UniProt: A0A0D2DU77

Database: UniProt
Entry: A0A0D2DU77_9EURO

LinkDB:  A0A0D2DU77_9EURO 
Original site:  A0A0D2DU77_9EURO

All links

Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   SMART (2)   
All databases (27)   

Download RDF

ID   A0A0D2DU77_9EURO        Unreviewed;      2234 AA.
AC   A0A0D2DU77;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN   ORFNames=PV06_08965 {ECO:0000313|EMBL:KIW39164.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW39164.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW39164.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW39164.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) 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|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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KN847340; KIW39164.1; -; Genomic_DNA.
DR   RefSeq; XP_016259380.1; XM_016410358.1.
DR   STRING; 215243.A0A0D2DU77; -.
DR   GeneID; 27361039; -.
DR   VEuPathDB; FungiDB:PV06_08965; -.
DR   HOGENOM; CLU_000556_0_1_1; -.
DR   OrthoDB; 5475218at2759; -.
DR   Proteomes; UP000053342; 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: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:UP000053342};
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          1516..1907
FT                   /note="DNA polymerase epsilon catalytic subunit A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01159"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1229..1248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2234 AA;  254832 MW;  0BB40F87CFA28747 CRC64;
     MPVRKPSRYG SNVRFSKASS RNQRTKTIDS ASLRDTEATS QDEKFQAIRL ANSIDESMGF
     PRYDSGKRRV GWLYNMHSTV IEDPKVPGGR AGVDFYFIGE DEENFKATVE YDPYFLLAVK
     RGREAEVEEW CKRMFEGLVK SVARVTKEDL KMPNHLLGYK RTFLRLNFAN VTDLLAVRKS
     VLPIAEKNKE KVNAMDTYAE VASATAGFDV YDEEQLNDIH TNGIAEASDF IVDIREYDVP
     YHVRVTIDED IRLGKWYTVD AKHGSVKLTC LEDRLQRADP VVLAFDIETT KLPLKFPDSL
     IDQIMMISYM IDGQGFLITN REIVSEDISD FDYTPKEEYE GPFMIFNEPN ERALIERFFS
     HIKEARPNVI ATYNGDFFDW PFVEARASVL GIDMYAEIGF RKNSEDIYQS DYCAHLDCFA
     WVNRDSYLPQ GSRGLKAVTV AKLGYDPDEL DPELMTPYAN EHPQILAEYS VSDAVATYYL
     YMKYVHPFIF SLCTILPLNP DDTLRKGTGT LCEMLLMVQA YHKNIVLPNK HKEPREAFWE
     GHLLESETYV GGHVESIEAG VFRADIPVNF AIDPAAIDEL LRDLDAALKF CITVEEKKNL
     DDITNYDEVR AQISEKLNSL KTTPHRNERP LIYHLDVASM YPNIMTTNRL QPDSMISESD
     CAACDFNRPG KTCDRRLPWA WRGEFLPTKR DEYNMIRRAM VNETFPGKHA KSMRRTFQEL
     SLDEQASAVR NRLQEYSKKI YHKIHDSKTI EREAIICQRE NPFYVDTVRD FRDRRYDFKG
     KQKVWKGKTE ALKSSGASAT EIEEAKKMIV LFDSLQLAHK VILNSFYGYV MRKGSRWYSL
     EMAGVTCLTG AHIIQMAREL VERIGRPLEL DTDGIWCMLP ATFPENVVFT LKNGKKMAVS
     YPCVMLNHLV HASYTNHQYQ TLTDPTIFKY ETHSDNSIFF EVDGPYKAMI LPTSKEEDKN
     LKKRYAVFNH DGSLAELKGF EVKRRGELKL IKIFQTQIFK FFLEGTTLAE TYAAVARVAN
     RWLDVLHQHG STLADEELID LICENKSMTK TLEEYGAQKS TSITTAKRLA EFLGEQMIKD
     KGLNCKYIIS AKPRNTPVTE RAIPVAIFSA DENVKRFFLR KWLKEDPGDM DPRTVIDWDY
     YLERLGSVIQ KLISIPAALQ KIRNPVPRVA HPEWLQKRIT AKDDKFKQKK MSDLFEKKPL
     GERSVNLLDH RLPPTGDIED ALDAEFKTPV QLTKQSKRKS PDTTNQTVID PYATLPADAP
     AADEDYSGWL QHQKQKWKIQ KQARARRRQL FGEKPNSAMD SIGSFFRNQA EMLYINTWQI
     LQLRQGESPG EVKAFVLIGK KIHPLDIKVQ RTLYLNLKGE ELPNVEIPGC EVEKVNHALP
     NGHPSIHLFQ LSMSEDTYLR EAESVSLLCN HPSVEGVYER QLPLFMRAML KLGNMCSFDE
     SQKGVLGKGL EQGFDLSSLL RSNSHSTYLE DLSAFGYVYF YHITSGDRTV FALFSSSRSE
     AHIIILSRTR DAQLPNADKI YAEQYRQKTA EEALVDSVLE YQASLHFKVS QVTTRRKAHL
     ELGEILKKWR SEESKPTVIL MQSTSSKQLS HDIRIVRDYP ILSLPSEHAD VDLPPLGWQA
     HAFKQLISHY LSAAGWLAHL TELARYGDVP LCNLEKDDPR FLIDLAYARR LKRSNVVLWW
     SEQPRPDHAG HERDDIIGPL TEVVEMPSIN NPGAYTSVCV DVSVQNLAIN TLLTSSIIND
     LEGSADSVAF NPAADDELSG GGISRSNGGF AQAALDVLRD MVKSWWAEAC QGNRLADVMV
     QHLVRWVEAP ASCLYDRHLH YYVQMMSKKA MQQLITDFRR VGSHVVFASP TRLLLQTSKQ
     EVENAYAYSQ YILKSIKQKP LFHFLGLGVK DYWDVLVWYD AYNYGGKGTS AITEQTNTSN
     LETVVHWQLS QFLPLSLQPV FEDWVITFIE VMQNLKRPTI ESGDSSTPRA TQLPSAFISL
     TEDPTSTEVT TVLQDDFSKP LKKQINALIR RQREELLHPE LASDWSFPNL PGGTLESTDA
     RHPRDPVLEL VKSLMQIVSL SKPLQLEARL LRKELLTLFD VREFGQEARF ENPSASLRFD
     NLVCDTCTMT RDLDLCRDED VLPDEQAGAN RPWTCLACQS EFSKIALEET LIARVQASLL
     GWQVQDLKCK KCGTLQGDDA VFSDHCACGG EWVGVLDRRE IRKKVNVLER VSSAYGLRML
     ASVVEGVKAM CLMS
//

DBGET integrated database retrieval system