UniProt: E9RHN5

Database: UniProt
Entry: E9RHN5_9ODON

LinkDB:  E9RHN5_9ODON 
Original site:  E9RHN5_9ODON

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   E9RHN5_9ODON            Unreviewed;      1007 AA.
AC   E9RHN5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
DE   Flags: Fragment;
GN   Name=DPD1 {ECO:0000313|EMBL:BAJ78739.1};
OS   Epiophlebia superstes.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Palaeoptera; Odonata; Epiprocta; Anisozygoptera; Epiophlebiidae;
OC   Epiophlebia.
OX   NCBI_TaxID=126247 {ECO:0000313|EMBL:BAJ78739.1};
RN   [1] {ECO:0000313|EMBL:BAJ78739.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=29 {ECO:0000313|EMBL:BAJ78739.1};
RA   Su Z., Ishiwata K.;
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAJ78739.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=29 {ECO:0000313|EMBL:BAJ78739.1};
RX   PubMed=21075208; DOI=10.1016/j.ympev.2010.11.001;
RA   Ishiwata K., Sasaki G., Ogawa J., Miyata T., Su Z.-H.;
RT   "Phylogenetic relationships among insect orders based on three nuclear
RT   protein-coding gene sequences.";
RL   Mol. Phylogenet. Evol. 58:169-180(2011).
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:RU000442};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         ECO:0000256|RuleBase:RU000442};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; AB598699; BAJ78739.1; -; mRNA.
DR   AlphaFoldDB; E9RHN5; -.
DR   GO; GO:0043625; C:delta DNA polymerase complex; IEA:UniProt.
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:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd05777; DNA_polB_delta_exo; 1.
DR   CDD; cd05533; POLBc_delta; 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; 1.10.287.690; Helix hairpin bin; 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; IPR017964; DNA-dir_DNA_pol_B_CS.
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; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   NCBIfam; TIGR00592; pol2; 1.
DR   PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF14260; zf-C4pol; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU000442};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000442}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000442};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          69..375
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          439..869
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          908..985
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAJ78739.1"
SQ   SEQUENCE   1007 AA;  114145 MW;  17DEC64E03290FA4 CRC64;
     NGQPVKGMPG SQIGPVPIMR MYGVTMEGHS VCCHVHGFSP YFFVHIPEAF NNDHCAPFKV
     ALNKALIADM RGNRDNLSEA VLAVEIQMKE NIFGYRGGNK VPFLRVTLAL PKLIPAAKRL
     LEKEMIYTAL GPHPYQAFES NIDFDIRFMV DTNLVGCSWV ELPPQKWSIR TKGGGKPIQS
     RCQLEVDVSW EEMISHPPDG EWAKVAPFRI LSYDIECAGR KGIFPEPDHD PVIQIANMVI
     RQGSTEPFIR NVFTLDTCAP IVGCQVLSFK DERELLEKWA DFVREVDPDL FTGYNINNFD
     LPYLINRAKH LNAKNFYFLG RIKDIKSVIK EQIMQNKQMG RRENKSINTE GRVPFDLLMV
     LLREYKLRSY TLNAVSYHFL QEQKEDVQHS IISDLQNGNP QTRRRLAVYC LKDAYLPLRL
     LDKLMCIINY MEMARVTGVP LSCLLTRGQQ IKVVSQLLRK GKEKDFVIPT YSGAVQDEQF
     EGATVIEPLR GYYADPITTL DFSSLYPSIM MAHNLCYTTL LQPGTKEKLG LSTDQYAKTP
     SGNFFVRESV RKGLLPEILE NLLSARKKAK NELKEETDPL RRKVLDGRQL ALKISANSVY
     GFTGAQVGKL PCLEISGSVT AYGRAMIEQT KQEVEAKYCI SKGYTHDAIV IYGDTDSVMV
     KFGVKTLEEA MELGKEAAEY VSSKFVKPIK LEFEKVYFPY LLINKKRYAG LYFTRPDKYD
     KMDCKGIETV RRDNCPLVAN MMNTCLQKLL IDRDPDGAVA YAKQVIADLL CNRIDISQLV
     VTKELAKQDY ASKQAHVELA NKMRKRDPGT APKLGDRVPY VLTAAAKGTP AYMKAEDPIY
     VLENSIPIDC NYYLENQLSK PLLRIFSPIL GDNKAESVLL RGDHTRTKAV VTSRIGALSA
     FTRKREACLG CKAVLPIAKE EGSPQGPVCQ HCSNRQAEIY TNELVRMQEL EKRFARLWTQ
     CQRCQGSLHE EVLCTSRDCP IFYMRKKVQM DLATQDTVIQ RFGNPIW
//

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