ID   DP2S_METJA              Reviewed;         594 AA.
AC   Q58113;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 122.
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=MJ0702;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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; L77117; AAB98694.1; -; Genomic_DNA.
DR   PIR; F64387; F64387.
DR   RefSeq; WP_010870207.1; NC_000909.1.
DR   AlphaFoldDB; Q58113; -.
DR   SMR; Q58113; -.
DR   STRING; 243232.MJ_0702; -.
DR   DNASU; 1451569; -.
DR   EnsemblBacteria; AAB98694; AAB98694; MJ_0702.
DR   GeneID; 1451569; -.
DR   KEGG; mja:MJ_0702; -.
DR   eggNOG; arCOG04455; Archaea.
DR   HOGENOM; CLU_027850_1_0_2; -.
DR   InParanoid; Q58113; -.
DR   OMA; HVQAALI; -.
DR   OrthoDB; 24499at2157; -.
DR   PhylomeDB; Q58113; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0042575; C:DNA polymerase complex; IBA:GO_Central.
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:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
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   Reference proteome; Transferase.
FT   CHAIN           1..594
FT                   /note="DNA polymerase II small subunit"
FT                   /id="PRO_0000096177"
SQ   SEQUENCE   594 AA;  69145 MW;  FA8F24702F2DE8FD CRC64;
     MEIINKFLDL EALLSPTVYE KLKNFDEEKL KRLIQKIREF KKYNNAFILL DEKFLDIFLQ
     KDLDEIINEY KDFDFIFYYT GEEEKEKPKE VKKEIKKETE EKIEKEKIEF VKKEEKEQFI
     KKSDEDVEEK LKQLISKEEK KEDFDAERAK RYEHITKIKE SVNSRIKWIA KDIDAVIEIY
     EDSDVSGKST CTGTIEDFVK YFRDRFERLK VFIERKAQRK GYPLKDIKKM KGQKDIFVVG
     IVSDVDSTRN GNLIVRIEDT EDEATLILPK EKIEAGKIPD DILLDEVIGA IGTVSKSGSS
     IYVDEIIRPA LPPKEPKRID EEIYMAFLSD IHVGSKEFLH KEFEKFIRFL NGDVDNELEE
     KVVSRLKYIC IAGDLVDGVG VYPGQEEDLY EVDIIEQYRE IAMYLDQIPE HISIIISPGN
     HDAVRPAEPQ PKLPEKITKL FNRDNIYFVG NPCTLNIHGF DTLLYHGRSF DDLVGQIRAA
     SYENPVTIMK ELIKRRLLCP TYGGRCPIAP EHKDYLVIDR DIDILHTGHI HINGYGIYRG
     VVMVNSGTFQ EQTDFQKRMG ISPTPAIVPI INMAKVGEKG HYLEWDRGVL EVRY