ID   DP2L_NANEQ              Reviewed;        1243 AA.
AC   Q74N29;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=NEQ420;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
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; AE017199; AAR39264.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q74N29; -.
DR   SMR; Q74N29; -.
DR   STRING; 228908.NEQ420; -.
DR   PRIDE; Q74N29; -.
DR   EnsemblBacteria; AAR39264; AAR39264; NEQ420.
DR   KEGG; neq:NEQ420; -.
DR   PATRIC; fig|228908.8.peg.428; -.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OMA; KRRNCDG; -.
DR   Proteomes; UP000000578; 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..1243
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000294697"
SQ   SEQUENCE   1243 AA;  142593 MW;  A48088166C1CF516 CRC64;
     MVYYDILAKE LEKLYEIAEK ARAQGYDPKD IVEIPLANNM GERVAHLISA IHEQLDVKKT
     AELILELEKQ YGFLDWRVGL KLIDYALEGK LIPYDDILKR IDLGVRLALG YITMGVVSAP
     LEGLVELRIK KRKDGKPYLA LYYAGPIRGA GGTAAAVSVL FADYARKKAG LYEYDPTKEE
     IERYKIEIDS YHNKVARLQY KPSDEEIEFL VKHIPVEING DPTSDKEVPS YKNLERVETN
     RIRGGMCLVI AEGIAQKAKK IYGKITEWGK EFGLEHWEFL GEYLKLQKEI QAKLAAESGG
     EIEGKEIKRK ITLFLDEIKK EEITVKYPTP AGKYLQEITA GRPIFSLPMA IGGFRLRYGR
     SFATGFATSG IHPATMFLTY GFLAIGTQMR GERPKKSTIV TPVTSLHPPI VKLKDGTVKK
     VHSVVEAIKI ANDVEEILFL GDILTAFGDW LNEKANLVPS PYVEEWWIQE FDRAAMKKTD
     YKIEFDVMKP RKLFKIEGLE NLSQYLGIPK DRLEEIIRKP FSRKPTIDEA ITISEKLGIP
     LHPEYTPFWV HITKEELIKL IEELRKAKIQ NNKIYFHESQ KELKAILEKL FIEHFREGEY
     FYINESMTKS LLYQLDNLNL EKAKKEFDNA IDALDLVNRL SPIEIRDVAG VYVGFRAGRP
     EKAKMREMTG RPHGLFPVGE EGGKMRNVIE AYNKGYVKAE FALYYCNHCK RYTIYRKCEV
     CGNKTKEVYV CKEIINRLKT SLFKQYKDWK KVEEEIASHL WAEAVTHSKN NCREPKRYSL
     IKLNIKHYVD RAVQKLKLFN IPKLVKGVRG TSNKDHIVER LEKAFLRSVS DVYVNKDGTI
     RYDGTQIPLT HFRPKDLIGV TIEKLKELGY THDIYGNPLE REDQILQLKP QDIILPYGIL
     VKSRLNKNKI VRTDAAEAFK KVANFVDEEL KRLYNLEPYY NIEKAEDLIG KIVFGIAPHT
     SAAVVGRIIG FTPIQGIIAH PIWHAGQRRN CDGDETAVML GLDALINFSR EYLPDKRGAR
     TMDAPLVLTL KLELKAVDDE VHDMDIVYNY PLEFYYETLK GSPAKDVKKQ CGILTLGDFL
     KEEDISKIPI GFTHPTKSIR LGNKVSLYKR LKTMQQKTEW QLKLAERIRA VDENIVAEIV
     IEKHFMPDIK GNLRGFSSQV FRCTKCDTTY DRVPLSGKCP KCGGNIVFTV HEGTIKKYLP
     TSLYLARKYK IKKFTKQSLF LLDRRIKQIF GGEKKSLADF INS