ID A0A4E0QZ59_9EURY Unreviewed; 507 AA.
AC A0A4E0QZ59;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 25.
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 ORFNames=CUN85_08220 {ECO:0000313|EMBL:TGC09004.1};
OS Methanolobus halotolerans.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX NCBI_TaxID=2052935 {ECO:0000313|EMBL:TGC09004.1, ECO:0000313|Proteomes:UP000297295};
RN [1] {ECO:0000313|EMBL:TGC09004.1, ECO:0000313|Proteomes:UP000297295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY-01 {ECO:0000313|EMBL:TGC09004.1,
RC ECO:0000313|Proteomes:UP000297295};
RA Shen Y., Huang H.-H., Lai M.-C., Chen S.-C.;
RT "Isolation and Characterization of Methanogenic Archaea from Saline
RT Meromictic Lake at Siberia.";
RL Submitted (NOV-2017) 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=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC EC=2.7.7.7; Evidence={ECO:0000256|ARBA:ARBA00049244,
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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TGC09004.1}.
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DR EMBL; PGGK01000007; TGC09004.1; -; Genomic_DNA.
DR RefSeq; WP_135389831.1; NZ_PGGK01000007.1.
DR AlphaFoldDB; A0A4E0QZ59; -.
DR OrthoDB; 372039at2157; -.
DR Proteomes; UP000297295; Unassembled WGS sequence.
DR GO; GO:0042575; C:DNA polymerase complex; IEA:TreeGrafter.
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:0006271; P:DNA strand elongation involved in DNA replication; IEA:TreeGrafter.
DR CDD; cd07386; MPP_DNA_pol_II_small_archeal_C; 1.
DR CDD; cd04490; PolII_SU_OBF; 1.
DR FunFam; 3.60.21.50:FF:000003; DNA polymerase II small subunit; 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; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR011149; Pol2_small_arc.
DR NCBIfam; NF003118; PRK04036.1-3; 1.
DR NCBIfam; NF003120; PRK04036.1-5; 1.
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 Pfam; PF01336; tRNA_anti-codon; 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|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00325};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00325};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_00325};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00325};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00325}; Reference proteome {ECO:0000313|Proteomes:UP000297295};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00325}.
FT DOMAIN 159..220
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
FT DOMAIN 250..451
FT /note="DNA polymerase alpha/delta/epsilon subunit B"
FT /evidence="ECO:0000259|Pfam:PF04042"
SQ SEQUENCE 507 AA; 56236 MW; EC31159F7D827E7E CRC64;
MNEVDVLTVF IEEGYQITAE AVELICSHCS PEKLIQHVLE NIDASVLVID MEHIDLETVG
TFDTGPDSDD TFTIQASRPL SSVVTSNDLS LSDNPVSVIS DISDNSTCVG EYIEFVQFFR
NRYSRLSEII RSRVNARPIE SLSKNRSPGL RGGKDFGEVS IIGMISNIKS TSNGHKILEV
EDTTGSFSVL VRMADKELYE QATHLVLDEV VGFSGILTND GKLMIARKII LPDLPNTMAK
KSGSSGKAVL TSDVHVGSST FLEEPWERFV DFLKGDTDNE ALAAISREVR YLVVAGDLVD
GVGIYPGQEH ELTIPDVYDQ YRKAAEYFDE IPKHIKVIIS PGNHDAVRQA EPQPKLPECI
RVDFPSNVTF VGNPSMVDLD GTKILIYHGR SIDDLVAAVP GVSYHAPTKG MVEMMKFRHL
SPMYGSRVSI APEKNDHFVL SHVPDILHCG HVHTVGVEWY KNVLLINSGT WQDQTEFQKR
MNVVPTPCQV PVVDLATYRT SILRFDE
//
