ID   DP2L_THEVO              Reviewed;        1088 AA.
AC   Q97CR6;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   10-JUN-2026, entry version 104.
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=TV0035; ORFNames=TVG0041370;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Methanobacteriati; Thermoplasmatota; Thermoplasmata;
OC   Thermoplasmatales; Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC         diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC         COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC         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; BA000011; BAB59177.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q97CR6; -.
DR   SMR; Q97CR6; -.
DR   STRING; 273116.gene:9380800; -.
DR   PaxDb; 273116-gene:9380800; -.
DR   KEGG; tvo:TVG0041370; -.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   PhylomeDB; Q97CR6; -.
DR   Proteomes; UP000001017; 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; IPR056172; PolC_DP2_cat_dom.
DR   InterPro; IPR056171; PolC_DP2_central_dom.
DR   InterPro; IPR016033; PolC_DP2_N.
DR   NCBIfam; TIGR00354; polC; 1.
DR   NCBIfam; NF003103; PRK04023.1; 1.
DR   PANTHER; PTHR42210; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR   PANTHER; PTHR42210:SF1; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR   Pfam; PF24846; PolC_DP2_cat; 1.
DR   Pfam; PF24844; PolC_DP2_central; 1.
DR   Pfam; PF03833; PolC_DP2_N; 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..1088
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000152581"
SQ   SEQUENCE   1088 AA;  122362 MW;  62B550A0A9BE7892 CRC64;
     MTILHSTMLS EVLDLESYRK KISDEVRECF DLASQARELG MDVTDKVEIP LASDMAERIE
     ALIGISGIAD QIRDLSKKMS REEVSLEMSR RVANIFKDNK KEALDKAIRV GLAILTEGIL
     VAPLEGIADV YIGKNADGSD YVGISYAGPI RGAGGTAQAL SVLIGDVVRR ELGITRYIPT
     EEEIERYIEE IESYDRIKHL QYLPTPDEIK LVVKNSPVCI DGEGSEEEEV SGHRDMARVK
     TNRIRGGMCL VLCEGLVQKA RKILKYTSSM HLEEWSFLSS ISGKSDDKGS KKSDKFLKDI
     VAGRPVFSHP SRPGGFRLRY GRSRVSGLAA ASLNPATMYI MGKFIAIGSQ IKVELPGKAA
     AVTPCDTIDG PTVLLRNGDH VKINNIEKAK ELYDEVVEIT DAGEILIAYG DFLENNYNLP
     TASFTKEWWM QYLPDGLDGN EVDQFRAVEL SRQYNIPLHP DFDYYWHDIS FEELEYLISA
     VENGRLSDNS FLIPYSASEV LIKLGVQFKR SGNFLVLNQY YPLLVSLGYD VFEDKIKRVK
     PYQRKSSVLE TVNYLSGITI KPRAPTRVGS RLGRPEKAGD RKMKPMVHSL FPVESYGEAR
     RSILNANKKT DGTYKAEVFF YRCTSCGYES PSPTCPKCGS RSKPIGTKNS EIDLSVILRK
     AEDRLGIKLD ELKEFKGVKK LMSKEKVAEP IEKGILRAIH GISVNKDGTC RFDMSDIPIT
     HFRYKEIGIS KEKLSELGYE VKDVNEIFPQ DVIIPRKAAK YLFDVSKFID DLLVRYYGLP
     PFYSLKSEED LVGHLVIGLA PHTSGGVVGR IIGFSDVNAF YAHPFFHAAK RRNCDGDEDS
     VMLLMDGFLN FSARYLPSTT GGLMDAPLVL SVLINPDEID KEALNVDTLQ KYPLIFYEAT
     ERHAAPSELE ETMMTMKVRI KKTATYRNSS YTFDTSDINK GVLVSSYKTL ATMDDKISEQ
     LGLARRIRAV DADDVAARVI STHFLPDMYG NFRRFFSQEF RCTKCNAKYR RIPLSGRCMK
     CGSDSLTLTI HKGSVIKYLD ETLKIEKEYN IPKYLKERID NLARTIKETF PDEEKPDAAI
     KITGLDMY
//