ID   DP2L_METTP              Reviewed;        1109 AA.
AC   A0B8K5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Mthe_1250;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) 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; CP000477; ABK15029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B8K5; -.
DR   SMR; A0B8K5; -.
DR   STRING; 349307.Mthe_1250; -.
DR   EnsemblBacteria; ABK15029; ABK15029; Mthe_1250.
DR   KEGG; mtp:Mthe_1250; -.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OMA; KRRNCDG; -.
DR   Proteomes; UP000000674; 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..1109
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000294691"
FT   REGION          571..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..586
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1109 AA;  122895 MW;  9CAFADACAC8D75C2 CRC64;
     MSAEYFERLE RGLREEMEIA RRARSKGLDP ETDVEIPIAV DLAERVEKLV SIPGVAERIR
     EFEVQGLSRE EAALAIGRDF AEGRLGKGAS RLDAIDMAIR TSVALLTEGV VAAPIEGIAR
     VGLGKNDDGS EYLKVYYAGP IRSAGGTAQA LSVLVADYVR RSMGIAPYKP TDEEIERYVE
     EIGLYKRLQH LQYTPSDDEI RTIIRNCPVC IDGEPTEEEE VSGYRDLPRV ETNRVRGGIA
     LVSAEGIALK RPKIKKHVSK LGIDGWGWLD VLGGEKKDGG GSSGKFLRDL IAGRPVFSHP
     SRPGGFRLRY GRSRNTGLAA AGINPATMMV LNQFLAPGTQ IKVEQPGKAA AVAPVSSIEG
     PTVRLTNGDV VRIDDPSSFP WISSPEALRR NISKIIDLGE ILVSFGDFME NNRPLAPASY
     TFEWWAEEFR RAGGDPAGME HVDGRTAIRL SRDFGVPLHP DHTYLWHDIT LDELDLLADA
     ASDGEIDGDA LLMDMREDVK EVLEKLLVHH KVRDGMIVVE DALPLLLCLG VDETGRRWRR
     EDLNADNALS AVNQLSGLVI RARAPTRIGC RMGRPEKSDR REMRPPPHVL FPTGSEGGKS
     RLVNEAAEHG FIEVVVERRR CPSCGKEGFA FRCECGAHTE RVRACLSCGV RADDKCPRCG
     TETSAATRMR IDVKGTLARA LESLGERVDN IRGVMGLTSR DSTPEPLEKG VLRAKHGVFI
     FKDGTSRYDL TDLPLTHFRP REIGTSVDAL LDLGYTHDIH GKPLESDDQI LELKVQDVVL
     CRNAGDWLLR VSKFIDDLLV KFYGLEPYYN AERPEDLIGR LMIGLAPHTS AGVLCRLIGF
     TRASAGYAHP YFHAAKRRNC DGDEDCVMLL MDALLNFSRS YLPEKRGGKM DAPLVLTTRI
     NPAEVDKEAH NLDLSFIYPL EFYEATLRNA NPKDVEGLID LVSKRLGSEG QYCGFGFTHD
     TDDIAGGPRN SSYKTLETMI DKMKSQLELA KLIRAVDATD VAERVINSHF LPDLMGNLRA
     FSRQSVRCVK CNAKYRRPPL SESCPKCGGR LVLTVHEGSV RKYLEVSMKV AEEYGVSSYT
     RQRLELIQME IESLFRSDKV KQTGLADFV