DP2L_PYRFU
ID DP2L_PYRFU Reviewed; 1263 AA.
AC P81409;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=DP2;
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=PF0019;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=9348040; DOI=10.1046/j.1365-2443.1997.1380336.x;
RA Uemori T., Sato Y., Kato I., Doi H., Ishino Y.;
RT "A novel DNA polymerase in the hyperthermophilic archaeon, Pyrococcus
RT furiosus: gene cloning, expression, and characterization.";
RL Genes Cells 2:499-512(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP CHARACTERIZATION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=8787781; DOI=10.1248/bpb.18.1647;
RA Imamura M., Uemori T., Kato I., Doi H., Ishino Y.;
RT "A non-alpha-like DNA polymerase from the hyperthermophilic archaeon
RT Pyrococcus furiosus.";
RL Biol. Pharm. Bull. 18:1647-1652(1995).
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; D84670; BAA25164.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL80143.1; -; Genomic_DNA.
DR PIR; T43934; T43934.
DR RefSeq; WP_014835497.1; NZ_CP023154.1.
DR AlphaFoldDB; P81409; -.
DR SMR; P81409; -.
DR STRING; 186497.PF0019; -.
DR PRIDE; P81409; -.
DR EnsemblBacteria; AAL80143; AAL80143; PF0019.
DR GeneID; 41711805; -.
DR KEGG; pfu:PF0019; -.
DR PATRIC; fig|186497.12.peg.21; -.
DR eggNOG; arCOG04447; Archaea.
DR HOGENOM; CLU_001154_0_0_2; -.
DR OMA; KRRNCDG; -.
DR OrthoDB; 559at2157; -.
DR PhylomeDB; P81409; -.
DR BRENDA; 2.7.7.7; 5243.
DR Proteomes; UP000001013; 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 Direct protein sequencing; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Exonuclease; Hydrolase;
KW Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..1263
FT /note="DNA polymerase II large subunit"
FT /id="PRO_0000152579"
FT REGION 1224..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1030
FT /note="G -> R (in Ref. 1; BAA25164)"
FT /evidence="ECO:0000305"
FT CONFLICT 1034
FT /note="R -> G (in Ref. 1; BAA25164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1263 AA; 143169 MW; 3BFFB2CC8D054F4C CRC64;
MELPKEIEEY FEMLQREIDK AYEIAKKARS QGKDPSTDVE IPQATDMAGR VESLVGPPGV
AQRIRELLKE YDKEIVALKI VDEIIEGKFG DFGSKEKYAE QAVRTALAIL TEGIVSAPLE
GIADVKIKRN TWADNSEYLA LYYAGPIRSS GGTAQALSVL VGDYVRRKLG LDRFKPSGKH
IERMVEEVDL YHRAVSRLQY HPSPDEVRLA MRNIPIEITG EATDDVEVSH RDVEGVETNQ
LRGGAILVLA EGVLQKAKKL VKYIDKMGID GWEWLKEFVE AKEKGEEIEE SESKAEESKV
ETRVEVEKGF YYKLYEKFRA EIAPSEKYAK EIIGGRPLFA GPSENGGFRL RYGRSRVSGF
ATWSINPATM VLVDEFLAIG TQMKTERPGK GAVVTPATTA EGPIVKLKDG SVVRVDDYNL
ALKIRDEVEE ILYLGDAIIA FGDFVENNQT LLPANYVEEW WIQEFVKAVN EAYEVELRPF
EENPRESVEE AAEYLEVDPE FLAKMLYDPL RVKPPVELAI HFSEILEIPL HPYYTLYWNT
VNPKDVERLW GVLKDKATIE WGTFRGIKFA KKIEISLDDL GSLKRTLELL GLPHTVREGI
VVVDYPWSAA LLTPLGNLEW EFKAKPFYTV IDIINENNQI KLRDRGISWI GARMGRPEKA
KERKMKPPVQ VLFPIGLAGG SSRDIKKAAE EGKIAEVEIA FFKCPKCGHV GPETLCPECG
IRKELIWTCP KCGAEYTNSQ AEGYSYSCPK CNVKLKPFTK RKIKPSELLN RAMENVKVYG
VDKLKGVMGM TSGWKIAEPL EKGLLRAKNE VYVFKDGTIR FDATDAPITH FRPREIGVSV
EKLRELGYTH DFEGKPLVSE DQIVELKPQD VILSKEAGKY LLRVARFVDD LLEKFYGLPR
FYNAEKMEDL IGHLVIGLAP HTSAGIVGRI IGFVDALVGY AHPYFHAAKR RNCDGDEDSV
MLLLDALLNF SRYYLPEKRG GKMDAPLVIT TRLDPREVDS EVHNMDVVRY YPLEFYEATY
ELKSPKELVG VIERVEDRLG KPEMYYGIKF THDTDDIALG PKMSLYKQLG DMEEKVKRQL
TLAERIRAVD QHYVAETILN SHLIPDLRGN LRSFTRQEFR CVKCNTKYRR PPLDGKCPVC
GGKIVLTVSK GAIEKYLGTA KMLVANYNVK PYTRQRICLT EKDIDSLFEY LFPEAQLTLI
VDPNDICMKM IKERTGETVQ GGLLENFNSS GNNGKKIEKK EKKAKEKPKK KKVISLDDFF
SKR
