ID   DP2L_METST              Reviewed;        1117 AA.
AC   Q2NHG2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
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=Msp_0255;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(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; CP000102; ABC56671.1; -; Genomic_DNA.
DR   RefSeq; WP_011405871.1; NC_007681.1.
DR   AlphaFoldDB; Q2NHG2; -.
DR   SMR; Q2NHG2; -.
DR   STRING; 339860.Msp_0255; -.
DR   GeneID; 41324828; -.
DR   KEGG; mst:Msp_0255; -.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OrthoDB; 7529at2157; -.
DR   Proteomes; UP000001931; Chromosome.
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:0008310; F:single-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0006308; P:DNA catabolic process; 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   NCBIfam; TIGR00354; polC; 1.
DR   PANTHER; PTHR42210; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR   PANTHER; PTHR42210:SF1; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR   Pfam; PF03833; PolC_DP2; 1.
DR   PIRSF; PIRSF016275; PolC_DP2; 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..1117
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000294693"
FT   REGION          279..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1117 AA;  124988 MW;  DE1855748F768A1F CRC64;
     MDYFGMLEEK TKELYAIARE ARKQGKDLEL EPEIPLAKDL AERVEGLVGP EGVAKRIKEL
     EKSMSREEVA FQIAKEIATK DDVEGQPNDY EVQEANADSA IRTALAILTE GVVAAPLEGI
     AKVKIKDNSD GTKCFGVYFA GPIRSAGGTA AALAVLLGDY IRMSQGLDRY KPTDDEIERY
     VEEVELYESE VTNLQYSPTP DEVRLAIRGI PVEVTGEQTD PVEVQNRDLP RVETNNLRGG
     ALLAVAEGVI QKSRKIVKYA KTLKIDGWDW LEYFTAPKST KEEEKKKEES SENKPKKKAK
     YMEDIIGGRP VMSYPGAKGG FRLRYGRTRD SGLASMAIHP ATMEIVEFLA IGTQMKIEKP
     GKGNCVVPCD SIEGPIVKLK NGDVIQVNDV SKAISIRRDV NEIIFLGDML VAFGEYLRGN
     IPLDVSAWCE EWWAQEIEAS EYFKETHDTF GIDFNENMEL NALLKLDIDA KKAFDIAKKT
     NTPLHPKFTF YYNDVTKEEL NDLHNYLYSL IDSPEDVFKS DMNRIPIDYH KRIIEVLGIP
     HHVNNKSLIM SNDNLYTLMS VLNKSLSPDE DMETIEAVNM ISPVSIKSKA PTYIGGRVGR
     PEKTKERLMK PAPHSLFPIG NYAGNIRNIV EAAKKGTIKV TLAKCKCTNP DCKVSSFKAL
     CPVCGSRTEL ESSAAKNIKL DKLLMDAFEN VNVRRLDEVK GVKGLISEDK YPEPLEKGIL
     RARNDVFTYR DGTIRHDSTD LPLTHFIPRE VGVPYEKILE MGYTEDIYGK PITNDNQIIE
     IKIQDIVVSE SCGDYLLKVS KFIDDLLIRY YHMEPFYNAE NRVDLVGHLI AGLAPHTSAG
     VLGRIVGFTK ASCCYAHPYF HSAKRRNCDS DEDAVMLLLD ALLNFGKTYL PSTRGGSMDA
     PLVLSIRIDP EEIDDESHNI DCMKRIPLEI YHKTEEGGVK PSDVNDLVDN VESRLGTDNQ
     YHGLMYSHPT SSIHAGPKIC LYKTLQTMTD KVESQIALAE LLRAVDQKGV VEGVLNSHFL
     PDMAGNIRAF SRQKVRCTKC GAKYRRIPLS GECTCGNNLI LSISKGSVLK YLDISKDLSH
     RYPINPYVVE RIEILETGIN SLFESDKSKQ SSLDAFF
//