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Database: UniProt
Entry: A0A1E4RS73_9ASCO
LinkDB: A0A1E4RS73_9ASCO
Original site: A0A1E4RS73_9ASCO 
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
//
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