ID I3D4V0_9ARCH Unreviewed; 1125 AA.
AC I3D4V0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=DNA polymerase II large subunit {ECO:0000256|HAMAP-Rule:MF_00324};
DE Short=Pol II {ECO:0000256|HAMAP-Rule:MF_00324};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_00324};
DE AltName: Full=Exodeoxyribonuclease large subunit {ECO:0000256|HAMAP-Rule:MF_00324};
DE EC=3.1.11.1 {ECO:0000256|HAMAP-Rule:MF_00324};
GN Name=polC {ECO:0000256|HAMAP-Rule:MF_00324,
GN ECO:0000313|EMBL:EIJ66743.1};
GN ORFNames=BD31_I0293 {ECO:0000313|EMBL:EIJ66743.1};
OS Candidatus Nitrosopumilus salaria BD31.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=859350 {ECO:0000313|EMBL:EIJ66743.1, ECO:0000313|Proteomes:UP000003423};
RN [1] {ECO:0000313|EMBL:EIJ66743.1, ECO:0000313|Proteomes:UP000003423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD31 {ECO:0000313|EMBL:EIJ66743.1,
RC ECO:0000313|Proteomes:UP000003423};
RX PubMed=22461555; DOI=10.1128/JB.00013-12;
RA Mosier A.C., Allen E.E., Kim M., Ferriera S., Francis C.A.;
RT "Genome sequence of "Candidatus Nitrosopumilus salaria" BD31, an ammonia-
RT oxidizing archaeon from the San Francisco Bay estuary.";
RL J. Bacteriol. 194:2121-2122(2012).
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 ECO:0000256|HAMAP-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:0000256|HAMAP-
CC Rule:MF_00324};
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, ECO:0000256|HAMAP-
CC Rule:MF_00324};
CC -!- SUBUNIT: Heterodimer of a large subunit and a small subunit.
CC {ECO:0000256|ARBA:ARBA00011315, ECO:0000256|HAMAP-Rule:MF_00324}.
CC -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family.
CC {ECO:0000256|ARBA:ARBA00011053, ECO:0000256|HAMAP-Rule:MF_00324}.
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:EIJ66743.1}.
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DR EMBL; AEXL02000023; EIJ66743.1; -; Genomic_DNA.
DR AlphaFoldDB; I3D4V0; -.
DR PATRIC; fig|859350.6.peg.244; -.
DR OrthoDB; 7529at2157; -.
DR Proteomes; UP000003423; Unassembled WGS sequence.
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:0008310; F:single-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0006308; P:DNA catabolic process; 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 NCBIfam; TIGR00354; polC; 1.
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.
DR PIRSF; PIRSF016275; PolC_DP2; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00324};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00324};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_00324};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00324};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00324};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_00324};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00324};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00324};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00324}.
FT DOMAIN 21..876
FT /note="DNA polymerase II large subunit DP2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03833"
SQ SEQUENCE 1125 AA; 126402 MW; 2A1F710264EBE12E CRC64;
MSENDAISRI SGIKMPEYYL EYYSNLSTDT YSIFEHAAKA KSSLVDSSGI IEPKIAFDLA
DRVAKMHEID IAEPLREILK INGKELSALI LSKEIAMGKY SLPDASLEEK LDLAVRVGLA
IVTEGVTIAP LQGIDKVKIK KNKDGTEYLS VSIAGPMRSA GGTESAVTML IADHVRKIAG
LGKFQANSFD DETGRFVEEL RIYEREASSF QFHILDEDIE HVISNLPVEL DGVDTDPYEV
VNHKGMTRIK TDRVRGGALR VLNDGLIGRS KKLLKRIELY NLDGWEWLND LKGAVQTGEN
QEDAAAKRMR EVITGRSVLS MPNKLGGFRL RYGRACNTGF AAVGIHPVIA EILDHTVAVG
TQIKIDIPGK GATIAFVDSI DTPTVRLKNG NVVKIRDVKH GLEIKNEIEK ILHLGDILIS
FGDFLENNAQ LVPSAYVEEF WIEELKQKIQ KYEPNDQFLN QFLARLPTLD EALKISLDFK
IPLHPHYLYY WDCISSDELV KLLEPNKVTT TSIEYPIEIK KILENLGTPH KVENDVIILE
NQEAKIFFNL LFRQKPTISD LSVPKILTQA SGIQINNKFS TSVGVRIGRP EKAAARQMKP
PTHVLFPISD KGGPTRDLLK ASRNEHFFAD IFNRQCNQCN QPSIGIKCSI CGTKTTITYR
CTNCRDELTE PFCQKCKRKA PTHSHKEFPL KTRLLLAQEK MGLRAKEPFK GVKELINQDR
IAEPLEKGLT RQNFGLTTFK DGTVRFDATN SPITHFKPSW IGTSIEKLKE LGYFHDIDGK
PLEHTDQIIE IRMQDVIIPY ESGNYLVSTC KYIDVLLQKF YGHSPFYNVQ NSKDLIGHLI
IGLAPHTSVG IVGRIIGYTE THVCFATPNW HSAKRRDADG DADSIMLLMD SLLNFSRQFL
SDRIGGLMDA PLLVQPLVLP HESQPQAHNL EVTKSLPLEF FESTLTQIKA SDISSVEIIK
TRLETERQFY DYFFTHSTSS LTTSKSRSAY STLGSMLDKF DMQVKNAELI NAVDTSEIVS
NVISTHLVPD IMGNLRAYAR QNFRCTGCGK SFRRMPLIQT CLCGHKLIPT ITRGSVEKYL
KLAKRLVEKY DVGEYQKGRI HALSDEIELV FGKSKGDQSL LTDYD
//
