ID A0A3P3R910_9EURY Unreviewed; 1653 AA.
AC A0A3P3R910;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, 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 ORFNames=EIK79_13455 {ECO:0000313|EMBL:RRJ29140.1};
OS Halomarina oriensis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomarina.
OX NCBI_TaxID=671145 {ECO:0000313|EMBL:RRJ29140.1, ECO:0000313|Proteomes:UP000282322};
RN [1] {ECO:0000313|EMBL:RRJ29140.1, ECO:0000313|Proteomes:UP000282322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP-AMP-1 {ECO:0000313|EMBL:RRJ29140.1,
RC ECO:0000313|Proteomes:UP000282322};
RA Pal Y., Srinivasana K., Verma A., Kumar P.;
RT "Taxonoimc description of Halomarina strain SPP-AMP-1.";
RL Submitted (NOV-2018) 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}.
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:RRJ29140.1}.
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DR EMBL; RRCH01000029; RRJ29140.1; -; Genomic_DNA.
DR OrthoDB; 7529at2157; -.
DR Proteomes; UP000282322; 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; 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; IPR004042; Intein_endonuc.
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; PF14890; Intein_splicing; 1.
DR Pfam; PF03833; PolC_DP2; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
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.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00324}.
FT DOMAIN 1162..1296
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT REGION 276..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1653 AA; 182457 MW; A2E56B38E29EF673 CRC64;
MSAEERYFEQ IEARLDEAFS VARSAKERGG DPSTEVEIPV AKDMADRVEN ILGIEGVAQR
VRELEGEMSR EEAALALAED FAEERVGDYE TTAGKIEGAV RTAVALLTEG VVAAPIEGID
RVEVLENDDG SRFVRVFYAG PIRSAGGTAQ ALSVLVADYA RTLLGLDRYK PREEEVERYA
EELGLYDNET GLQYSPKDKE TTFIAEHCPI MLDGEATGET EVSATRDLER VDTNNPRGGM
CLVLGEGIAQ KAPKIKRYTG QLAELEWPWL DDLIEGTIGT DSDDGSDTDT ETDTDGDADS
QTSAVEDASA SESGPPRAEQ TTKFLRDLIA GRPVFSHPSR TGGFRLRYGR ARNHGFATAG
VHPATMHLVD DFLATGTQIK TERPGKAAGV VPVDTIEGPT VRLANGEVRR IDDPEEAKEI
RNGVEAILDL GEYLVNYGEF VENNHPLAPA SYTVEWWVQE FERAGGDVQA LRDDPHVDLA
APPVTRALAW ATDEVPLHPE YTYLWHDLTV GQFDELADAV SAGRVSETDD TLVVPRTEST
RTALETLLVE HTTDEEITIP DASALIHSLG LTPDLEREWS LNDLSETARS WGESAGSNAI
KAVNEVAPFS VRERAPTRVG NRMGRPEKSE KRELSPAVHT LFPIGESGGS QRDVAQAAAH
TESMRSTAGE VELTIARREC VDCGTTTFTA RCPDCGGVTE PVYVCRDCDI RVEPDESGRA
ECPRCEELAT PVENRTVDLN EAYHEALSAV GEREHAFEIL KGVKGLTSEQ KVPEPMEKGV
LRAKHDVSAF KDGTIRYDMT DLPVTAVRPA ELDVTVEQFR ELGYETDIDG AALRHDDQLV
ELRVQDIVLS SGAAEHMLKT ADFVDDLLER YYGMEPFYDV DDRDELVGEL VFGMAPHTSA
AVVGRVVGFT DAAVGYAHPY FHAAKRRNCD GDEDCVMLLM DGLLNFSKLY LPDKRGGSVT
ADTRLTAFDP AGELQTLPIE ELWTELDCPI EYDGKFEKKS CLGEGWTTYA FDEHHETTPQ
PIEKAIRYRV EDEQLLQVKT QFGRSVTITD NHSLFRYDEG IETIAGAELD AGDLILAPRR
LAVDETETTI DVTDCLDTPH VFINDPDDGD QSTGRETLPF RVVAGSSSHS SQSVPNVMEI
GRKDSSSGLN RYIPVDEEVA WLLGLLIADG SQGKRPTLSV TEAAVLDRVL TIATGTLGCE
PAVETEHDTE HVRFPAVFND VLDHLGVTDT DADNEAFAVP DCVLRGERQI VQSFLRGYMT
GGRSGNETTA RSRIDLHAHS ESVKDGLVFL LHRLGLVANI TTHQTGEPAY TLSATREPQA
DSDGSEESLV VPVPDALLEL REMVQNGGQL IPRKYARRDT IPATKLREIV DTLTRRELST
AAETRLERLR PLVDGDLSYL KVTDIERVNY SGYLYDLQVG GEPIFTANWL YAHNSMDAPL
VMSSRIDPTE IDDEAHNVDI VSSYPVEFYE ATREMADPDE VDITIAEDTL GTDDQYSGFD
HTHDTSDLAA GPDLSAYKTL GSMLEKMDAQ LALARKLRAV DETDVAERII EYHFLPDLIG
NLRAFARQET RCLDCNRKYR RVPLSGECRE CGGRVNLTVH EGSVNKYLDT AIRVAEEFDC
REYTKQRLEI LKRQLESIFE NDHNKPSTLG DFM
//
