ID   DP2S_HALS3              Reviewed;         508 AA.
AC   B0R7U1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=DNA polymerase II small subunit {ECO:0000255|HAMAP-Rule:MF_00325};
DE            Short=Pol II {ECO:0000255|HAMAP-Rule:MF_00325};
DE            EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_00325};
DE   AltName: Full=Exodeoxyribonuclease small subunit {ECO:0000255|HAMAP-Rule:MF_00325};
DE            EC=3.1.11.1 {ECO:0000255|HAMAP-Rule:MF_00325};
GN   Name=polB {ECO:0000255|HAMAP-Rule:MF_00325}; OrderedLocusNames=OE_4390F;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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_00325};
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_00325};
CC   -!- SUBUNIT: Heterodimer of a large subunit and a small subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00325}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase delta/II small subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_00325}.
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DR   EMBL; AM774415; CAP14810.1; -; Genomic_DNA.
DR   RefSeq; WP_012289503.1; NC_010364.1.
DR   AlphaFoldDB; B0R7U1; -.
DR   SMR; B0R7U1; -.
DR   EnsemblBacteria; CAP14810; CAP14810; OE_4390F.
DR   GeneID; 5954293; -.
DR   GeneID; 62887670; -.
DR   KEGG; hsl:OE_4390F; -.
DR   HOGENOM; CLU_027850_0_0_2; -.
DR   OMA; HVQAALI; -.
DR   PhylomeDB; B0R7U1; -.
DR   Proteomes; UP000001321; 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_00325; DNApol_II_A_arch; 1.
DR   InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR   InterPro; IPR024826; DNA_pol_delta/II_ssu.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR011149; Pol2_small_arc.
DR   PANTHER; PTHR10416; PTHR10416; 1.
DR   Pfam; PF04042; DNA_pol_E_B; 1.
DR   PIRSF; PIRSF000803; Arc_Pol2_small; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW   Hydrolase; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN           1..508
FT                   /note="DNA polymerase II small subunit"
FT                   /id="PRO_1000116096"
FT   REGION          66..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  54539 MW;  8E8AF89D9F915B24 CRC64;
     MPLEPSVRVV RELTSRGYNA DREAVTLLAG ADDPGAAVER AVAAAAADAA TLTVSDVRAV
     LDAHTASSAA QTSAPASTPP DEATTHTDPS ATDTPPNHDG GRAATADARS VEIDGDMTGA
     STGTGEYQDF VSVFRDRYDR LAAQLRGRVN HRPTSALASM PGGSDAAIVG MVNDIRSTTS
     GHWRVELEDT NGVFPVLVLK DRDVSDLVDD LLLDEVIAVS GTLADDGTIL FADDIYFPEV
     PRTYSPSTAD RSVQAALISD VHVGSQEFAA DAWRSFADWL HTPAAESVEY LLIAGDMVEG
     VGVYPGQDEE LDIVDIYDQY ETFAEHLKDV PGDMEIVMIP GNHDAVRLAE PQPAFDEELR
     SIMRAHDARI TSNPSTVTID GVSVLLYHGV SLDEVIAEHP SDDVTYDDPQ NAMELLLKKR
     HVAPPFGGRT RLAPEAEDHL AIDTVPDVFH TGHVHKLGVG IHHNVRLVNS GCWQHQTAFQ
     ESVNISPDVA TAPILDLDTL DITVHKFS