ID   DP2L_METMA              Reviewed;        1152 AA.
AC   Q8PXH2;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=MM_1246;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM30942.1; -; Genomic_DNA.
DR   RefSeq; WP_011033195.1; NC_003901.1.
DR   AlphaFoldDB; Q8PXH2; -.
DR   SMR; Q8PXH2; -.
DR   STRING; 192952.MM_1246; -.
DR   PRIDE; Q8PXH2; -.
DR   EnsemblBacteria; AAM30942; AAM30942; MM_1246.
DR   GeneID; 1479588; -.
DR   KEGG; mma:MM_1246; -.
DR   PATRIC; fig|192952.21.peg.1452; -.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OMA; KRRNCDG; -.
DR   Proteomes; UP000000595; Chromosome.
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   Reference proteome; Transferase.
FT   CHAIN           1..1152
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000152577"
SQ   SEQUENCE   1152 AA;  128786 MW;  48FDEEBAB8546737 CRC64;
     MGETIASEEM HRYFDGLEAR LKEAIEIANR ARARGGDPRP VVEIPLAKDL ADRVENLIGV
     KGVAEKIREL EARMSREEAA LEIGKQVAEG VVGSFPSKKD AVEAAIRVSM AVLTEGVVAA
     PIEGIDKVDL GKNDDGSQYI RIFYSGPIRS AGGTAQALSV LVGDYVRRGI GIDRYKPREE
     EVERYVEEIL LYKRVASLQY TPSEDEIRLI VRNCPVCIDG DPTEEAEVEG HRDLERIGTN
     RVRGGMCLVL AEGLALKAPK VKKHVNKLKM DGWDWLETLI GGAKSGESDE DEQKNKIKPK
     DKYIRDLIAG RPVFSHPSRP GGFRLRYGRS RNTSFASAGI NPAGMVLLDD FITNGTQLKI
     ERPGKAAAMS AVDSIEGPTV RLFSGDLIRV DDIKEAYEVR QQVEVIVDIG EILINYGDFL
     ENNHPLMPSP YVFEWWIYDY ESVCSEKILE KDLKNPSASL ALKLAEKYNV PLHPKFTYLW
     HDINRNEFEA LRKFVAEKGT FLEGEGEGEG EGILKLPLED SVKEGIKPVL EKLLVLHKVK
     EGGIFVEEAL PFILCLGLDR SLKEKVSMPD TGDMVEAAGI LSGFKVYPKA PSRIGARMGR
     PEKSDLRKMS PAAQVLFPIS NAGGMTRNLV SASDYTSCMN AKIGEIEVEL GLRECPACGK
     ESYFWRCECG EFTNPKLSCP RCKIDVRGAE TCPKCGRKPT SVANVKLDFR PIYKQAFENV
     GERERMDIIK GVKRLMNGQM TPEPLEKGIL RAKHDVYIFK DGTVRYDMSD IPLTHIRADE
     LGITAARLRE LDYKEDIYGK PLERDDQVVC LKVQDLLLSY DGAEYMLRTA KYVDELLVKY
     YKVEPYYNAE TIQDLVGVLM IGLAPHTSAG VLGRLIGFTK ASVGYAHPFF HASKRRNCDG
     DEDCVMLLMD GILNFSRSYL PEKRGGKMDA PLVLTTRIDP KEVDKEAHNI DLLARYPLEF
     YRATQEIKNP TEIESIMDLV SSRLGKPDQY EHFMFTHDTS NIAAGPLKSS YKTLGSMIEK
     MEAQLSLAGK IRAVDAPDVA ERVLKSHFLP DLIGNLRSFS RQRMRCIKCG EKFRRPPLTG
     ACPKCGGNVV LTVHEGAVRK YLEISKEIGE RYGVSSYTRQ RIELLDYDIC SLFENHKVKQ
     LGLSDFMSGS AR