ID B5I9U6_ACIB4 Unreviewed; 466 AA.
AC B5I9U6;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=DNA polymerase II small subunit {ECO:0000256|HAMAP-Rule:MF_00325};
DE Short=Pol II {ECO:0000256|HAMAP-Rule:MF_00325};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_00325};
DE AltName: Full=Exodeoxyribonuclease small subunit {ECO:0000256|HAMAP-Rule:MF_00325};
DE EC=3.1.11.1 {ECO:0000256|HAMAP-Rule:MF_00325};
GN Name=polB {ECO:0000256|HAMAP-Rule:MF_00325};
GN OrderedLocusNames=Aboo_0612 {ECO:0000313|EMBL:ADD08423.1};
OS Aciduliprofundum boonei (strain DSM 19572 / T469).
OC Archaea; Candidatus Thermoplasmatota; DHVE2 group; Aciduliprofundum.
OX NCBI_TaxID=439481 {ECO:0000313|EMBL:ADD08423.1, ECO:0000313|Proteomes:UP000001400};
RN [1] {ECO:0000313|Proteomes:UP000001400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19572 / T469 {ECO:0000313|Proteomes:UP000001400};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., Woyke T.;
RT "Complete sequence of Aciduliprofundum boonei T469.";
RL Submitted (FEB-2010) 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:ARBA00024817,
CC ECO:0000256|HAMAP-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;
CC Evidence={ECO:0000256|ARBA:ARBA00000563, ECO:0000256|HAMAP-
CC Rule:MF_00325};
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_00325};
CC -!- SUBUNIT: Heterodimer of a large subunit and a small subunit.
CC {ECO:0000256|ARBA:ARBA00011315, ECO:0000256|HAMAP-Rule:MF_00325}.
CC -!- SIMILARITY: Belongs to the DNA polymerase delta/II small subunit
CC family. {ECO:0000256|ARBA:ARBA00006035, ECO:0000256|HAMAP-
CC Rule:MF_00325}.
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DR EMBL; CP001941; ADD08423.1; -; Genomic_DNA.
DR RefSeq; WP_008082174.1; NC_013926.1.
DR AlphaFoldDB; B5I9U6; -.
DR STRING; 439481.Aboo_0612; -.
DR GeneID; 8827557; -.
DR KEGG; abi:Aboo_0612; -.
DR eggNOG; arCOG04455; Archaea.
DR HOGENOM; CLU_027850_1_0_2; -.
DR OrthoDB; 372039at2157; -.
DR Proteomes; UP000001400; Chromosome.
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: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 CDD; cd07386; MPP_DNA_pol_II_small_archeal_C; 1.
DR Gene3D; 3.60.21.50; -; 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; IPR011149; Pol2_small_arc.
DR PANTHER; PTHR10416; DNA POLYMERASE DELTA SUBUNIT 2; 1.
DR PANTHER; PTHR10416:SF0; DNA POLYMERASE DELTA SUBUNIT 2; 1.
DR Pfam; PF04042; DNA_pol_E_B; 1.
DR PIRSF; PIRSF000803; Arc_Pol2_small; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00325};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00325};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_00325};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_00325};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00325};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_00325}; Nuclease {ECO:0000256|HAMAP-Rule:MF_00325};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00325}; Reference proteome {ECO:0000313|Proteomes:UP000001400};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00325}.
FT DOMAIN 216..412
FT /note="DNA polymerase alpha/delta/epsilon subunit B"
FT /evidence="ECO:0000259|Pfam:PF04042"
SQ SEQUENCE 466 AA; 53346 MW; 1A9D403491FC72EF CRC64;
MDVRKEIVEE LLKHEILVEP EVVDYIIEKG GLNYVPSFIE LHKNSSFVSI SSIKPPKIEN
KPKEKSDMTK PEAYEYDWDF KVLIDPGNIQ SSGKVDDFRA LFLDRYKRLS KYVRRNMQMR
GATEIANMER GEVKIIGLVD DVRYTSRGSL SFYLEDPTGR VKCIAPQGEF LLNDEVIGVI
GKYNEESNLI YVNEIVRPGF RKINKGRVTE EQIGAVIISD VHIGSKMFLQ KNWEKFLDWL
KSGKNGAEIV KYLIIGGDLV DGIGIYPNQE EELEILDIYK QYEALASYIQ ELPDYIKVIM
IPGNHDLVRN AEPQPPLPSD VRALFNGNVE FLSNPTLFSL HGYKFLLYHG AAINDLVELI
PGMNYEKIGS IMRNMLEMRH LYPPYGGKVP IAPLKRDFLA IDLVPDVFVT GHVHAFTYEK
YKDVHIINAS CWQAQTKYQK MMNFNPVPGK VALINFHTDE VKVLSF
//
