ID   DP2L_METAR              Reviewed;        1134 AA.
AC   Q0W5U6;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
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}; Synonyms=pol2b;
GN   OrderedLocusNames=UNCMA_19460; ORFNames=RCIX896;
OS   Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the rice
RT   rhizosphere.";
RL   Science 313:370-372(2006).
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; AM114193; CAJ36247.1; -; Genomic_DNA.
DR   RefSeq; WP_012036271.1; NC_009464.1.
DR   AlphaFoldDB; Q0W5U6; -.
DR   SMR; Q0W5U6; -.
DR   STRING; 351160.RCIX896; -.
DR   PRIDE; Q0W5U6; -.
DR   EnsemblBacteria; CAJ36247; CAJ36247; RCIX896.
DR   GeneID; 5142819; -.
DR   KEGG; rci:RCIX896; -.
DR   PATRIC; fig|351160.9.peg.1995; -.
DR   eggNOG; arCOG04447; Archaea.
DR   OMA; KRRNCDG; -.
DR   OrthoDB; 559at2157; -.
DR   Proteomes; UP000000663; 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..1134
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000294700"
SQ   SEQUENCE   1134 AA;  126003 MW;  E6B275750F34B3D5 CRC64;
     MPPKTSEAQE AYFKKLEAEF LHCREIATAA RRKGYDPSLE VEIPSATDLA DRVEVIMGVP
     GLAAHIRKCE EKMSREEASL QVAADIAEGL VGKFKDEEEA VQCAVRTAVA VLTEGVVAAP
     LEGISAVKLA KNDDGTEYIK VYFAGPIRSA GGTAEALAVL AADYVRRKTG RAPYKIRDVE
     VERFVEEIML YKSIAHLQYT PTDEEIRLIV RNCPVCIDGE PTEQEEVQGY RNLERVETNR
     VRGGIALVIA EGIILKAPKV KKHVDKLKFD GWEWLDKIIA GSKPAGGENK EEEKKIKPKD
     KFLADLIAGR PVFGHPSRAG GFRLRYGRSR NTGFATAGIH PASMTIMDDF IATGTQLKVE
     RPGKAAAMVP VDSLEGPTVR LFNGDVVRIS DEKTALKVRP DVSQILDNGE IIINYGDFLE
     NNHTFVPSPY VEEWWIQDLE EKTKDKVEVN SPEEAFAVSE KYGVPLHPKY TYMWMDLTTD
     DVVYLARYIS ASGMVENGEL RLPVEQRSKS LLEILLIPQK VRDNTVILSA EDTYILCRCL
     GLNPDLSMKN PDAYAGLDSH AWKAVSALCG VTVMDRAPAR IGARMGRPEK SKLREMKPPV
     HVLFPVGEAG GMRRSLQDAS AYSKSMTDRI GEIEVEVGRR KCPDCGKMTY MVACECGGHT
     IPVYGCPDCG ISGIEGDCPK CHKPTTPNVK QKIDVKGLYA AALKRVGERD NFEVLKGVQG
     LISKEKTPEP LEKGILRAKH EVFVFKDGTI RYDMSDVPLT HFIPREIGLS VEKARELGYE
     KDTYGAPLES PEQVCELRVQ DIILSHDASN YLLKVCAFLD DELEKYYGLP RYYNVHEEQD
     LIGHLVIGLA PHTSAGVLGR IIGFVSSSAG YAHPFFHAAK RRNCDGDEDC VMMLMDGLLN
     FSLSYLPDRR GGKMDAPLVL SMRIDPKEID KESHNIDVMA RYPKEFYLAT REFKAPKDVE
     KIMDLVSKRL GTPEQYEGFK FTHGTSDIAA GPANSAYKTL GSMEDKLKAQ LELGRRLRAV
     DEKDVAERVI NSHFLPDLIG NLRAFSTQQM RCVKCGERYR RPPLTGTCPR CGGGRVILTV
     HEGAVTKYMD VSLAIAKEYG VPSYTIQRLE LLSLSIKSLF ENDKSKQTGL ADFM