ID   DP2S_ARCFU              Reviewed;         488 AA.
AC   O28484;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=DNA polymerase II small subunit;
DE            Short=Pol II;
DE            EC=2.7.7.7;
DE   AltName: Full=Exodeoxyribonuclease small subunit;
DE            EC=3.1.11.1;
GN   Name=polB; OrderedLocusNames=AF_1790;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.11.1;
CC   -!- SUBUNIT: Heterodimer of a large subunit and a small subunit.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase delta/II small subunit
CC       family. {ECO:0000305}.
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DR   EMBL; AE000782; AAB89458.1; -; Genomic_DNA.
DR   PIR; E69473; E69473.
DR   RefSeq; WP_010879286.1; NC_000917.1.
DR   AlphaFoldDB; O28484; -.
DR   SMR; O28484; -.
DR   STRING; 224325.AF_1790; -.
DR   DNASU; 1485013; -.
DR   EnsemblBacteria; AAB89458; AAB89458; AF_1790.
DR   GeneID; 24795533; -.
DR   KEGG; afu:AF_1790; -.
DR   eggNOG; arCOG04455; Archaea.
DR   HOGENOM; CLU_027850_1_0_2; -.
DR   OMA; HVQAALI; -.
DR   OrthoDB; 24499at2157; -.
DR   PhylomeDB; O28484; -.
DR   Proteomes; UP000002199; 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; IPR004843; Calcineurin-like_PHP_ApaH.
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; PF00149; Metallophos; 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   Reference proteome; Transferase.
FT   CHAIN           1..488
FT                   /note="DNA polymerase II small subunit"
FT                   /id="PRO_0000096175"
SQ   SEQUENCE   488 AA;  54586 MW;  E2BF48D9294F3175 CRC64;
     MVIKNIDAAT VAKKFLVRGY NIDPKAAELI CKSGLFSDEL VDKICRIANG GFIIEKSVVE
     EFLRNLSNLK PATLTPRPEE RKVEEVKASC IALKVIKDIT GKSSCQGNVE DFLMYFNSRL
     EKLSRIIRSR VNTTPIAHAG KVRGNVSVVG MVNEVYERGD KCYIRLEDTT GTITCVATGK
     NAEVARELLG DEVIGVTGLL KGSSLYANRI VFPDVPINGN GEKKRDFYIV FLSDTHFGSK
     EFLEKEWEMF VRWLKGEVGG KKSQNLAEKV KYIVIAGDIV DGIGVYPGQE DDLAISDIYG
     QYEFAASHLD EIPKEIKIIV SPGNHDAVRQ AEPQPAFEGE IRSLFPKNVE HVGNPAYVDI
     EGVKVLIYHG RSIDDIISKI PRLSYDEPQK VMEELLKRRH LSPIYGGRTP LAPEREDYLV
     IEDVPDILHC GHIHTYGTGF YRGVFMVNSS TWQAQTEFQK KVNLNPMPGN VAVYRPGGEV
     IRLRFYGE