ID   DP2L_METM7              Reviewed;        1131 AA.
AC   A6VI14;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, 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=MmarC7_1023;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
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., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000745; ABR66090.1; -; Genomic_DNA.
DR   RefSeq; WP_011977403.1; NC_009637.1.
DR   AlphaFoldDB; A6VI14; -.
DR   SMR; A6VI14; -.
DR   STRING; 426368.MmarC7_1023; -.
DR   PRIDE; A6VI14; -.
DR   EnsemblBacteria; ABR66090; ABR66090; MmarC7_1023.
DR   GeneID; 5329159; -.
DR   KEGG; mmz:MmarC7_1023; -.
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..1131
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_1000019390"
SQ   SEQUENCE   1131 AA;  128380 MW;  143EE34A3D4BE0B5 CRC64;
     MLHVSASKGM TEYFKNILDN VTELYTLADD CRKSGYDVTD HVEIPLAKDM ADRVEGIVGP
     KNVAERIREL VSDLGKEPAA LEIAKEIVEG KFGEFGREVG AEQAVRTALA VITEGIVAAP
     LEGIAHVKIK KNNDSGEYLA IYFAGPIRSA GGTAQALAVL VGDYVRKNMG LDKFKPTEDE
     VERYGEEVDL YQSEVTTFQY QPKAEEIRAA VRNISVEITG EATDDVEVSG HRDLPRVETN
     QIRGGALLAL VEGVLLKAPK ILRHVDKLGI EGWDWLKELK SKKEEVIEEI EEEKDDFNYE
     EEEDLSQYED YEVEAVTKFI GEVIAGRPVF SHPSKKGGFR LRYGRSRNTG FATDGFHPAI
     MYLVDDFMAV GTQLKTERPG KATCVVPVDS IEGPIVRLKD KSVLKIDTVE KAKQYRDDVE
     EILFLGDILV NYGDFLENNH TILPSSWCTE WYEKILKSEN LEYKKEFIEN PDQKEAVNYA
     KLTKTPLHPK YTYFWHDISK DNINVLRNWI IGGKYNESND SWEVTYDSEN PEISNAKRYL
     ELIGCPHTVT GEKLEIFEYY PLLYSLGYDF DEKRDIVEEI EEKLQNTKNN MHFINTIAPF
     EIRRNAYIYV GARMGRPEKA ASRKMKPPVN GLFPIGNAGA LVRLINKAVE EGKTDEIEIS
     NVKCSCGNVS LYRTCPFCGN SVEPSGPSRI KLPIKEYWYK ALENLKINKA GDVKCIKGMT
     SKDKIIEPLE KAILRAKNDI YVFKDGTTRF DCTDVPVTHF RPVEIHVGIE KLKSLGYLKD
     IHGNSLENED QVLELKVQDV IVPESCMDYF FNVSKFIDDL LEKYYKKDRF YNVNKRDDLV
     GHLIIGMAPH TSAGMVGRII GYSNANVGYA HPYFHASKRR NCDGDEDAFF LLLDAFMNFS
     KRFLPDKRGG QMDAPLVLTT ILDPKEVDGE VHNMDSMWEY PIEFYEKSLE GIAPKEIKKI
     MQTVEDRLDK DSQYEGIGYT HETLKIDEGP LVCAYKTLGS MMEKTSAQLA VAKKIRATDE
     RDVAEKVIQS HFVPDLIGNL RAFSRQGVRC KCGAKYRRMP LKGVCRKCGS RLILTVSKGA
     VEKYMDVSQT MAEKYEASDY IKQRLEIIRS GIDSLFVNDK RKQVKIEDFF K