DP2L_METMP
ID DP2L_METMP Reviewed; 1131 AA.
AC Q6M191;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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}; OrderedLocusNames=MMP0026;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF29582.1; -; Genomic_DNA.
DR RefSeq; WP_011169970.1; NC_005791.1.
DR AlphaFoldDB; Q6M191; -.
DR SMR; Q6M191; -.
DR STRING; 267377.MMP0026; -.
DR EnsemblBacteria; CAF29582; CAF29582; MMP0026.
DR GeneID; 2762226; -.
DR KEGG; mmp:MMP0026; -.
DR PATRIC; fig|267377.15.peg.26; -.
DR eggNOG; arCOG04447; Archaea.
DR HOGENOM; CLU_001154_0_0_2; -.
DR OMA; KRRNCDG; -.
DR OrthoDB; 559at2157; -.
DR BioCyc; MMAR267377:MMP_RS00160-MON; -.
DR Proteomes; UP000000590; 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..1131
FT /note="DNA polymerase II large subunit"
FT /id="PRO_0000294686"
SQ SEQUENCE 1131 AA; 128381 MW; 3A000B7DAC5961DE CRC64;
MLHVSASKGM TEYFKNILDD VSNLYNLAEE CRKNGYDVTD HVEIPLAKDM ADRVEGIVGP
KNVAERIREL VSEFGKEPAA LEIAKEIVEG KFGEFGREVG AEQAVRTALA VITEGIVAAP
LEGIAYVKIK KNSDNSEYLA IYFAGPIRSA GGTAQALAVL VGDYVRKNMG LDRFKPTEDE
VERYGEEVDL YQSEVTTFQY QPKAEEIRVA VRNISVEITG EATDDVEVSG HRDLPRVETN
QIRGGALLAL VEGVLLKAPK ILRHVDKLNI EGWNWLKELK SKKEEVIEEL EEENDEYNYE
DEEDLSQYED YEVEAVTKFI GEVIAGRPVF SHPSKKGGFR LRYGRSRNTG FATDGFHPAI
MYLVDDFMAV GTQLKTERPG KATCVVPVDS IEGPIVKLND GSVLKIDTVE KAKQYTDEVQ
EILFLGDILV NYGDFLENNH TVLPSSWCTE WYEKILKSQN LEYTEEFIKN PGQKEAVNYA
KITKTPLHPK YTYFWHDISK ENISTLRSWV IGGKYNPSND SWELNYDPED EEISNAKRYL
ELIGCPHIVM EEKVEIFEYY PFLYSLGYDF DEKRDMIDNI DEKLQNTKNN MHFINTIAPF
EIRRNAYIYV GARMGRPEKA AARKMKPPVN GLFPIGNAGA LVRLINKAVD EGKTDEIEIA
NVKCSCGKVS LYRTCPFCGN SVEPTGPSRI KLPIKDYWYK TLENLKINKP GDVKCIKGMT
SKDKIIEPLE KAILRAKNNI YVFKDGTTRF DCTDVPVTHF KPVEIHVPIE KLKSLGYLKD
IHGNPLENED QVLELKVQDV IVPESCMDYF LNVSGFIDDL LEKYYKKDRF YNVNTREDLV
GHLIIGMAPH TSAGMVGRII GYSNANVGYA HPYFHASKRR NCDGDEDAFF LLLDAFMNFS
KRFLPDKRGG QMDAPLVLTT ILDPKEVDGE VHNMDSMWEY PLEFYEKSLE GIAPKEIKKM
METIEDRLDK DSQYEGIGYT HETSKIDEGP PICAYKTLGS MMEKTSAQLA VAKKIRATDE
RDVAEKVIQS HFVPDLIGNL RAFSRQGVRC KCGAKYRRMP LKGVCRKCGS RLILTVSKGA
VEKYMNVSQT MAEKYDASDY IKQRLEIIKS GIDSLFVNDK RKQVKIEDFF K