ID A0A1G7JQI3_9EURY Unreviewed; 1195 AA.
AC A0A1G7JQI3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=SAMN05216218_10512 {ECO:0000313|EMBL:SDF26719.1};
OS Halorientalis regularis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorientalis.
OX NCBI_TaxID=660518 {ECO:0000313|EMBL:SDF26719.1, ECO:0000313|Proteomes:UP000199076};
RN [1] {ECO:0000313|EMBL:SDF26719.1, ECO:0000313|Proteomes:UP000199076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10760 {ECO:0000313|EMBL:SDF26719.1,
RC ECO:0000313|Proteomes:UP000199076};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNBK01000005; SDF26719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7JQI3; -.
DR STRING; 660518.SAMN05216218_10512; -.
DR OrthoDB; 7529at2157; -.
DR Proteomes; UP000199076; 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: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 7..945
FT /note="DNA polymerase II large subunit DP2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03833"
FT REGION 274..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..308
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1195 AA; 132130 MW; 280CB1A665B7253B CRC64;
MREADRRYFE RLEADLDDAF EVATAARERG GDPTKDVEIP TARDMADRVE NILGIDGVAE
RVRDLEGEMS REEAALELVE DFVDGSVGDY DTDAGKIEGA VRTAVALLTE GVVAAPIEGI
DRVEVLENDD GTEFVNVYYA GPIRSAGGTA QALSVLVADY ARSLLGMDEF KARNDEIGRY
AEEVDLYDQE TGLQYSPKEK ESEFIAEHMP IMLDGEATGD DEVSGYRDLE RIDTNSARGG
MCLVFAEGIA LKAPKIQRYT RNLDEVEWPW LQDLIDGTIG EDGGDEGEDG EEAEASDGEA
DDAAEDATDE PAGPPRVDPS EKFLRDLIAG RPVFTHPSEP GGFRLRYGRA RNHGFATAGV
HPATMHLVDD FLATGTQIKT ERPGKAAGVV PVDTIEGPTV RLANGDVRRI DDPAEALEVR
NGVEKILDLG EYLVNYGEFV ENNHPLAPAS YTVEWWEQDL EASAADVQAM RDSVRVDLAD
PSADEAIEWA SEYDAPLHPK YTYCWHDISV AEFERLAAAV ADGEIANTDG AVLSDDDTGD
PADGDLIVPR PDDPDKEVSG VLESLLVEHH QHEDRLVVPD WKPLVLSLGL TERLEREWEP
ADLPAAAREY ADGENAIRAV DAVAPVEIRE RAPTRIGNRM GRPEKSESRE LSPAVHTLFP
IGEAGGSQRD VSKAADAGDA VEGTQGEVEV QVGRRECTEC ASRTYHARCP DCNGVTDAVY
VCRDCDIEVE PDESGRAQCH RCESLASPVQ TKTISVREEF RDALDEVGLR ENAFDIVKGV
KGLSSKTKTP EPIEKGILRA KHGVSAFKDG TVRYDMTDLP VTAVRPAELD VTADQFRELG
YEEDMQGEPL RHDDQLVELK VQDIVLSDGA AEHMLKTADF VDDLLESYYG LDPFYDVDDR
QELVGELVFG MAPHTSAAVI GRVIGFTSAA VGYAHPYFHA SKRRNCDGDE DCVMLLLDGL
LNFSKKFLPD QRGGRMDAPL VMSSRIDPTE IDDEAHNMDV MDQYPREFYE ATREMADPGE
VEDIMTIAEE NLGTDREYTD FRHSHDTSNI ALGPDLSAYK TLDDMMKKMN AQLELSRKLR
AVDETDVAER VIEYHFLPDI IGNLRAFSQQ ETRCLDCGEK YRRVPLTGDC RKCGGDMTLT
VHHGSVNKYI DTALEVAEEY DTREYTTQRL EILQKSIKRI FENDNNKQSG IGDFM
//
