALSAYKQEQ SGPTMLCLQT AIEARKLSAA
MPVLLEFPQA QIHISDDASL LSGLDWQRQG ARAVVRHFLN LNNVLELMLD QCRYFHVPIG
NMPPDTVLFG ADLFFARLLQ KHNFVLWWSA STRPDLGGRE ADDSRLLAEF EESITVVQNR
AGFYSDVCVE LALDSLAVSA LLQSNRIQEM EGASSAITFD VMPQASLEEM IGTVPAATLP
SYDETALCSA AFRVMRSMVN GWLREVSINQ NIFSDFQIVH FYRWVRSSNA LLYDPALRRS
LNNLMRKMFL RIIAEFKRLG ATIVYADFNR IIISSGKRNV PDALGYVDYI VQSLRNKEMF
HSIQLSFEQC WNFMLWLDQS NFSGIRGRLP KGIDETVSAI AVGSTTLRQS QARNEQVHED
DDDDNDDVQE VEAGLDEPLE EQEEEEEEEL SLELNWTIGE QLPEENECRE KFESLLTLFM
QALAERKTTE QAIKDISHCA FDFVLKLHKN YGKGKPSPGL DLIRTIVKVL SVDKALADQI
NELRRNMLRL VGVGEFSDLA DWTDPCDTYI INEVICKACN HCRDLDLCKD KHRAMKDGIP
VWLCAQCYVA YDNEEIETRM IDALQRKMMS FVLQDLRCER CNEIKRENLA EFCTCAGNFL
PLISGKEIET LLKTFSNVAG YHKMQLLQQT VQQAQKTPR
//