ID   DP2L_THEAC              Reviewed;        1087 AA.
AC   Q9HM33;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=DNA polymerase II large subunit;
DE            Short=Pol II;
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; OrderedLocusNames=Ta0036;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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;
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:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family.
CC       {ECO:0000305}.
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DR   EMBL; AL445063; CAC11185.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HM33; -.
DR   SMR; Q9HM33; -.
DR   STRING; 273075.Ta0036m; -.
DR   EnsemblBacteria; CAC11185; CAC11185; CAC11185.
DR   KEGG; tac:Ta0036; -.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OMA; KRRNCDG; -.
DR   Proteomes; UP000001024; 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; 2.
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..1087
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000152580"
SQ   SEQUENCE   1087 AA;  122284 MW;  9DACD6508846857D CRC64;
     MIMSQKPFDL EGYRKYITEK VREAFNVAQE ARAKGLDVSD HVEIPLASDM AERIEALIGI
     KGIAQEIRDL SSRMSREEVS LEMSRRIAAM FKDNRKEALD KAIRVGLAIL TEGILVAPLE
     GIADVYIGKN QDGSEYVGIS YAGPIRGAGG TAQALSVLIG DVVRRELGIS RFQPTEDEIE
     RYIEEIESYD RIKHLQYMPT PDEIKLVVRN SPICIDGEGS EEEEVSGHRD MERIKTNRIR
     GGMCLVLCEG LVQKARKILK YTSSMHLDDW NFLANLGGKA EGKSSKKSDK FLKDIVAGRP
     VFSHPSRPGG FRLRYGRSRV SGLAAASLNP ATMYIMGKFI AIGSQIKVEL PGKAAAVTPC
     DTIDGPTVLL KNGDHVKIND IEKAREVYDD VVEITDAGEI LIAYGDFLEN NYPLPTPSFT
     VEWWEQYLPD GVNAKDIDQF SAVEISRKYG IPLHPYYDYY WHDISFEDLE FLVKNAEQWS
     ITEDGMRVPY PAFDVFIRLG IEFRRSGDYL IIRDYYPLLI SLGYDVRNGK IVNVKKYERK
     GSVMETVNYL SGLIIKPRAP TRVGSRLGRP EKAGDRKMKP MVHSLFPVES YGEARRSIIG
     ANKNSEGSYK AEVFFYRCNS CGFETPTPVC PRCGGHCSPL GEKTGSIDLE SILNRAESIL
     GISLDSLKEF KGVKKLMSKE KVAEPIEKGI LRAVHDISVN KDGTCRFDMS DIPITHFRYR
     EIGIDERTLA DLGYEVRDVN ELFPQDVIIP RKAAKYLFNV SRFIDDLLVK YYNMPPFYSL
     ESEEDLIGHL IIGLAPHTSG GVVGRIIGFS DVNAFYAHPF FHAAKRRNCD GDEDSVMLLM
     DGFLNFSARY LPSTRGGLMD APLVLSVLIN PDEIDKEALN VDTLSRYPVL FYEAAERHAS
     PAEIEDTMMT MKVRIKKTGT YMGSSYTMDT SDINSGVLVS SYKTLGTMDE KINEQLGLAK
     KLRAVDADDV AARVISTHFL PDMYGNFRKF FSQEFRCTKC NAKYRRIPLS GRCQKCGSTS
     LTLTIHKGSV VKYLNETLKI AENYRLPDYL KARIDNLART IKETFPDTEE EEKPEPREVK
     ITGLDMY