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Entry: A0A0E3KW71_9EURY
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ID   A0A0E3KW71_9EURY        Unreviewed;      1150 AA.
AC   A0A0E3KW71;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 47.
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   ORFNames=MSWH1_0082 {ECO:0000313|EMBL:AKB20353.1};
OS   Methanosarcina sp. WH1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1434102 {ECO:0000313|EMBL:AKB20353.1, ECO:0000313|Proteomes:UP000033112};
RN   [1] {ECO:0000313|EMBL:AKB20353.1, ECO:0000313|Proteomes:UP000033112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH1 {ECO:0000313|EMBL:AKB20353.1,
RC   ECO:0000313|Proteomes:UP000033112};
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) 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; CP009504; AKB20353.1; -; Genomic_DNA.
DR   RefSeq; WP_048125100.1; NZ_CP009504.1.
DR   AlphaFoldDB; A0A0E3KW71; -.
DR   GeneID; 24812537; -.
DR   KEGG; mef:MSWH1_0082; -.
DR   PATRIC; fig|1434102.4.peg.100; -.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   Proteomes; UP000033112; Chromosome.
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          12..895
FT                   /note="DNA polymerase II large subunit DP2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03833"
SQ   SEQUENCE   1150 AA;  128293 MW;  A6367E03CDE92CCF CRC64;
     MGETIASEEM HEYFNGLEAR LKEAIEVANR ARSRGGDPKP TVEIPLAKDL ADRVENLIGV
     KGVAAKIREL EVNMSREEAA LEVGRQVAEG IVGSFPAKKD AVEAAIRVSM AVLTEGVVAA
     PIEGIDKVDL GKNDDGSQYI RIFYSGPIRS AGGTAQALSV LVGDYVRRGI GIDRYKPRDE
     EIERYVEEIL LYKRVASLQY MPSEDEIRLI VRNCPVCIDG DPTEEAEVEG HRNLERIGTN
     RVRGGMCLVL AEGLALKAPK VKKHVNKLKM DGWDWLETLI GGAKSGESAE DEQKNKIKPK
     DKYIRDLIAG RPVFSHPSRP GGFRLRYGRS RNTSFASAGI SPASMVLLDD FIANGTQLKV
     ERPGKAAAMS AVDSIEGPTV RLFSGDLIRI DNIKEAYEVR PQVEVIVDIG EILINYGDFL
     ENNHPLMPSP YVFEWWQYDY QAACPEQIPE DELKNPSAAL ALRLAEEFNV PLHPKFTYLW
     HDINRNEFEA LRNFVAEKGS FLAGEVAGAG VLKLPMKASL EEGIKPVLEK LLVLHRVKDD
     EILIEEALPF ILCLGLDPSL KEKASMPDLD DMVEAAGVLS GFKVYPRAPS RIGARMGRPE
     KSDLRKMSPA AQVLFPLNNS GGITRNLVSA SDYTSCMNGK IGEIEVELGL RECPACRKET
     YFWRCECGEF TNPKLFCSRC KIDVRGAEVC PKCGRKPTSV ANVKLDFRSI YKQAFENLGE
     REKMGLIKGV KRLMNGQMTP EPLEKGILRS KHNVYVFKDG TIRYDMSDIP LTHIRADELG
     ITAAKLLELG YREDICGNPL ERDDQVVCLK VQDLVISYDG AEYMLRTAKY VDDLLVKYYK
     IEPYYNAETI QDLVGVLLIG LAPHTSAGVL GRLIGFTKAS VGYAHPFFHA SKRRNCDGDE
     DCIMLLMDGI LNFSRSYLPD KRGGKMDAPL VLTTRIDPKE VDKEAHNIDV SARYPFEFYR
     ATQEIKSPTE LESIMDLISS RLGTPEQYEH FMFTHDTSNI AAGPLNSSYK TLGSMIEKME
     AQLTLANRIR AVDASDVAER VLKSHFLPDL IGNLRSFSRQ RMRCIKCGEK FRRPPLTGAC
     PKCGGNVILT VHEGSVRKYL EISKEIGERY GVSSYTRQRI ELLDYDISSL FENHRVKQLG
     LSDFMSGSAR
//
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