ID   DP2L_CENSY              Reviewed;        1112 AA.
AC   A0RYM0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   20-JAN-2009, entry version 11.
DE   RecName: Full=DNA polymerase II large subunit;
DE            Short=Pol II;
DE            EC=2.7.7.7;
GN   Name=polC; OrderedLocusNames=CENSYa_1827;
OS   Cenarchaeum symbiosum.
OC   Archaea; Crenarchaeota; Thermoprotei; Cenarchaeales; Cenarchaeaceae;
OC   Cenarchaeum.
OX   NCBI_TaxID=46770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
CC   -!- FUNCTION: Possesses two activities: a DNA synthesis (polymerase)
CC       and an exonucleolytic activity that degrades single stranded DNA
CC       in the 3'- to 5'-direction. Has a template-primer preference which
CC       is characteristic of a replicative DNA polymerase (By similarity).
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1).
CC   -!- CATALYTIC ACTIVITY: Degradation of single-stranded DNA. It acts
CC       progressively in a 3'- to 5'-direction, releasing nucleoside 5'-
CC       phosphates.
CC   -!- SUBUNIT: Heterodimer of a large subunit and a small subunit (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family.
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DR   EMBL; DP000238; ABK78437.1; -; Genomic_DNA.
DR   GenomeReviews; DP000238_GR; CENSYa_1827.
DR   BRENDA; 2.7.7.7; 281607.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:HAMAP.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:HAMAP.
DR   GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IEA:HAMAP.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:HAMAP.
DR   HAMAP; MF_00324; -; 1.
DR   InterPro; IPR004475; PolC_DP2.
DR   InterPro; IPR016033; PolC_DP2_N.
DR   Pfam; PF03833; PolC_DP2; 1.
DR   TIGRFAMs; TIGR00354; polC; 1.
PE   3: Inferred from homology;
KW   Complete proteome; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Exonuclease; Hydrolase;
KW   Multifunctional enzyme; Nuclease; Nucleotidyltransferase; Transferase.
FT   CHAIN         1   1112       DNA polymerase II large subunit.
FT                                /FTId=PRO_0000294676.
SQ   SEQUENCE   1112 AA;  121039 MW;  BA05392302C4ECF4 CRC64;
     MSGGDVEEYL RGADMPEEYR RYYSSLSGGT YDIFEKAASA KSNLADSSGM VEPKIAVDLS
     DRVAKMHDLD IAGPLRELLA TKGKELAALM LAKEIMDGKY LPEADIEKRI DSAVRVGLAV
     VTEGVTIAPL QGIADVITKK NKDGSEYLSV SIAGPMRSAG GTESAVTMLI ADYVRRQAGL
     AEYQADSLDD ETGRFIEELR IYEREVGSFQ FHVLDEDIRA VISHLPVELD GVDTDPYEVV
     NHKGMSRIQT DRVRGGALRV LNDGLIGRSK KLLKRIELYG LDGWEWLAEL KGAVQTGENK
     EDAAAKRMRE VITGRSVLSM PNRLGGFRLR YGRACNTGYT SVGFHPAVAE ILDHTIAVGT
     QVKIDIPGKG ATVAFVDTIE APTVRLAGGD VVKIRDVAHG IELKGSIERI LHLGDMLISF
     GDFLENNAQL VPSGYVEEIW KMDMEAAGAA QGSPSSADEA VRISRELGVP LHPRYLYYWD
     QISHEELAML LSPLDKGDAI SYPAACKPVL EKLGVPHKAG PEGPVLEGDE ARIFRELILD
     NPPGPDASAP VPELISRSSG ITIRDKFSTS IGVRIGRPEK AAPRQMRPPT HCLFPVGGTG
     GPTNNLLKSA ARPGFSADIL SRRCPGCGEP SISIRCWACG ERTAVERTCM QCGTDVDGEE
     CERCGRPGLA HSRVEFPLKK MLVSAQEKTG VRAHDPLKGV KELAHQDRIA EPLEKGLIRQ
     SRSLTVFKDG TVRFDATNSP MTHFKPSWIG TSAEKLRELG YETDVDGKKL EGPDQLVELR
     MQDIVIPLEG AKYLVSACGY IDAELDKLYG APPFYKVPDL GGLIGHLVVG LAPHTSVGVA
     ARIIGYTETH VCFGTPNWHS AKRRDADGDA DSIILLMDAL LNFSRHYLSD RIGGLMDAPL
     LIQPLVLPHE SQSQAHNIEV VKRLPPGFYE AAAARKKASE VGCVEIVKSR LETAGQFGGY
     HFTHGTSSLT TSRPRSAYST LGSMLDKLDL QIRNANLIAA VDAAEIISNV ISTHLVPDIM
     GNLRAYARQN FRCTACGKSY RRIPLAQRCS CGNGLIQTIT RASVEKYLKL AKRLVNEYDV
     GAYQRGRIHA LSDEIELVFG KGGGDQALLT DF
//