ID A0A1E4RS73_9ASCO Unreviewed; 2221 AA.
AC A0A1E4RS73;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN ORFNames=HYPBUDRAFT_101979 {ECO:0000313|EMBL:ODV69915.1};
OS Hyphopichia burtonii NRRL Y-1933.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Hyphopichia.
OX NCBI_TaxID=984485 {ECO:0000313|EMBL:ODV69915.1, ECO:0000313|Proteomes:UP000095085};
RN [1] {ECO:0000313|Proteomes:UP000095085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-1933 {ECO:0000313|Proteomes:UP000095085};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00024632,
CC 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; KV454538; ODV69915.1; -; Genomic_DNA.
DR RefSeq; XP_020078982.1; XM_020218169.1.
DR STRING; 984485.A0A1E4RS73; -.
DR GeneID; 30992719; -.
DR OrthoDB; 5475218at2759; -.
DR Proteomes; UP000095085; Unassembled WGS sequence.
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: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:UP000095085};
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 1529..1913
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2221 AA; 256152 MW; 3E75CD20F81C1D71 CRC64;
MSSKPQFKGS TSARFVKNGG GANNYSKKNS NTIRSEFKGD RNESIDPSKL NPMLNDSIQK
KELVTRIDQL DSVMGFDRVE NGELDGLKPR KGWLINMHST TIPTDDYLAG YSGVDYYFLD
EEGGSFKATI KFDPYFYLAV IPGHEAEVEE MLKKFLEPCH LKNIARLDKE DLALPNHLVG
LKKTLIKLSF HNVSDLLSSR RLLTPIIKDN QMNRESRDVF QVMNNFNNQN SESSNADPTT
FIDDIREYDV PYHARVSIDM NIRVGKWYDV YVKHGDVSLV EDKEKIAFAD PVVLAFDIET
TKAPLKFPDA KIDQIMMISY MIDGEGYLIT NREIISEDID DFEYTPKPEY PGLFTIFNEP
DEKHVLLRFF EHIRDVRPTV IATFNGDFFD WPFVENRTNF HDLDMFDEIG FAKDNEGEYK
SKYCVHMDCF RWVKRDSYLP QGSQGLKAVT TAKLGYNPTE LDPELMTPYA YEKPQLLSEY
SVSDAVATYY LYYKYVHPFI FSLCTILPLN PDEVLRKGTG TLCEMLLMVQ AYENNIILPN
KYTDPIERFY DGHLLESETY VGGHVESLEA GVFRSDIPNK FKIDPTAIDE LLNDLKSAIK
FCVEVENGKK LEDVENFDEV YNQIKSELIE LRDNPVRNET PLIYHVDVAS MYPNIMTSNR
LQPDSIKSEE DCAACDFNRP GKNCDRRLPW AWRGEYYPAE MNEYGMIKRT LQNESFPGVK
PWLPQRSFDE LPYAEQALLI KKRLSDYSRK VYHRIKQSKI VTREAIVCQR ENPFYVNTVR
NFRDRRYEFK TLAKVWKGKT SKIASSDQIA KDEAKKMVVL YDSLQLAHKV ILNSFYGYVM
RKGSRWYSME MAGITCLTGA TIIQMARSLV ERLGRPLELD TDGIWCILPK SFPENFNLKC
KDGKKIFVEY PCSMLNYIVH EKFTNHQYQD LVDSESLKYK TRSENSILFE VDGPYKAMIL
PTSKEEGKGL KKRYAVFNDD GSLAELKGFE LKRRGELQLI KNFQSDIFKL FLDGDSLEGC
YQAVASVANN WLDVLDTKGG MLEDEDLIEL ICENRSMSKA LVEYEGQKST SITTAKRLGE
FLGEEMVKDA GLACKYIISS KPIGSPVTER AIPVSIFSSE KKEFFLKKWL KDPSLSDFDP
RSVIDWDYYY ERLASVVQKI ITIPAALQDV KNPVPRVPHP DWLQKRIKIK DDTKQQSSIS
KFFGKSTKSE ALQNQVKHIQ DIEDFGELDS GISKTKVGKV TSKKRRNGKI NNASDTEEEE
RNNAVLNGPC PLMTEDYVGY LQYQKAKWKV QAKNRERRRK LFGNNTESSH RSSVGGLFRK
QAESVAGSDW EILEYKPDPT TPGDVKVYIL SGNKVHSFIF HIPKQIYATF KTDISQRKYI
QNCEIEKSNA ILPNGHDGSH LYKFVMPEPV YNEQISKIDS ILQDSKILGL YESNINSVDR
AIINLGNTVK FDDTKVGALG KGLKNGFNMK DLSKIEKDSY LKRFNMDIVY LLHIVTNSYE
FFTVFKTWDN SANMFVLKPS SNAQELPTNI HKIYQEVYEN KKDKLGKLYN IIDYPSEMSF
DTNYYNSRSS LYKKLNTFVS KIHESRSNKA LFTIQSPYVS KVLVHLPAIS NFPTIRMNVT
ELSLPAIGWQ SLITKRVINH FFVLASWIKN LISLSNYGKI PLCNLQTENM GYLIDIEYAR
RLSYNNIVLW WSSNPLPDHG GFEADKTQDL ESFDFPTINS PEIYETACLE VEIGTLTINT
ILTSSLINEA EGADLAEDSM VFDQNNGAST MAEDSFSTPS LSILRSMVKD WWDDAMKNNI
NADSMMNHLV SWVQRKDSFL YDNALHYHVH NLTSKALLQL IGEFRRMNAQ VVFANRNRII
LQTTRVSVEN SYAYGQYIVK AARSKPLFNF LDLRIVKYWD ILIWMDEYNF GGRCCTEITN
DETQNLVPVN NWHIKKFLPL IFQNEFEDWL VIFLDSLAKY KNETLLGNTQ SGTPRVTQIN
HILKGQKKID SAEVEDEDIN NGVMELFRKP LQKRIQRLHR QQNESIINPD LKIEYEFPKL
TGSFLKMRNP ILELVKFLCS VFSLSKKRSI EVSLLRKELL ASLDVREFSR EATFHNPSTS
LKIPHIICDY CNYIRDVDFC RDEERDIFTC TNCSKEYNKI TIEEELISLF NKMMVQFFTQ
DLKCVKCQVV KVDSMSEHCK CSGDWAETIK HEEVEDKMKV FANVSHYYGL KLLEGLLDEY
Q
//