ID B4KAW6_DROMO Unreviewed; 2260 AA.
AC B4KAW6;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-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=Dmoj\GI24369 {ECO:0000313|EMBL:EDW14644.1};
GN ORFNames=Dmoj_GI24369 {ECO:0000313|EMBL:EDW14644.1};
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230 {ECO:0000313|EMBL:EDW14644.1, ECO:0000313|Proteomes:UP000009192};
RN [1] {ECO:0000313|EMBL:EDW14644.1, ECO:0000313|Proteomes:UP000009192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
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|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; CH933806; EDW14644.1; -; Genomic_DNA.
DR RefSeq; XP_001999183.1; XM_001999147.2.
DR SMR; B4KAW6; -.
DR EnsemblMetazoa; FBtr0175094; FBpp0173586; FBgn0147092.
DR GeneID; 6573092; -.
DR KEGG; dmo:Dmoj_GI24369; -.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_0_1; -.
DR InParanoid; B4KAW6; -.
DR OMA; MLDQCRY; -.
DR OrthoDB; 5475218at2759; -.
DR PhylomeDB; B4KAW6; -.
DR Proteomes; UP000009192; 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: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:UP000009192};
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 1185..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 1965..1991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2260 AA; 258480 MW; E10F06DB4088FE6E CRC64;
MAESGRAKVL QNTGKFVSET RAEGDDFFNE AGYRQSREND KIDSKYGFDR VKDSQERTGY
LINMHTNEVL DDDRRLVAAL DLFFIQMDGS RFKCTVAYQP YLLIRPETNM QLEVARFLGR
KYSGQIASLE HITKEDLDLA NHLSGLKQHY IKLSFLNQTA MTKVRRELMA AVRRNMEREK
SNTYYMQMLA NSLAQSASGA DDGSGKRQQD YMDCIMDIRE HDVPYHVRVS IDLRIFCGQW
YNIRCRSGVE LPIITCRPDI LDRPEPVVLA FDIETTKLPL KFPDAQTDQI MMISYMIDGQ
GYLITNREII SSDIEDFEYT PKPEFEGNFI IFNEENEMQL LQKFFDHIME VRPHIVVTYN
GDFFDWPFVE TRAAVYDLDM KQEIGFSKMR DGNYLSRPAI HMDCLCWVKR DSYLPVGSQG
LKAVAKAKLR YDPVELDPED MCRMAVEQPQ VLSNYSVSDA VATYYLYMKY VHPFIFALNT
IIPMEPDEIL RKGSGTLCET LLMVQAYHAN IVFPNKHQSE LNKLSNEGHV LDSETYVGGH
VEALESGVFR ADIPCRFRLD PSMVKQLMDH VDAVLKHAIE VEEGIPLELV SNLDDVKQEI
VQALQGLHDI PNRLEQPVIY HLDVGAMYPN IILTNRLQPS AMVTELDCAA CDFNKPGVRC
KRTMDWLWRG EMLPASRNEF QRIQQQLETE KFPPLFPGGP TRAFHELSKE DQAAYEKKRL
SDYCRKAYKK TKITKLETRT STICQKENSF YVDTVRAFRD RRYEYKGLTK TAKAAVNAAV
ASGDAAEIKA AKGREVLYDS LQLAHKCILN SFYGYVMRRG ARWHSMPMAG IVCLTGSNII
TKAREIIERV GRPLELDTDG IWCILPGSFP QEFTVHTTHE KKKKINISYP NAVLNTMVKD
HFTNDQYHEL RKSAEGEPPS YDVRDENSIF FEVDGPYLAM VLPAAKEEGK KLKKRYAVFN
FDGSLAELKG FEVKRRGELQ LIKNFQSSVF EAFLAGSTLE ECYASVAKVA DYWLDVLYSR
GSNLPDSELF ELIAENKSMS KKLEEYGAQK STSISTAKRL AEFLGEQMVK DAGLACKYII
SKKPEGAPVT ERAIPLAIFQ SEPSVRRHHL RRWLKDNTMG DADIRDVLDW NYYIERLGGT
IQKIITIPAA LQGLANPVPR VQHPDWLHKK MLEKNDVLKQ RRINEMFTSR ARPKPALTTE
DKQLELGDME DLAGKDDADG SGRPMVTKRK RVHLDGEDGE GSGGESTPQP KTWRQALGAP
PAIGETRKTI VEWVRFQKRK WAWQQEQRQR CRQQSKRHRS GNDSAAAAAS AQAASRATTA
TATLGGFLRR AQRTLLDQPW QILQLVPVND LGQFNVWALI GEELHRIKLT VPRIFYVNQR
SAAPPEEGQL WRKVNRVLPR SRPVYNLYRY SVPEQLFRDN CLGMLADLAT PDIEGIYETH
MTLEFRALMD MGCICGVQRE EARRLAQLST RELESFNIEQ LEQRPQSHVR YLQHASTKLR
KIYLYQHNIP TAKKEIWALF LLPSKKAFVF ALDTVRANQM PNMKQLYTAE RLALIKNLQQ
AAQVEKLPPD DFTFEVLIEV DVKQIYRHIQ RALSAYKQEQ PGPTMLCLQT ANEARKLSAA
MPVLLEFPQA QIHISDDASL LSGLDWQRQG ARAVVRHFLN LNNVLELMLD QCRYFQVPIG
NMPPDTVLFG ADLFFARLLQ KHNFVLWWSA STRPDLGGRE ADDSRLLAEF EENITVVQNR
PGFYPDVCVE LALDSLAVSA LLQSNRIQEM EGASSAITFD VMPQASLEEM IGTVPAATLP
SYDETALCSA AFRVMRSMVN GWLREVSINQ NIFSDFQIVH FYRWVRSSNA LLYDPALRRS
LNNLMRKMFL RIIAEFKRLG ATIVYADFNR IILSSGKRNV SDALGYVDYI VQSLRNKEMF
HSIQLSFEQC WNFMLWLDQS NFSGIRGSLP KGIDETVSAI AAGSTTLHQS QARKKPRSED
DDDDDDDDDV EEVEAGADEV QLEQDEEEEE LALELNWTIG EQLPEENECR EKFESLLTLF
MQALAERKTT EQAIKDISHC AFDFVLKLHK NYGKGKPSPG LELIRTLVKV LSVDKTLADQ
INELRRNMLR LVGVGEFSDL ADWTDPCDTY IINEVICKAC NHCRDLDLCK DKHRAMKDGI
PVWLCAQCYV AYDNEEIEMR MIDVLQRKLM SFVLQDLRCA RCNEIKRENL AEFCTCAGNF
LPLIGGNEIE KLLKTFSNVA SYHKMQLLQQ TVQQALNTPR
//
