DP2L_NATPD
ID DP2L_NATPD Reviewed; 1198 AA.
AC Q3IU54;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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}; Synonyms=polA2;
GN OrderedLocusNames=NP_0476A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI48329.1; -; Genomic_DNA.
DR RefSeq; WP_011321965.1; NC_007426.1.
DR AlphaFoldDB; Q3IU54; -.
DR SMR; Q3IU54; -.
DR STRING; 348780.NP_0476A; -.
DR EnsemblBacteria; CAI48329; CAI48329; NP_0476A.
DR GeneID; 3703041; -.
DR KEGG; nph:NP_0476A; -.
DR eggNOG; arCOG04447; Archaea.
DR HOGENOM; CLU_001154_0_0_2; -.
DR OMA; KRRNCDG; -.
DR OrthoDB; 559at2157; -.
DR Proteomes; UP000002698; 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..1198
FT /note="DNA polymerase II large subunit"
FT /id="PRO_0000294698"
FT REGION 281..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..316
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 132156 MW; 0F886B4A2B484FFA CRC64;
MREDDEQYFR RLESDLDTAL SVAREARKRG GDPTEDIEIP IAKDMADRVE NILGIDGVAE
RVREMEADPD LSREEAALEL AADFANDEVG DYETRAGKVE GAVRTAVALL TEGVVAAPIE
GIDRVELLEN DDGTEFINIY YAGPIRSAGG TAQALSVLVA DYTRTLIGID EYKARNDETE
RYAEELSLYD DETGLQYAPK DEETKFIAEH MPIMLDGEAT GDEEVSGFRD LERVDTNSAR
GGMCLVLGEG IAQKAPKIQR YTSQLDEVDW PWLQDLIDGT YKTGEDTDEA DADSDDGTDE
DAADDSDIDD SSAGDEEADA PSGPPRPDPQ KKFLRDLIAG RPVFGHPSEP GGFRLRYGRA
RNHGFATAGV HPAAMHLIDD FLATGTQIKT ERPGKAAGVV PVDTIEGPTV KLANGDVRRV
DDPEEALEIR NGVEAILDLG EYLVNYGEFV ENNHPLSPAA YAPEWWTQDL AAAGADVQAL
ADSPRVDLEH PSAEQALEWA ERYDAPLHPE YTYLWHDLDV ERFEALAAAA SEGHWAETDG
AQQTRPPDGA AESTLVVPRS EPVREALEVL LVEHTQGEET LTVPDAEPLV RSLGLTEGLE
RTWDELSTAA RSYDDGDNAV RAVNEVAPFE VRERAPTRIG CRMGRPEKSE KRDLSPAVHT
LFPIGEAGGS QRDIAEAATH AESMQDTPGE VEVQVGRRQC PACDTETFRA RCPDCESVTD
PRYVCYDCNI DVDPDESGRA ICPNCEREAD AVQNRTVNVH EEYRSALSNV GERENAFDVL
KGVKGLSSEH KVPEPIEKGV LRAKHGVSAF KDGTVRYDMT DLPVTSVRAA ELDVTADQLR
SLGYETDIHG EPLTHEDQLV ELRVQDVVLS NGAAEHMLRT ADFVDDLLEQ YYGLEPFYDA
EDRDDIVGEL VFGMAPHTSA AVVGRVIGFT SAAVGYAHPY FHAAKRRNCD GDEDCVMLLL
DGLLNFSKTF LPDQRGGRMD APLVMSSRID PAEIDDEAHN MDIVSSYPRA FFEATREMAD
PGEVESLIQL GEDTLGTADE YRGFEHTHDT VDLAAGPDLS AYKTLGDMME KMDAQLELSR
KLRSVDETDV AERVIEYHFL PDIIGNLRAF SRQETRCLDC GEKYRRVPLT GDCRECGGRV
NLTVHQGSVN KYIDTAIQVA EEYGCREYTK QRLRILDRAV ESIFEDDTNK QSGIADFM
