ID   DP2L_METM5              Reviewed;        1131 AA.
AC   A4G0G9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=MmarC5_1656;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000609; ABO35953.1; -; Genomic_DNA.
DR   RefSeq; WP_011869400.1; NC_009135.1.
DR   AlphaFoldDB; A4G0G9; -.
DR   SMR; A4G0G9; -.
DR   STRING; 402880.MmarC5_1656; -.
DR   EnsemblBacteria; ABO35953; ABO35953; MmarC5_1656.
DR   GeneID; 4928217; -.
DR   KEGG; mmq:MmarC5_1656; -.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OMA; KRRNCDG; -.
DR   OrthoDB; 559at2157; -.
DR   Proteomes; UP000000253; 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   Transferase.
FT   CHAIN           1..1131
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_1000019389"
SQ   SEQUENCE   1131 AA;  128289 MW;  7D2826B4CE998567 CRC64;
     MLHVSASKGM TEYFKNILDN VKNLYDLAEG CRKSGYDVTD HVEIPLAKDM ADRVEGIVGP
     KNVAERIREL VSDLGKEPAA LEIAKEIVEG KFGEFGREVG AEQAVRTALA VITEGIVAAP
     LEGIAHVKIK KNNDGGEYLA IYFAGPIRSA GGTAQALAVL VGDYVRKNMG LDKFKPTDDE
     VERYGEEVDL YQSEVTTFQY QPKAEEIRVA VRNISVEITG EATDDVEVSG HRDLPRIETN
     QIRGGALLAL VEGVLLKAPK ILRHVDKLGI EGWDWLKELK SKKEELVEEI EEENDEFNYE
     EEEDLSQYED YEVEAVTKFI GEVIAGRPVF SHPSKKGGFR LRYGRSRNTG FATDGFHPAI
     MYLVDDFMAV GTQLKTERPG KATCVVPVDS IEGPIVKLND KSVLKIDTVE KAKQYRDDVE
     EILFLGDILV NYGDFLENNH TILPSSWCTE WYEKILKSEN LEYTKEFIEN PDQKEVVKYA
     KLTNTPLHPK YTYFWHDISK DNINVLRNWI IGGRYNESND SWGLTYDPED PEISIVKRYL
     ELIGCPHTVV DEKVEIFEYY PLLYSLGYDF DEKQDVVEDI EEKLQNTKNN MHFINTIAPF
     EIRRNAYIYV GARMGRPEKA ASRKMKPPVN GLFPIGNAGA LVRLINKAVD EGKTDEIEIS
     NVKCSCGNVS LYRTCPFCGS SVEPSGPSRI KLPIKEYWYK ALENLKINKA GDVKCIKGMT
     SKDKIIEPLE KAILRAKNDI FVFKDGTTRF DCTDVPVTHF RPVEIHGDIE KLKSLGYLKD
     IHGNPLENEN QVLELNVQDV IVPESCMDYF LNVSKFIDDL LEKYYKKDRF YNVNKREELV
     GHLIIGMAPH TSAGMVGRII GYSKANVGYA HPYFHASKRR NCDGDEDAFF LLLDAFMNFS
     KRFLPDKRGG QMDAPLVLTT ILDPKEVDGE VHNMDSMWEY PLEFYEKSLE GIAPKEIKKI
     METVEDRLDK ESQYEGIGYT HETLKIDEGP LVCAYKTLGS MMEKTSAQLA VAKKIRATDE
     RDVAEKVIQS HFVPDLIGNL RAFSRQGVRC KCGAKYRRMP LKGICRKCGS RLILTVSKGA
     VEKYMDVSQT MAEKYNASDY IKQRLEIIRS GIDSLFVNDK RKQVKIEDFF K