DP2L_METAC
ID DP2L_METAC Reviewed; 1145 AA.
AC Q8THG5;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=MA_4552;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE010299; AAM07891.1; -; Genomic_DNA.
DR RefSeq; WP_011024425.1; NC_003552.1.
DR AlphaFoldDB; Q8THG5; -.
DR SMR; Q8THG5; -.
DR STRING; 188937.MA_4552; -.
DR EnsemblBacteria; AAM07891; AAM07891; MA_4552.
DR GeneID; 1476446; -.
DR KEGG; mac:MA_4552; -.
DR HOGENOM; CLU_001154_0_0_2; -.
DR InParanoid; Q8THG5; -.
DR OMA; KRRNCDG; -.
DR OrthoDB; 559at2157; -.
DR PhylomeDB; Q8THG5; -.
DR Proteomes; UP000002487; 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..1145
FT /note="DNA polymerase II large subunit"
FT /id="PRO_0000152574"
SQ SEQUENCE 1145 AA; 127679 MW; 36C329A400C09E43 CRC64;
MGETIASEEM HEYFDGLEAR LKEAIEIANR ARAQGGDPKP TVEIPLAKDL ADRVENLIGV
QGVAAKIREL ETRMSREEAA LEIGKQVAEG VVGSFPTKKD AVEAAIRVSM ATLTEGVVAA
PIEGIDKVEL GKNDDGSQYI RIFYSGPIRS AGGTAQALSV LVGDYVRRGI GIDRYKPREE
EVERYVEEIL LYKRVASLQY TPSEDEIRLI VRNCPVCIDG DPTEEAEVEG HRDLERIGTN
RVRGGMCLVL AEGLALKAPK VKKHVNKLKM DGWDWLETLI GGAKSGGSAE DEQKSKIKPK
DKYIRDLIAG RPVFSHPSRP GGFRLRYGRS RNTSFASAGI NPASMVLLDD FITNGTQLKV
ERPGKAAAMS AVDSIEGPTV RLFSGDLVRI DNIKEAYELR PQVESIVDIG EILINYGDFL
ENNHPLMPSP YVFEWWQYDY EAACPEKTPE EELKNPSSAL ALRLAEEYNV PLHPTFTYLW
HDINRNEFEA LRKFVVEKGT FDGEGTLKLP LTASFEEGIK PLLEKLLVLH RVKEDKILVE
EALPFVLCLG LDSSLKEKAG MPDTDDMVEA AGVLSGFKVY PRAPSRIGAR MGRPEKSDLR
KMSPAAQVLF PINNCGGITR NLVSASDYTS CMNGKIGEIE VELGLRECPA CGKETYFWRC
ECGEFTNPKL SCPRCKIDVR GAETCPKCGR KPTSVANVKL DFRSVYKQAF ENVGEREKMD
LIKGVKRLMN GQMTPEPLEK GILRAKHDVY IFKDGTVRYD MSDIPLTHIR ADELGITATK
LLELGYREDI YGNPLERDDQ VVCLKVQDLV ISYDGGEYML RTAKYVDDLL VKYYKVGPYY
NAETIQDLVG VLLIGLAPHT SAGVLGRLIG FTKASVGYAH PFFHASKRRN CDGDEDCIML
LMDGILNFSR SYLPDKRGGK MDAPLVLTTR IDPKEVDKEA HNIDVPARYP LEFYRATQEI
KNPTELESIM DLISGRLGTP EQYEHFMFTH DTSDIAAGPL NSSYKTLGSM IEKMEAQLSL
ANRIRAVDAP DVAERVLKSH FLPDLIGNLR SFSRQRMRCI KCGEKFRRPP LTGACPKCGG
NVVLTVHEGA VRKYLEISKE IGERYGVSSY TRQRIELLDY DICSLFENHK VKQLGLSDFM
SGSAR
