ID   DP2L_METJA              Reviewed;        1139 AA.
AC   Q59024;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=MJ1630;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=9555910; DOI=10.1128/jb.180.8.2232-2236.1998;
RA   Ishino Y., Komori K., Cann I.K.O., Koga Y.;
RT   "A novel DNA polymerase family found in Archaea.";
RL   J. Bacteriol. 180:2232-2236(1998).
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.
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   -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family.
CC       {ECO:0000305}.
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DR   EMBL; L77117; AAB99651.1; -; Genomic_DNA.
DR   PIR; D64503; D64503.
DR   AlphaFoldDB; Q59024; -.
DR   SMR; Q59024; -.
DR   STRING; 243232.MJ_1630; -.
DR   PRIDE; Q59024; -.
DR   EnsemblBacteria; AAB99651; AAB99651; MJ_1630.
DR   KEGG; mja:MJ_1630; -.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   InParanoid; Q59024; -.
DR   OMA; KRRNCDG; -.
DR   PhylomeDB; Q59024; -.
DR   Proteomes; UP000000805; 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   1: Evidence at protein level;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW   Hydrolase; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1139
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000152575"
SQ   SEQUENCE   1139 AA;  129402 MW;  3B7968A013AAC45A CRC64;
     MIVMVHVACS ENMKKYFENI VDEVKKIYRI AEECRKKGFD PTDEVEIPLA ADMADRVEGL
     VGPKGVAERI RELVKELGKE PAALEIAKEI VEGKFGNFDK EKKAEQAVRT ALAVLTEGIV
     AAPLEGIADV KIKKNPDGTE YLAIYYAGPI RSAGGTAQAL SVLVGDFVRK AMGLDRYKPT
     EDEIERYVEE VELYQSEVGS FQYNPTADEI RTAIRNIPIE ITGEATDDVE VSGHRDLPRV
     ETNQLRGGAL LVLVEGVLLK APKILRHVDK LGIEGWDWLK DLMSKKEEKE EEKDEKVDDE
     EIDEEEEEIS GYWRDVKIEA NKKFISEVIA GRPVFAHPSK VGGFRLRYGR SRNTGFATQG
     FHPALMYLVD EFMAVGTQLK TERPGKATCV VPVDSIEPPI VKLKNGDVIR VDTIEKAMDV
     RNRVEEILFL GDVLVNYGDF LENNHPLLPS CWCEEWYEKI LIANNIEYDK DFIKNPKPEE
     AVKFALETKT PLHPRFTYHW HDVSKEDIIL LRNWLLKGKE DSLEGKKVWI VDLEIEEDKK
     AKRILELIGC CHLVRNKKVI IEEYYPLLYS LGFDVENKKD LVENIEKILE SAKNSMHLIN
     LLAPFEVRRN TYVYVGARMG RPEKAAPRKM KPPVNGLFPI GNAGGQVRLI NKAVEENNTD
     DVDVSYTRCP NCGKISLYRV CPFCGTKVEL DNFGRIKAPL KDYWYAALKR LGINKPGDVK
     CIKGMTSKQK IVEPLEKAIL RAINEVYVFK DGTTRFDCTD VPVTHFKPNE INVTVEKLRE
     LGYDKDIYGN ELVDGEQVVE LKPQDVIIPE SCAEYFVKVA NFIDDLLEKF YKVERFYNVK
     KKEDLIGHLV IGMAPHTSAG MVGRIIGYTK ANVGYAHPYF HAAKRRNCDG DEDSFFLLLD
     AFLNFSKKFL PDKRGGQMDA PLVLTTILDP KEVDGEVHNM DTMWSYPLEF YEKTLEMPSP
     KEVKEFMETV EDRLGKPEQY EGIGYTHETS RIDLGPKVCA YKTLGSMLEK TTSQLSVAKK
     IRATDERDVA EKVIQSHFIP DLIGNLRAFS RQAVRCKCGA KYRRIPLKGK CPKCGSNLIL
     TVSKGAVEKY MDVAEKMAEE YNVNDYIKQR LKIIKEGINS IFENEKSRQV KLSDFFKIG