ID   DP2L_METBF              Reviewed;        1146 AA.
AC   Q46E19;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=DNA polymerase II large subunit {ECO:0000255|HAMAP-Rule:MF_00324};
DE            Short=Pol II {ECO:0000255|HAMAP-Rule:MF_00324};
DE            EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_00324};
DE   AltName: Full=Exodeoxyribonuclease large subunit {ECO:0000255|HAMAP-Rule:MF_00324};
DE            EC=3.1.11.1 {ECO:0000255|HAMAP-Rule:MF_00324};
GN   Name=polC {ECO:0000255|HAMAP-Rule:MF_00324}; OrderedLocusNames=Mbar_A0899;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
CC   -!- FUNCTION: Possesses two activities: a DNA synthesis (polymerase) and an
CC       exonucleolytic activity that degrades single-stranded DNA in the 3'- to
CC       5'-direction. Has a template-primer preference which is characteristic
CC       of a replicative DNA polymerase (By similarity). {ECO:0000250}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00324};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.11.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00324};
CC   -!- SUBUNIT: Heterodimer of a large subunit and a small subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00324}.
CC   -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family.
CC       {ECO:0000255|HAMAP-Rule:MF_00324}.
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DR   EMBL; CP000099; AAZ69873.1; -; Genomic_DNA.
DR   RefSeq; WP_011305922.1; NC_007355.1.
DR   AlphaFoldDB; Q46E19; -.
DR   SMR; Q46E19; -.
DR   STRING; 269797.Mbar_A0899; -.
DR   PRIDE; Q46E19; -.
DR   EnsemblBacteria; AAZ69873; AAZ69873; Mbar_A0899.
DR   GeneID; 3625944; -.
DR   KEGG; mba:Mbar_A0899; -.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OMA; KRRNCDG; -.
DR   OrthoDB; 559at2157; -.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008852; F:exodeoxyribonuclease I activity; IEA:UniProtKB-EC.
DR   GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00324; DNApol_II_L_arch; 1.
DR   InterPro; IPR004475; PolC_DP2.
DR   InterPro; IPR016033; PolC_DP2_N.
DR   PANTHER; PTHR42210; PTHR42210; 1.
DR   Pfam; PF03833; PolC_DP2; 1.
DR   PIRSF; PIRSF016275; PolC_DP2; 1.
DR   TIGRFAMs; TIGR00354; polC; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW   Hydrolase; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN           1..1146
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000294692"
SQ   SEQUENCE   1146 AA;  128094 MW;  867140FA2D6E386A CRC64;
     MGETIASKEM HEYFDELEAR LKKAIEIANT ARARGGDPKP VVEIPLAKDL ADRVENLIGV
     EGVAAKIRVL EEKMSREECA LEIGRQVAEG EVGNFATKKD AVEAAIRVSM AVITEGVVAA
     PIEGINKVEL GKNDDGSEYI RIFYSGPIRS AGGTAQALSV LVGDYVRRGI GIDRYKPRPE
     EVERYVEEIV LYKRVASLQY MPSEDEIRLI VKNCPVCIDG DPTEEAEVEG HRNLERIGTN
     RIRGGMCLVL AEGLALKAPK VKKHVNKLNM DGWDWLDILI GGAKTGGDEE DEKKNKIKPK
     DKYIRDLIAG RPVFSHPSRP GGFRLRYGRS RNTSFAAAGI NPSTMVLLDD FITNGTQLKV
     ERPGKAAAMS AVDSIEGPTV RLYSGDLVRI DDIKEAYELR SQVEVIVDIG EILINYGDFL
     ENNHPLMPSP YVFEWWRYDY EAACSEIIPE DELKDPSSAL ALRLAEEYDV PLHPKFTYLW
     HDINRTEFEA LRKFVVGRGN FSVEDEILRL PLKACIENGV KLILEKLLVL HRVKADTILI
     KEALPFILCL GLDCHLKEKA PMPDTDNMVN ATAFLSGFKV LPRAPSRIGA RMGRPEKANL
     RKMSPAAQVL FPIGNAGGLT RNLVSASNYS VSMNGKIGEI EVEMGIRECP ACGKETYFWR
     CDCGEYTRPK LFCPRCKIEV RNSETCPKCG RKPTSVSNVK LDFRSIYKRA FENVGEREKM
     DLIKGVKRLM NGQMTPEPLE KGILRAKHDV YIFKDGTVRY DMSDIPLTHV RADEIGITAA
     KLRELGYVED IYGNPLERDD QIVCLKVQDL VISYDGGGYM LRTAQYVDDL LVKYYGVEPY
     YNAKTIQDLV GVLLIGLAPH TSAGVLGRLI GFTRASVGYA HPFFHASKRR NCDGDEDCVM
     LLMDGILNFS RAYLPEKRGG KMDAPLVLTT RIDPKEVDKE AHNIDLPARY PLEFYRATQE
     IKNPTELEGI MDLVSSRLGT PEQYEHFMFT HDTSDIAAGP LNSSYKTLGS MIDKMEAQLS
     LANKIRAVDA PDVAERVLKS HFLPDLLGNL RSFSRQRMRC IKCGAKFRRP PLTGACPKCG
     GNVVLTVHEG AVRKYLEISK EIGKRYGVSS YTQQRIELLD KDICSLFENH RVKQLGISDF
     MSGSAR