DPOL_MIMIV
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 23-FEB-2022, entry version 81.
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; Mimivirus.
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 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; 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; 3.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
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 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