ID   DP2L_METM6              Reviewed;        1131 AA.
AC   A9A8R5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=MmarC6_0923;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-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; CP000867; ABX01738.1; -; Genomic_DNA.
DR   RefSeq; WP_012193690.1; NC_009975.1.
DR   AlphaFoldDB; A9A8R5; -.
DR   SMR; A9A8R5; -.
DR   STRING; 444158.MmarC6_0923; -.
DR   EnsemblBacteria; ABX01738; ABX01738; MmarC6_0923.
DR   GeneID; 5738641; -.
DR   KEGG; mmx:MmarC6_0923; -.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OMA; KRRNCDG; -.
DR   OrthoDB; 559at2157; -.
DR   PhylomeDB; A9A8R5; -.
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_1000116095"
SQ   SEQUENCE   1131 AA;  128285 MW;  D859FF8022B7946F CRC64;
     MLHVSASKGM AEYFKNILDN VTELYTLADD CRKSGYDVTD HVEIPLAKDM ADRVEGIVGP
     KNVAERIREL VSDLGKEPAA LEIAKEIVEG KFGEFGREVG AEQAVRTALA VITEGIVAAP
     LEGIAHVKIK KNNDGSEYLA IYFAGPIRSA GGTAQALAVL VGDYVRKNMG LDKFKPTEDE
     VERYGEEVDL YQSEVTTFQY QPKAEEIRVA VRNISVEITG EATDDVEVSG HRDLPRVETN
     QIRGGALLAL VEGVLLKAPK ILRHVDKLGI EGWDWLKELK SKKEEVIEEI EEEKDDFNYE
     EEEDLSQYED YEVEAVTKFI GEVIAGRPVF SHPSKKGGFR LRYGRSRNTG FATDGFHPAI
     MYLVDDFMAV GTQLKTERPG KATCVVPVDS IEGPIVKLND KSVLKIDTVE KAKQYRDDVE
     EILFLGDILV NYGDFLENNH TILPSSWCVE WYEKILKSEN LEYTKEFIEN PDQKEAVTYA
     KLTKTPLHPK YTYFWHDISK DNINVLRNWL IGGKYNENND SWELTYNLED SEIATSKRYL
     ELIGCPHTVT AETVEIFEYY PLLYSLGYDF DKKQDIVEDI GEKLQNTKNN MHFINTIAPF
     EIRRNAYIYV GARMGRPEKA ASRKMKPPVN GLFPIGNAGA LVRLINKAVE EGKTDEIEIS
     NVKCSCGNVS LYRTCPFCGS SVEPSGPSRI KLPIKEYWYK ALENLKINKA GDVKCIKGMT
     SKDKIIEPLE KAILRAKNDI FVFKDGTTRF DCTDVPVTHF RPVEIHVGIE KLKFLGYLKD
     IHGNPLENEN QVLELKVQDV IVPESCMDYF FNVSKFIDDL LEKYYKKDRF YNVNKREELV
     GHLIIGMAPH TSAGMVGRII GYSYANVGYA HPYFHASKRR NCDGDEDAFF LLLDAFMNFS
     KRFLPDKRGG QMDAPLVLTT ILDPKEVDGE VHNMDSMWEY PLEFYEKSLE GIAPKEIKKI
     MQTVEDRLDK DSQYEGIGYT HETLKIDEGP LVCAYKTLGS MMEKTSAQLA VAKKIRATDE
     RDVAEKVIQS HFVPDLIGNL RAFSRQGVRC KCGAKYRRMP LKGVCRKCGS RLILTVSKGA
     VEKYMDVSQT MAEKYNASDY IKQRLEIIRS GIDSLFVNDK RKQVKIEDFF K