ID   DPOL_MIMIV              Reviewed;        1740 AA.
AC   Q5UQR0;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=DNA polymerase;
DE            EC=2.7.7.7;
DE   Contains:
DE     RecName: Full=Mimv polB intein;
GN   Name=POLB; OrderedLocusNames=MIMI_R322;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus;
OC   Mimivirus bradfordmassiliense.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISCUSSION OF SEQUENCE.
RX   PubMed=15707490; DOI=10.1186/1743-422x-2-8;
RA   Ogata H., Raoult D., Claverie J.-M.;
RT   "A new example of viral intein in Mimivirus.";
RL   Virol. J. 2:8-8(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
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; AY606804; AAU11330.1; -; Genomic_DNA.
DR   EMBL; AY653733; AAV50591.1; -; Genomic_DNA.
DR   RefSeq; YP_003986825.1; NC_014649.1.
DR   MEROPS; N10.007; -.
DR   GeneID; 9924939; -.
DR   KEGG; vg:9924939; -.
DR   Proteomes; UP000001134; Genome.
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:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   CDD; cd00081; Hint; 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; 3.10.28.10; Homing endonucleases; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 2.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR030934; Intein_C.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 3.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   SUPFAM; SSF55608; Homing endonucleases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 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   Reference proteome; Repeat; Transferase; Viral DNA replication.
FT   CHAIN           1..1052
FT                   /note="DNA polymerase, 1st part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000041777"
FT   CHAIN           1053..1403
FT                   /note="Mimv polB intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000041778"
FT   CHAIN           1404..1740
FT                   /note="DNA polymerase, 2nd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000041779"
FT   DOMAIN          1189..1334
FT                   /note="DOD-type homing endonuclease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT   REGION          472..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1673..1701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1680..1701
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1740 AA;  201945 MW;  DC8B2AFF4EEE7724 CRC64;
     MPSETIDSTK QFEFQISDWN SYHELDQEEE EKYVIQLFGR TEDDHDVCLK VTGYTPFFYV
     EIPKQWKQRQ VDKFVEILKN KVQYHCKKNL DEDFDLSKSL IKYAMVKKHK FYNFRNKQLY
     NFLLLVFKSH TAMKEFSSIL ARPLEAKGLT NKPMLYQRYE SNIEPHIRFM HINNLSSCGW
     ASIDKDKLKK IPEYSNCDYS FSVNWKDVKP SNNDDRMAPF KIMGYDIECV SCDQNFPQAE
     RPSDKIIQIG ITMYRYGSMK CYEQHILTLK KCAPIEGVNV ECYKKEKGLL RGFAKKIAEL
     RPDFKTGYNN FGFDDKYIYD RILRIDKREG KKQGVNINAL KNKFMDEILR TIGKVNNNYL
     IENEGLDRIP IYTTVKDKKI SSKASRFIQI RGGTYVENGN NLKYVQSPGI TYFEVKNLSS
     SALGDNELKF IQIPGVLSID MMKVIQRDHR LIGYKLDNVS ANFITEKADK IIEMPHNQED
     SDSEKEDEDT DDKTYDVNIY TKSTKALEKD SYIQIMVNDG YSSSPLSEGA KYKVYDIQTI
     TEKKLNEKTN KEEIFVYQAI KTKICQKDIQ QLRETIKNPL LGISWTFAKD DMHHTKINEY
     FEEGDPKKIR QIAKYCLKDC KLVNLLLAKL EIIVNSVGMA KVCHVPLSYL FLRGQGVKIF
     SLVSKKCREK NFLIPVLRRK SKDNEGDEDE TYEGATVITP KPNVYLSPIG VLDYSSLYPN
     SMRERNLSQE CYVDDSKYDN LPGYIYHDVE IILKDKKGKI LRNIDGTPQK EYHRFAQEII
     TDEQINRELK DIFDKINTVF ENNVAIIQNQ KYFTEKNISE LIDKHKNISD SKIEDIEFDE
     SLSDKRKNKL VDAEKDSLDK NIGFYQKIKS QIDKIKLDSK IEIDNLSKNL NEEEKSKQIN
     KMELNTKNLI SKVFSKYLIT EQQREELIVL EKERAKRSVN AEKAKVYNTV DGITVRYGIL
     PEILTELLNK RKETNGKLAN EKDPFVKAIL NALQLAFKVT ANSLYGQTGA PTSPLYFIAI
     AACTTAIGRE RLHYAKKTVE DNFPGSEVIY GDSVTGDTPI ITRHQNGDIN ITTIEELGSK
     WKPYEIFKAH EKNSNRKFKQ QSQYPTDSEV WTAKGWAKIK RVIRHKTVKK IYRVLTHTGC
     IDVTEDHSLL DPNQNIIKPI NCQIGTELLH GFPESNNVYD NISEQEAYVW GFFMGDGSCG
     SYQTKNGIKY SWALNNQDLD VLNKCKKYLE ETENIQFKIL DTMKSSSVYK LVPIRKIKYM
     VNKYRKIFYD NKKYKLVPKE ILNSTKDIKN SFLEGYYAAD GSRKETENMG CRRCDIKGKI
     SAQCLFYLLK SLGYNVSINI RSDKNQIYRL TFSNKKQRKN PIAIKKIQLM NETSNDHDGD
     YVYDLETESG SFHAGVGEMI VKNTDSIFIN FHIKDENGEE KTDKEALMKT IAKCQRAAKL
     INQNVPKPQS IVYEKTLHPF ILVAKKKYVG LLFEKSPDKY FLKSMGIVLK RRDNAPIVKI
     VVGGIIDNIL KNRDIDKAIE YTKIVLDKLM NGEYPMDKFI ISKTLKSRYK KPSTIAHKVL
     ADRMAVRDPG NKPQINDRIP FVYIVKDMGK KKKKDILQGD LIEHPEYVIA NNLKIDYLYY
     LEHQIINPAS QILELMMDTK DVQKFFNKYI IDEQNKRKGA QSLTKWMDFS KLPKESGSKT
     AKKPYQSQKL QKTKSSNKSQ IDPKYINLIK NKSRKHECQN MNKWISSTDK CTDDWEPIVE
//