DP2S_PYRFU
ID DP2S_PYRFU Reviewed; 613 AA.
AC P81412;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-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=DP1;
DE AltName: Full=Exodeoxyribonuclease small subunit;
DE EC=3.1.11.1;
GN Name=polB; OrderedLocusNames=PF0018;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=9348040; DOI=10.1046/j.1365-2443.1997.1380336.x;
RA Uemori T., Sato Y., Kato I., Doi H., Ishino Y.;
RT "A novel DNA polymerase in the hyperthermophilic archaeon, Pyrococcus
RT furiosus: gene cloning, expression, and characterization.";
RL Genes Cells 2:499-512(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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.
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 -!- INTERACTION:
CC P81412; O73947: pcn; NbExp=2; IntAct=EBI-15906191, EBI-15762053;
CC -!- SIMILARITY: Belongs to the DNA polymerase delta/II small subunit
CC family. {ECO:0000305}.
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DR EMBL; D84670; BAA25163.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL80142.1; -; Genomic_DNA.
DR PIR; T43933; T43933.
DR RefSeq; WP_011011130.1; NC_018092.1.
DR AlphaFoldDB; P81412; -.
DR SMR; P81412; -.
DR DIP; DIP-59599N; -.
DR IntAct; P81412; 1.
DR STRING; 186497.PF0018; -.
DR DNASU; 1467846; -.
DR EnsemblBacteria; AAL80142; AAL80142; PF0018.
DR GeneID; 41711804; -.
DR KEGG; pfu:PF0018; -.
DR PATRIC; fig|186497.12.peg.20; -.
DR eggNOG; arCOG04455; Archaea.
DR HOGENOM; CLU_027850_1_0_2; -.
DR OMA; FIGPGNH; -.
DR OrthoDB; 11652at2157; -.
DR PhylomeDB; P81412; -.
DR BRENDA; 2.7.7.7; 5243.
DR Proteomes; UP000001013; 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 Gene3D; 2.40.50.140; -; 1.
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; IPR012340; NA-bd_OB-fold.
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; SSF50249; SSF50249; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW Hydrolase; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..613
FT /note="DNA polymerase II small subunit"
FT /id="PRO_0000096180"
SQ SEQUENCE 613 AA; 69184 MW; 7161981456358832 CRC64;
MDEFVKSLLK ANYLITPSAY YLLREYYEKG EFSIVELVKF ARSRESYIIT DALATEFLKV
KGLEPILPVE TKGGFVSTGE SQKEQSYEES FGTKEEISQE IKEGESFIST GSEPLEEELN
SIGIEEIGAN EELVSNGNDN GGEAIVFDKY GYPMVYAPEE IEVEEKEYSK YEDLTIPMNP
DFNYVEIKED YDVVFDVRNV KLKPPKVKNG NGKEGEIIVE AYASLFRSRL KKLRKILREN
PELDNVVDIG KLKYVKEDET VTIIGLVNSK REVNKGLIFE IEDLTGKVKV FLPKDSEDYR
EAFKVLPDAV VAFKGVYSKR GILYANKFYL PDVPLYRRQK PPLEEKVYAI LISDIHVGSK
EFCENAFIKF LEWLNGNVET KEEEEIVSRV KYLIIAGDVV DGVGVYPGQY ADLTIPDIFD
QYEALANLLS HVPKHITMFI APGNHDAARQ AIPQPEFYKE YAKPIYKLKN AVIISNPAVI
RLHGRDFLIA HGRGIEDVVG SVPGLTHHKP GLPMVELLKM RHVAPMFGGK VPIAPDPEDL
LVIEEVPDVV HMGHVHVYDA VVYRGVQLVN SATWQAQTEF QKMVNIVPTP AKVPVVDIDT
AKVVKVLDFS GWC
