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Database: UniProt
Entry: W6JJH3_9MYRI
LinkDB: W6JJH3_9MYRI
Original site: W6JJH3_9MYRI 
ID   W6JJH3_9MYRI            Unreviewed;      1022 AA.
AC   W6JJH3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
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:BAO48686.1};
OS   Thereuonema tuberculata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Notostigmophora; Scutigeromorpha; Scutigeridae; Thereuonema.
OX   NCBI_TaxID=353554 {ECO:0000313|EMBL:BAO48686.1};
RN   [1] {ECO:0000313|EMBL:BAO48686.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Th1 {ECO:0000313|EMBL:BAO48686.1};
RX   PubMed=24535281; DOI=10.1038/srep04127;
RA   Miyazawa H., Ueda C., Yahata K., Su Z.-H.;
RT   "Molecular phylogeny of Myriapoda provides insights into evolutionary
RT   patterns of the mode in post-embryonic development.";
RL   Sci. Rep. 4:4127-4127(2014).
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; AB831769; BAO48686.1; -; mRNA.
DR   AlphaFoldDB; W6JJH3; -.
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; 2.40.50.730; -; 2.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 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          91..397
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          461..890
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          929..1000
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:BAO48686.1"
SQ   SEQUENCE   1022 AA;  116487 MW;  EE84BB115988653D CRC64;
     VPTINSKTDT LEFQQIEIDY YVGKPLQGMP GNQSASVVPI MRMYGVTMNG NSVMCHVHGF
     APYFFVPAPP GFTDNHCRGF KDALNKTVLN DMRSNKDNIT ETVLAVEITL KENMYGYHGN
     RKVPFLKVTM ALPRLIAPAR RLLNDGINIP GLGQHAMASF ESNIDYEIRF MVDTNVVGCC
     WIKLPAGKYR IRQSNSGPPL MSRCQLEVDV AWDEFIAHSP EGEWSKLAPF RILSFDIECA
     GRKGIFPEPD KDPVIQIANM VVRQGDPTHF IRNVFTLKSC ASIVGAQVLS YDKESELLEK
     WSDFIREVDP DIITGYNIQN FDLYYLLSRA NHLKVPKFPY LGRVKDIRTI IKTQMLQSKQ
     MGRRENKNIN IEGRTQFDLL LILLRDYKLR SYTLNAVSFH FLQEQKEDVQ HSIITDLQNG
     NEQTRRRLAV YCLKDAYLPL RLLDKLMCLF NYIEMARVTG VPLSYLLTRG QQIKVISQLL
     RKSKEHDFVI PTVKAEVGED YTGATVIEPS VGYYNEPIAT LDFASLYPSI MIAHNLCYTT
     VLKKQSDREN LNPEDFIKTP SNDYFMKSHV RRGLLPEIVE NLLAARKKAK ADLKNETDPL
     RRKVLDGRQL ALKISANSVY GFTGAQVGKL PCLEISQSVT AFGRCMIEKT KSTVEAKYTK
     ANGYKQNAQV IYGDTDSVMV KFGVETVADA MELGREAAEY VTQEFVKPIR LEFEKVYFPY
     LLINKKRYAG LYFTRPETYD KMDCKGIETV RRDNCPLVAN LMNTCLQKIL IERDPDGAVE
     YAKQIISDLL CNRIDISQLV ITKELTKTDD EYKGKQAHVE LSHRMRKRDA GSAPNLGDRV
     PFVIIKAAKG TAAYMKSEDP IYVLENNIPI DTEYYLENQL SKPLLRIFNP VLKEKAESVL
     LKGDHTRTKI VVTSKVGALS AFTKKRAACI GCKAVLENND AAVCKHCKVK ESEIFQREVA
     QLGVLEEKFS RLWTQCQRCQ ESLHEDILCT SRDCPIFYMR KKVQKDLSDQ DKLMRRFGNL
     DW
//
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