ID   DPOL_CEV01              Reviewed;        1623 AA.
AC   A7U6F1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   23-FEB-2022, entry version 65.
DE   RecName: Full=DNA polymerase;
DE            EC=2.7.7.7;
DE   Contains:
DE     RecName: Full=CeV01 dpo intein;
GN   Name=dpo;
OS   Chrysochromulina ericina virus (CeV01).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae; unclassified Phycodnaviridae.
OX   NCBI_TaxID=455364;
OH   NCBI_TaxID=156174; Haptolina ericina.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=18359826; DOI=10.1128/aem.02548-07;
RA   Larsen J.B., Larsen A., Bratbak G., Sandaa R.A.;
RT   "Phylogenetic analysis of members of the Phycodnaviridae virus family,
RT   using amplified fragments of the major capsid protein gene.";
RL   Appl. Environ. Microbiol. 74:3048-3057(2008).
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   -!- PTM: This protein undergoes a protein self splicing that involves a
CC       post-translational excision of the intervening region (intein) followed
CC       by peptide ligation. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; EU006632; ABU23716.1; -; Genomic_DNA.
DR   MEROPS; N10.007; -.
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:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.10.28.10; -; 1.
DR   Gene3D; 3.30.420.10; -; 2.
DR   Gene3D; 3.90.1600.10; -; 2.
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; IPR036844; Hint_dom_sf.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR006142; INTEIN.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR004042; Intein_endonuc.
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; 2.
DR   PRINTS; PR00106; DNAPOLB.
DR   PRINTS; PR00379; INTEIN.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF51294; SSF51294; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF55608; SSF55608; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Protein splicing;
KW   Repeat; Transferase; Viral DNA replication.
FT   CHAIN           1..964
FT                   /note="DNA polymerase, 1st part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338005"
FT   CHAIN           965..1335
FT                   /note="CeV01 dpo intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338006"
FT   CHAIN           1336..1623
FT                   /note="DNA polymerase, 2nd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338007"
SQ   SEQUENCE   1623 AA;  187901 MW;  669E878EF1B17322 CRC64;
     MSQWQFKLFE FDIREELETD KNEFIPGRDT KRFIIQMYGI DENGKTACIF VKGFNPFFYV
     KVLDEWDNSK VTEFVAFVRK EMGAYFGDSL VSAKIVYRHK FYEFDNKKLY KFVQLKFTSI
     GAFNKCKNLW YNETKYGEDR KLKENGLEFL DTKTTLYEAQ VPPLLRLFHI RQIKPSGWVA
     LKNGHYSQNR KQLTTCDYEF TVNYKNIYPI NDERLEKICV PFKILSLDIE ASSSHGDFPL
     ARKNYLKLAT NIVDYLINNN IETCDKDLLS NLIKTGFSYR INKDIEKIYL KKSITEEELD
     ELIDNLVDIK PGKKENYIDI KDEDENSDSS DIENDGIVEE FTTKKRQKVT GTKNKDSNIL
     EIINDLTCNR NTRILELAKC FGQHNPNRDN KWEGKFPELE GDQVTIIGST IRRNGEDKPY
     LQHAIVVNDC NSIDNVVIES YKTERDALLA WTNFVQRENP DIIIGYNHHG WDEGFMYDRS
     IELNCMTQFS KLSRFKNEKC IKEIFQGKNK PKKITIEESS TKLASGQFDL RYFKMSGRLQ
     IDFLNLFRRE EQLPSYKLDY VAGHFIGDNI KKIEYDENCS ILYSKNLTGL SKNDYIVIQE
     IGYSTDQYAN GKKFKVLDIV DDKIILNDKI TPDTNKILRW CLGKDDVGPQ DIFRLTNEGP
     EGRAIVTKYC IKDCDLVQDL MRKNDTMTSY DEMSNLCWVP KSFLVTRGQG IKLTSYVAQK
     CREKNTLMPV IDKGIDGEGY EGAIVLEPKC NLYLKKPVAC VDYSSLYPSS IISENISHDS
     KVWTKEYDLD DNLINETGEK DENGKFIYDE LPEYDYIDIT YDTFKWIRKT PKAAATKVKS
     GYKTCRYVQF QNNEKAILPS ILDELLGARK STKRQMKNET DPFMQNVLDK RQLSIKITAN
     SLYGQAGAKT STFYDKDIAA STTATGRKLL IYAKELIEAC YDNTIEETTN YGEVKCYGEY
     IYGDSVASYT PIYVRYNKSI IDICSVEELA EKYGNGWHLE SPKEYCELNN IESWTENGWT
     ECHRVIRHRL APYKKMVRIL THTGLVDVTD DHSLVKNTGE EISPKDVSIG TKLLHCTMSE
     NESNIESDIS IDEARIMGFF FGDGSCGIYD CPSGHKASWA LNNSNKELIE KYYNLCKSVY
     PEFEWKVYDT LNSSGVYKIC FNKKSGSKSK IQFIEKYRSM LYNKKSKIIP SEIINGSIEL
     RKSFWEGLYD ADGDKDKNGY TRIDQKSQIS AAYICWLANS IGYKTSLNIR DDKTDIYRIT
     ATKNKQRRDG DKIKKIVNIQ NSANIQNSAN IQNSVNIQNS VNIQNSKDNQ DYVYDLTTEN
     HHHFAAGIGN MIVHNTDSVF FTFNLKDLDS KEIVGKKALE ITIELAKKAG WLATMFLKSP
     HDLEYEKTFL PFCLLSKKRY VGILYEEDPN KGKRKEMGLV LKRRDNCAQV KDVYGGAIDI
     LMKDQVVHKA VDFVKHSLQD VIDEKISQQK LIITKSLRSY YKNPKQIAHN VLAIRIGERD
     PGNKPKPGDR MEFIYIKNSD KKALQGDRIE TPLFINENNI EIDYGFYITN QIMKPLQQLF
     ALVLEDMEDF VTKRGISMKS WKAEIDKLHE KWTEPDKFSK KYEELRCKEV KSILFDPYIK
     LLK