ID   DP2L_METTH              Reviewed;        1092 AA.
AC   O27579;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=DNA polymerase II large subunit;
DE            Short=Pol II;
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; OrderedLocusNames=MTH_1536;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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;
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:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family.
CC       {ECO:0000305}.
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DR   EMBL; AE000666; AAB86010.1; -; Genomic_DNA.
DR   PIR; H69071; H69071.
DR   AlphaFoldDB; O27579; -.
DR   SMR; O27579; -.
DR   STRING; 187420.MTH_1536; -.
DR   EnsemblBacteria; AAB86010; AAB86010; MTH_1536.
DR   KEGG; mth:MTH_1536; -.
DR   PATRIC; fig|187420.15.peg.1498; -.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OMA; KRRNCDG; -.
DR   Proteomes; UP000005223; 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; 2.
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..1092
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000152578"
SQ   SEQUENCE   1092 AA;  123060 MW;  AA6970F7A6F42DFF CRC64;
     MMDYFNELER ETERLYEIAR KARARGLDVS TTPEIPLAKD LAERVEGLVG PEGIARRIKE
     LEGDRGREEV AFQIAAEIAS QAVPDDDPEE REKLADQALR TALAILTEGV VAAPLEGIAR
     VRIKENFDKS RYLAVYFAGP IRSAGGTAAA LSVLIADYIR LAVGLDRYKP VEREIERYVE
     EVELYESEVT NLQYSPKPDE VRLAASKIPV EVTGEPTDKV EVSHRDLERV ETNNIRGGAL
     LAMVEGVIQK APKVLKYAKQ LKLEGWDWLE KFSKAPKKGE GEEKVVVKAD SKYVEDIIGG
     RPVLAYPSEK GAFRLRYGRA RNTGLAAMGV HPATMELLQF LAVGTQMKIE RPGKGNCVVP
     VDTIDGPVVK LRNGDVIRIE DAETASRVRS EVEEILFLGD MLVAFGEFLR NNHVLMPAGW
     CEEWWIQTIL SSPKYPGDDP LNLSYYRTRW NELEVSAGDA FRISEEYDVP LHPRYTYFYH
     DVTVRELNML REWLNTSQLE DELVLELRPE KRILEILGVP HRVKDSRVVI GHDDAHALIK
     TLRKPLEDSS DTVEALNRVS PVRIMKKAPT YIGTRVGRPE KTKERKMRPA PHVLFPIGKY
     GGSRRNIPDA AKKGSITVEI GRATCPSCRV SSMQSICPSC GSRTVIGEPG KRNINLAALL
     KRAAENVSVR KLDEIKGVEG MISAEKFPEP LEKGILRAKN DVYTFKDATI RHDSTDLPLT
     HFTPREVGVS VERLRELGYT RDCYGDELED EDQILELRVQ DVVISEDCAD YLVRVANFVD
     DLLERFYDLE RFYNVKTRED LVGHLIAGLA PHTSAAVLGR IIGFTGASAC YAHPYFHSAK
     RRNCDSDEDS VMLLLDALLN FSKSYLPSSR GGSMDAPLVL STRIDPEEID DESHNIDTMD
     MIPLEVYERS FDHPRPSEVL DVIDNVEKRL GKPEQYTGLM FSHNTSRIDE GPKVCLYKLL
     PTMKEKVESQ ITLAEKIRAV DQRSVVEGVL MSHFLPDMMG NIRAFSRQKV RCTKCNRKYR
     RIPLSGECRC GGNLVLTVSK GSVIKYLEIS KELASRYPID PYLMQRIEIL EYGVNSLFES
     DRSKQSSLDV FL