ID C9RGL5_METVM Unreviewed; 1609 AA. AC C9RGL5; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 28-JAN-2026, entry version 82. 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 OrderedLocusNames=Metvu_0859 {ECO:0000313|EMBL:ACX72717.1}; OS Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7) OS (Methanococcus vulcanius). OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group; OC Methanococci; Methanococcales; Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=579137 {ECO:0000313|EMBL:ACX72717.1, ECO:0000313|Proteomes:UP000002063}; RN [1] {ECO:0000313|EMBL:ACX72717.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M7 {ECO:0000313|EMBL:ACX72717.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Lcollab F.I., Brettin T., Detter J.C., RA Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Ovchinikova G., Sieprawska-Lupa M., Whitman W.B., Woyke T.; RT "Complete sequence of chromosome of Methanocaldococcus vulcanius M7."; RL Submitted (OCT-2009) 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=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + CC diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA- CC COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; CC EC=2.7.7.7; Evidence={ECO:0000256|ARBA:ARBA00049244, 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 -!- 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 --------------------------------------------------------------------------- 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; CP001787; ACX72717.1; -; Genomic_DNA. DR RefSeq; WP_015732937.1; NC_013407.1. DR STRING; 579137.Metvu_0859; -. DR MEROPS; N10.005; -. DR GeneID; 8513196; -. DR KEGG; mvu:Metvu_0859; -. DR eggNOG; arCOG04447; Archaea. DR HOGENOM; CLU_001154_0_0_2; -. DR OrthoDB; 7529at2157; -. DR Proteomes; UP000002063; 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:0004519; F:endonuclease activity; IEA:InterPro. 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 GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR CDD; cd00081; Hint; 1. DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1. DR Gene3D; 3.10.28.10; Homing endonucleases; 1. DR HAMAP; MF_00324; DNApol_II_L_arch; 1. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR036844; Hint_dom_sf. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR004042; Intein_endonuc_central. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR004860; LAGLIDADG_dom. DR InterPro; IPR004475; PolC_DP2. DR InterPro; IPR056172; PolC_DP2_cat_dom. DR InterPro; IPR056171; PolC_DP2_central_dom. DR InterPro; IPR016033; PolC_DP2_N. DR NCBIfam; TIGR01445; intein_Nterm; 1. DR NCBIfam; TIGR00354; polC; 1. DR NCBIfam; NF003103; PRK04023.1; 1. DR NCBIfam; NF011303; PRK14715.1; 1. DR PANTHER; PTHR42210; DNA POLYMERASE II LARGE SUBUNIT; 1. DR PANTHER; PTHR42210:SF1; DNA POLYMERASE II LARGE SUBUNIT; 1. DR Pfam; PF14890; Intein_splicing; 1. DR Pfam; PF14528; LAGLIDADG_3; 1. DR Pfam; PF24846; PolC_DP2_cat; 2. DR Pfam; PF24844; PolC_DP2_central; 1. DR Pfam; PF03833; PolC_DP2_N; 1. DR PRINTS; PR00379; INTEIN. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1. DR SUPFAM; SSF55608; Homing endonucleases; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813}; 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}; Protein splicing {ECO:0000256|ARBA:ARBA00023000}; KW Reference proteome {ECO:0000313|Proteomes:UP000002063}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00324}. FT DOMAIN 1115..1250 FT /note="DOD-type homing endonuclease" FT /evidence="ECO:0000259|PROSITE:PS50819" SQ SEQUENCE 1609 AA; 184482 MW; 6863F49EA8059E6B CRC64; MIHVACSENM RKYFENIVKE VEKLYKIAEE CRSRGFDPTD EVEIPLAVDM ADRVEGLVGP KGVAKRIREL VKELGKEPAS LEIAKEIVEG KFGNFEKEKK AEQAVRTALA VLTEGIVAAP LEGIADVKIK KNPDGTEYLA IYYAGPIRSA GGTAQALSVL VGDFVRKAMN LDKYKPTEDE IERYVEEVEL YQSEVGSFQY SPTADEIRTA IRNIPIEITG EATDNVEVSG HRDLPRVETN QIRGGALLVL VEGVLLKAPK ILRHVDKLGI EGWDWLKDLK GKKDDNKSEE KVEDEEIDEE NDEELEGYWR DVNIEANKKF ISEVIAGRPV FAHPSKVGGF RLRYGRSRNT GFATQGFHPA LMYLVDEFMA VGTQLKTERP GKATCVVPVD SIEPPIVRLK NGDVVRVETA EKAIELRNRV DEILFLGDVL VNYGDFLENN HPLLPSCWCE EWYEQLLKSK NISYNEEFIG NPRPDEAVKF ALETKTPLHP RFTYHWHDVS KEEIILLRNW LLKGKEDNFE GKKVWIVDLE TEEDKKAKRV LELIGCCHLV RNKKVVIEEY YPLLYSLGFD VENKKDLVEN IEETANSAKN SIHFVNLLSP FEVRRNTYVY VGARMGRPEK AAPRKMKPPV NGLFPIGNAG GQVRLINKAV EENNTDDIDV SYAVCPKCEK ISLYRVCPFC GTKVELNKFG KIKAPLKDYW YNALKRLGIN KPGDVKCIKG MTSKQKIVEP LEKAILRAMN EVYVFKDGTT RFDCTDVPIT HFKPSEINVS VEKLKELGYE KDIHGRELVD EDQVLELKPQ DVIIPENCAE YFVKVANFID ELLEKLYKMD RFYNVKEKKD LIGHLVIGMA PHTSAGMVGR IIGYTEARVG YAHPYFHAAK RRNCFPGDTR ILVNIDGNVE RITLKELYEL FDEKYEVFEN DAFVRKKPLN NKNIKVYSFN PEHKNVVLTD IEEVIKLESP NHQIKITLDG NREFITTHDH SVMVYENGKF IKKLAMDVKE GDLMLIPKVD FEEDNIEEFD LLKEFSKEEF KDLWSILRVI GISNWIKENI GKELIRELKL DEYLKYDTIP LDKLLILLEK SNLTIDEVPK NCYIAVKDDK TNINRIIKIE PLLKLIGYYL SEGYARESKT VYQINFSNSE EEIRENIKKS IKEAFGGINV YESKEEGKLS LSSRVVYLFF TRVLKIGKNA KSKRIPSFIF KLPKEKVKLM LSAYFDVEGS ISNTKPRISV YSINKTLLED IDLLLNRFGI KTYWIDDKNV EGGGKENPKL AVYALNISGY YCDIFFKEIG FFLKRKQMIY ELHKNKVRKN DSTEHNFGWI VKVKKVEIIK SNDEFIYTLN AKKYHNVIIN ENIQTFQCDG DEDSFFLLLD AFLNFSKKFL PDKRGGQMDA PLVLTTILDP KEVDGEVHNM DTMWSYPLEF YEKTLEMPSP KDVKDIMETV EDRLGKPEQY EGIGYTHETS RVDLGPKVCA YKTLGSMLEK TASQLLVAKK IRATDEKDVA EKVIQSHFIP DLIGNLRAFS RQSVRCKCGA KFRRVPLRGK CPKCGSKLIL TVSKGAVEKY MDVAEKMAEQ YDVNNYIKQR LKIIREGINS IFENDKSKQV KLSDFFKIG //