ID   DPOL3_SACSH             Reviewed;         763 AA.
AC   O05706;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=DNA polymerase 3;
DE            EC=2.7.7.7;
DE   AltName: Full=DNA polymerase B3;
DE   AltName: Full=DNA polymerase III;
GN   Name=dpo3;
OS   Saccharolobus shibatae (Sulfolobus shibatae).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=2286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9098062; DOI=10.1128/jb.179.8.2632-2640.1997;
RA   Edgell D.R., Klenk H.-P., Doolittle W.F.;
RT   "Gene duplications in evolution of archaeal family B DNA polymerases.";
RL   J. Bacteriol. 179:2632-2640(1997).
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   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; U92874; AAB53089.1; -; Genomic_DNA.
DR   AlphaFoldDB; O05706; -.
DR   SMR; O05706; -.
DR   PRIDE; O05706; -.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 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; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00136; DNA_pol_B; 2.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..763
FT                   /note="DNA polymerase 3"
FT                   /id="PRO_0000046485"
SQ   SEQUENCE   763 AA;  88197 MW;  7A7EFD9A5B9305E2 CRC64;
     MIKDFFILDF SYEIKDNIPL IYIWSIDDEG NSCVVVERNF KPYFYVVYEG NGDEIIENIR
     KNCEVLLITK VKRKYLGNVV DALLVQTFTP TQIKRCREKI SRINGIKSIF DADIRFTMRY
     SIDFDLRPFT WFKAEVSEVK LEGFRAKKVY ILDKILSHYE GKIPELRAIG IDFQIYSKYG
     SLNPRKDPIV VLSLWSKEGS MQFSLDESMD DLKIIRKFVD YILNYDPDII YVFDVDVFHW
     KYITERANSL GVKIDIGRKI GSEVSQGTYG HYSISGRLNV DLVGLLMNER LTGHIDLIEV
     ANYLGISPKR DSLNWYEISR YWDDEKNRDL VKQYSLENAK SIYLLGNFLL SPYSELVKII
     GLPLDKLSVA SWGNRIEASL IRTAAKSEEL IPIRMDNPNR SSKIKKTVIE PKIGIYSDVY
     VLDISSVYLS VIRKFNISPD TLVKGQCDDC YVSTISNYKF KKEPSGLYKT FLEELSNIQD
     TRKSKVIEEL MSSFYDYIHW INSRWYSREI ASAVDELSYE IGKLVIDLIK NSGFEVILAN
     DFLVFVKGGS GDKLNELIFK INSLYDLNLK VRKIYRSLLI LGNDRYAGLL EGDKIDIARI
     GKEDRDLCEL VRNVKRKVVE EILISKDVKK AVKLVKSAVI KLRRGEFDIG ELITWVHIEK
     DFSEYDKQLP FVVAARKAIQ SGYLISKDSR IGYLIVKGHG SVHDRAEPFF FVKEKNRIDI
     EYYVDQLLRE SLKVLTPLGV SEESLKKTNI TDILDMFGAS KKK