ID A0A1D3KZI4_9EURY Unreviewed; 1105 AA.
AC A0A1D3KZI4;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:SCG84693.1};
GN ORFNames=MCBB_0105 {ECO:0000313|EMBL:SCG84693.1};
OS Methanobacterium congolense.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=118062 {ECO:0000313|EMBL:SCG84693.1, ECO:0000313|Proteomes:UP000094707};
RN [1] {ECO:0000313|EMBL:SCG84693.1, ECO:0000313|Proteomes:UP000094707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Buetzberg {ECO:0000313|EMBL:SCG84693.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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 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}.
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DR EMBL; LT607756; SCG84693.1; -; Genomic_DNA.
DR RefSeq; WP_071905773.1; NZ_LT607756.1.
DR AlphaFoldDB; A0A1D3KZI4; -.
DR STRING; 118062.MCBB_0105; -.
DR GeneID; 30410970; -.
DR KEGG; mcub:MCBB_0105; -.
DR PATRIC; fig|129848.4.peg.111; -.
DR OrthoDB; 7529at2157; -.
DR Proteomes; UP000094707; Chromosome I.
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}; Reference proteome {ECO:0000313|Proteomes:UP000094707};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00324}.
FT DOMAIN 3..856
FT /note="DNA polymerase II large subunit DP2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03833"
FT REGION 588..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1105 AA; 123188 MW; 6CABA52F808043A9 CRC64;
MGYFENLEEE TRKLYDIAKE ARLKGHDIEL EPEIPLAKDL AERVEGLVGP VGVAKRIKEL
EKDVSREEVA FQIAREIVTT PDEEGVEDSI EVKEQKSDQA TRTALAILTE GVVAAPLEGI
SQIRIKKNFD DGNYLAVYFA GPIRSAGGTA AALAVLIGDY IRISLGLDVF KPTDIEVERY
VEEVELYESE VTNLQYSPKP EETRLAIKNI PVEVTGEPTD KIEVSNRDLE RVETNNIRGG
ALLAMAEGVI QKAPKVMKYA SKLNIDGWNW LEKFSKAPDS KSDDGDSGKV DDKYMRDIIG
GRPVLSYPKA KGGFRLRYGR SRNTGLAAMG VHPSTMEIVE FLAVGTQMKI ERPGKGNCVV
PCDTIEGPIV KLKNGSVVKV ESEAQARKIK NQVEEILFIG DMLIAFGEFL RNNHVLLPAG
WCEEWWVQTI EKSPAYSEDE ALQEGVDLKT LETEKITAER AFELSKRYNV PLHPSYTYFY
HDATKEDLNE LIEWMKSGST VDLTTDNGLV KKSFSLEMDP GKRILEILGV PHLVEEGKIL
VDHEDAYALL HTLREPLDLS EDTKTLEAVN KVSEVEIMAK APTYIGGRVG RPEKSKERMM
KPAPHSLFPI GTNGGSRRNI IDAAKKGSIN VDIGRCKCTE CGINSIQAIC PVCGARTVPA
GSGRKNVNLS NLLKKAFENV GIRKMDEVKG VQGMISEEKF PEPLEKGILR AKNGVYTFKD
ATIRHDSTDL PLTHFIPSEV GVTHEKLLEM GYTHDAYGAA LENDEQVVEL KIQDVVISDN
CAEYLIRVSH FIDDLLEDFY GLERFYKVEK KEDLISHLIV GLAPHTSAGV LGRVVGFTRA
LCCYAHPYFH SAKRRNCDSD EDSVMLLMDA LLNFSKVYLP STRGGKMDAP LVLSSRIDPE
EIDDESHNID VMPRLPKELY EKTLEFAKPS DVLDLVDNVK KRIGTDDQYH GLMFSHNTSS
IHSGPTQCLY KRLPTMKEKV EGQITLAERL RAVDQKGVVE GVLTSHFLPD MAGNLRAFSR
QKVRCTKCGK KYRRMPLSGE CTCGSNLILS ISKGSVMKYL EISNELSKRY PIDPYLVQRI
GLLESGINSL FESDKSKQSS LDVFL
//
