ID   DP2L_ARCFU              Reviewed;        1143 AA.
AC   O28552;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=AF_1722;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB89529.1; -; Genomic_DNA.
DR   PIR; A69465; A69465.
DR   AlphaFoldDB; O28552; -.
DR   SMR; O28552; -.
DR   STRING; 224325.AF_1722; -.
DR   EnsemblBacteria; AAB89529; AAB89529; AF_1722.
DR   KEGG; afu:AF_1722; -.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OMA; KRRNCDG; -.
DR   PhylomeDB; O28552; -.
DR   Proteomes; UP000002199; 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..1143
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000152573"
SQ   SEQUENCE   1143 AA;  129368 MW;  7D874532600D851F CRC64;
     MDATLDRFFP LFESESNEDF WRIEEIRRYH ESLMVELDRI YRIAEAARKK GLDPELSVEI
     PIAKNMAERV EKLMNLQGLA KRIMELEEGG LSRELICFKV ADEIVEGKFG EMPKEEAIDK
     AVRTAVAIMT EGVVAAPIEG IARVRIDREN FLRVYYAGPI RSAGGTAQVI SVLVADYVRR
     KAEIGRYVPT EEEILRYCEE IPLYKKVANL QYLPSDEEIR LIVSNCPICI DGEPTESAEV
     SGYRNLPRVE TNRVRGGMAL VIAEGIALKA PKLKKMVDEV GIEGWEWLDA LIKGGGDSGS
     EEEKAVIKPK DKYLSDIVAG RPVLSHPSRK GGFRLRYGRA RNSGFATVGV NPATMYLLEF
     VAVGTQLKVE RPGKAGGVVP VSTIEGPTVR LKNGDVVKIN TLSEAKALKG EVAAILDLGE
     ILINYGDFLE NNHPLIPASY TYEWWIQEAE KAGLRGDYRK ISEEEALKLC DEFHVPLHPD
     YTYLWHDISV EDYRYLRNFV SDNGKIEGKH GKSVLLLPYD SRVKEILEAL LLEHKVRESF
     IVIETWRAFI RCLGLDEKLS KVSEVSGKDV LEIVNGISGI KVRPKALSRI GARMGRPEKA
     KERKMSPPPH ILFPVGMAGG NTRDIKNAIN YTKSYNAKKG EIEVEIAIRK CPQCGKETFW
     LKCDVCGELT EQLYYCPSCR MKNTSSVCES CGRECEGYMK RKVDLRELYE EAIANLGEYD
     SFDTIKGVKG MTSKTKIPER LEKGILRVKH GVFVFKDGTA RFDATDLPIT HFKPAEIGVS
     VEKLRELGYE RDYKGAELKN ENQIVELKPQ DVILPKSGAE YLLRVANFID DLLVKFYKME
     PFYNAKSVED LIGHLVIGLA PHTSAGVLGR IIGFSDVLAG YAHPYFHAAK RRNCDGDEDC
     FMLLLDGLLN FSRKFLPDKR GGQMDAPLVL TAIVDPREVD KEVHNMDIVE RYPLEFYEAT
     MRFASPKEME DYVEKVKDRL KDESRFCGLF FTHDTENIAA GVKESAYKSL KTMQDKVYRQ
     MELARMIVAV DEHDVAERVI NVHFLPDIIG NLRAFSRQEF RCTRCNTKYR RIPLVGKCLK
     CGNKLTLTVH SSSIMKYLEL SKFLCENFNV SSYTKQRLML LEQEIKSMFE NGTEKQVSIS
     DFV