ID L0I794_HALRX Unreviewed; 536 AA.
AC L0I794;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=Halru_0003 {ECO:0000313|EMBL:AGB14658.1};
OS Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halovivax.
OX NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB14658.1, ECO:0000313|Proteomes:UP000010846};
RN [1] {ECO:0000313|Proteomes:UP000010846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18193 / JCM 13892 / XH-70
RC {ECO:0000313|Proteomes:UP000010846};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Halovivax ruber XH-70.";
RL Submitted (SEP-2011) 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; CP003050; AGB14658.1; -; Genomic_DNA.
DR AlphaFoldDB; L0I794; -.
DR STRING; 797302.Halru_0003; -.
DR KEGG; hru:Halru_0003; -.
DR eggNOG; arCOG00258; Archaea.
DR eggNOG; arCOG04455; Archaea.
DR HOGENOM; CLU_027850_0_0_2; -.
DR OrthoDB; 372039at2157; -.
DR Proteomes; UP000010846; 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; cd04490; PolII_SU_OBF; 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|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00325}; 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:UP000010846};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00325}.
FT DOMAIN 284..481
FT /note="DNA polymerase alpha/delta/epsilon subunit B"
FT /evidence="ECO:0000259|Pfam:PF04042"
FT REGION 64..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 58825 MW; B3390AFE497FD8D3 CRC64;
MPLEGPARIV QQLTAHGYNA EREAVTLLAS RPDPTQALDR VLENTPDETL VIGAKDVERV
LDAETESTRE IAPPSESKAG TSDSAPATDT SRKTEIDTAG QDPTASPGER TTDSPGEAAV
DAVETGGFER AGDRSQRDIA IRGDMTGEST GTGEYRDFIA VFRDRLDKLS SKLSGRVNHR
PASSIESMPG GSDVAMIGLV NDIRSTASGH WLVELEDTTG TFPFLVMKDR EYVDLVDELL
RDEVIAMEGT LADDSGIAFV DSMYSPDVPR THEPKTADRH VEAALISDVH VGSDEFMADA
WNDFADWLHT EEAQHVEYLC IAGDMVEGVG VYPNQDEELD IIDIYEQYEA FNEYLKRVPG
DLDIVMIPGN HDAVRLAEPQ PGFNEELRSI MSAHDPQIVS NPSTVEIEGV SILMYHGVSL
DEVIAELPSE KASYDEPHKA MYQLLKKRHV APQFGGHTRL APEEKDHLVM ESVPDIFHTG
HVHKLGFGKY HDVLAINSGC WQAQTDFQKS VNIDPDSGFA PIVDLSTLDV TVRKFS
//
