ID A0A2H9NW83_9ARCH Unreviewed; 457 AA.
AC A0A2H9NW83;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=DNA polymerase II large subunit {ECO:0000256|ARBA:ARBA00026137};
DE Flags: Fragment;
GN ORFNames=COY95_01170 {ECO:0000313|EMBL:PIY60556.1};
OS Candidatus Woesearchaeota archaeon CG_4_10_14_0_8_um_filter_47_5.
OC Archaea; Candidatus Woesearchaeota.
OX NCBI_TaxID=1974451 {ECO:0000313|EMBL:PIY60556.1, ECO:0000313|Proteomes:UP000229955};
RN [1] {ECO:0000313|Proteomes:UP000229955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.K.,
RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT "Depth-based differentiation of microbial function through sediment-hosted
RT aquifers and enrichment of novel symbionts in the deep terrestrial
RT subsurface.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025068}.
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 Evidence={ECO:0000256|ARBA:ARBA00024632};
CC -!- SUBUNIT: Heterodimer of a large subunit and a small subunit.
CC {ECO:0000256|ARBA:ARBA00011315}.
CC -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family.
CC {ECO:0000256|ARBA:ARBA00011053}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIY60556.1}.
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DR EMBL; PFLA01000094; PIY60556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9NW83; -.
DR Proteomes; UP000229955; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR004475; PolC_DP2.
DR InterPro; IPR016033; PolC_DP2_N.
DR PANTHER; PTHR42210; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR PANTHER; PTHR42210:SF1; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR Pfam; PF03833; PolC_DP2; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..454
FT /note="DNA polymerase II large subunit DP2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03833"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PIY60556.1"
FT NON_TER 457
FT /evidence="ECO:0000313|EMBL:PIY60556.1"
SQ SEQUENCE 457 AA; 50926 MW; 3F3C78DA447E4B83 CRC64;
ELDEKLRKAY DCAATARKKG IDPELRVDIP LAKNMAERVE GLLSIIAPGL VGSGMTGRIM
ELEKKYGILD WRVALVLAEE VALEKFCTFK DKKEAMEVGI RAGFAYQTVG IVAAPLEGFI
GLVIKKRKDG NEYFSLKYSG PIRGAGGTAA AFSLVIADYV RTKMGYSPFD PTEEEIERYV
TEIEDYHERV TNLQYFPSKD EIRFLVKHLP VEVNGDPTET REVSNYKDLP RVETNAIRGG
VCLVLAEGLA QKAPKINKRL SVWGPSFGLG WEFLKGFLLL QKKIKAQTTR QENQASKIMP
NYTYIADLVA GRPVLTHPLR AGGFRLRYGR SRTSGFSSCS LHPATQVLLR NYIAVATQLK
VERPGKAAAV TICDTLDGPI VLLNDGSVVK VSSRSQAKLI KDQVKKILFL GDILFNYGDF
SENNHSLVPA GYCEEWWVQE LEQALKKKKD KKNKKTA
//
