ID A0A6A9T666_9EURY Unreviewed; 1886 AA.
AC A0A6A9T666;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 02-APR-2025, entry version 20.
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:MUW14810.1};
GN ORFNames=GJ633_09140 {ECO:0000313|EMBL:MUW14810.1};
OS Halorubrum sp. CBA1125.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Halobacteria; Halobacteriales; Haloferacaceae; Halorubrum.
OX NCBI_TaxID=2668072 {ECO:0000313|EMBL:MUW14810.1, ECO:0000313|Proteomes:UP000432575};
RN [1] {ECO:0000313|EMBL:MUW14810.1, ECO:0000313|Proteomes:UP000432575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBA1125 {ECO:0000313|EMBL:MUW14810.1,
RC ECO:0000313|Proteomes:UP000432575};
RA Roh S.W.;
RT "Genomic analysis of Halorubrum sp. CBA1125.";
RL Submitted (DEC-2019) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MUW14810.1}.
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DR EMBL; WPCE01000085; MUW14810.1; -; Genomic_DNA.
DR RefSeq; WP_156588571.1; NZ_WPCE01000085.1.
DR OrthoDB; 7529at2157; -.
DR Proteomes; UP000432575; Unassembled WGS sequence.
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; 2.
DR CDD; cd00350; rubredoxin_like; 1.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR HAMAP; MF_00324; DNApol_II_L_arch; 1.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
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; TIGR01443; intein_Cterm; 1.
DR NCBIfam; TIGR01445; intein_Nterm; 1.
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; PF14890; Intein_splicing; 2.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF24846; PolC_DP2_cat; 3.
DR Pfam; PF24844; PolC_DP2_central; 1.
DR Pfam; PF03833; PolC_DP2_N; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 2.
DR SMART; SM00306; HintN; 2.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 2.
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:UP000432575};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00324}.
FT DOMAIN 1378..1514
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT REGION 277..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..292
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..312
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1886 AA; 209343 MW; 12C89471F7FB5799 CRC64;
MRPADERYFT RIEERLDEAW AVAEAAKEQG RDPEPEIEIP VARDMADRVE NILGIDGVAE
RVRELEGEIS REEAALELVT DFVEGTVGDY DSRAGKVEGA VRTAVALLTE GVVAAPIEGI
DRVEILENDD GTEFVNVYYA GPIRSAGGTA QALSVLVADY ARSLLGVDEY KPRDEEIERY
AEEIDLYDKE TGLQYTPKDK ESKFIAEHIP IMLDGEATSD EEVSGFRDLE RVDTNSARGG
MCLVAAEGIA LKAPKIQRYT RELDEVDWPW LQDLIDGTIG TDGAGDGDGG DAAGDDASEG
DDDPTEADET IADGDGADKE GAAEDGDALT GPPRAEPSQK FLRDLIAGRP VFTHPSEPGG
FRLRYGRARN HGFATGGVHP ATMHLVDDFL AAGTQIKTER PGKAHGVVPV DSIEGPTVRL
ANGEVRRIDD PEEAKAVRNG VEKVLDLGEY LVNYGEFVEN NHPLAPASYV PEWWVQEFEA
AGADVQALRD DPHVDLEHPA VDEALAWADE YDCPLHPEYT YLWHDVSVEQ FEALGGAVAA
GDVVEGVLAI ERTETTRETL EALLVEHAAT ADALRIPAWR PLAQSLGVDD GLRKTWEDLS
EAAREWDGGE NAVKAVNEVA PFEVRERAPT RVGNRMGRPE KSESRDLSPA VHTLFPINEA
GGPQRDVAEA ANTMDDRGRR GRLELDVADR VCPDCGDHTY RALCPGCETH TEPHYECGDC
GTVCEPDEAG RVECPRCEWE VSAATRREID VNDAYRSALA AVGEREAAFE ILKGVQGLTS
RNKTPEPIEK GVLRAKNGVT SFKDGTVRYD MTDLPVTAVR PEELDVTADH FRELGYETDI
DGEPLRHDDQ LVELKVQDIV LSDGAAEHML KTADFVDDLL AQFYGLDRFY EVNERDDLVG
ELVFGMAPHT SAATVGRVVG FTSAAVGYAH PYFHAAKRRN CFHPETEISY RDDAGWHRET
IEAFVEDRLD DPETDDFGTL VDELDGNVEV PSIDEDGNRS TQAVNAVSKH LSQDHLVRVE
TRRGRSIRVT PDHTMLRVAD GGVQQITANE LEVGDSVPAT ALRPEISAGT TADVTADGGI
ETDVVASIDF LESDVEHTYN LTVAETHTLV ANDLLVAQCD GDEDCVMLLM DGLLNFSKEY
LPDQRGGSVS EDSRLVARDP QGRIRYLTFD EFWNELGSPI EIDGKFKKRT CVREGWQTYT
FDENHKSSLQ PIEKAIRYRA DKDETLLKVE TQFGRSLDIT PNHSLFRYND GIEEVAGDDL
KPGDLVVAPK QLDVEPQAGT VVDVAECVDD PYVFIDESVE SYLREVWDDS AWGSDARAAF
DGGLSYRLSK KKVALRTLRE IEGVSRNWRA ELNPQIGRKG SSKGISRFIP MNDDFSWLLG
LFAAEGSTSS VRPTITNADE EIVRQTERII KDTLGVEPSV RWSNKAYEIG FPAVFEDVLF
ELGFRDEESY DSSEKIVPEP IRRGDRSTVR SFLRGFIVGD GSETSDDNQT TIAFHTTSED
LKDGIVFLLH RLGIVANVST RDREPPRQRI YTITVSGGAS DNPLRRVLDG EDPYQPKSLT
VSIPEELLEI RQMDIPDITE TIPKYLKRRE NISLEQLESI VETLDEHDLP VTAREKLETI
RPLVDGDLAY LRVTDIDSVE YDGHLYDLQV GGEPVFTADW LYAHNSMDAP LVMSSRIDPS
EIDDEAHNMD IVREYPLELY EASRELADPG EVEDRIQLGE DTLDTDDEYR GFDHTHDTTD
IAMGPDLSAY KTLGDMMEKM DAQLELARKL RAVDETDVAE RVIEYHFLPD IIGNLRAFSR
QETRCLDCGE KYRRMPLTGD CRECGGRVNL TVHEGSVSKY VDTAIEVAER FGCRPYTKQR
LKVLDESLES IFEDDTNKQS GIADFM
//
