DP2L_CENSY
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 03-AUG-2022, entry version 54.
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=CENSYa_1827;
OS Cenarchaeum symbiosum (strain A).
OC Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX NCBI_TaxID=414004;
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) 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; DP000238; ABK78437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0RYM0; -.
DR SMR; A0RYM0; -.
DR STRING; 414004.CENSYa_1827; -.
DR PRIDE; A0RYM0; -.
DR EnsemblBacteria; ABK78437; ABK78437; CENSYa_1827.
DR KEGG; csy:CENSYa_1827; -.
DR PATRIC; fig|414004.10.peg.1669; -.
DR HOGENOM; CLU_001154_0_0_2; -.
DR OMA; KRRNCDG; -.
DR Proteomes; UP000000758; 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..1112
FT /note="DNA polymerase II large subunit"
FT /id="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