ID A0A238XGW3_HALVU Unreviewed; 588 AA.
AC A0A238XGW3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=SAMN06264855_1185 {ECO:0000313|EMBL:SNR58235.1};
OS Halorubrum vacuolatum (Natronobacterium vacuolatum).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=63740 {ECO:0000313|EMBL:SNR58235.1, ECO:0000313|Proteomes:UP000198397};
RN [1] {ECO:0000313|EMBL:SNR58235.1, ECO:0000313|Proteomes:UP000198397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8800 {ECO:0000313|EMBL:SNR58235.1,
RC ECO:0000313|Proteomes:UP000198397};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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=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; FZNQ01000018; SNR58235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238XGW3; -.
DR OrthoDB; 372039at2157; -.
DR Proteomes; UP000198397; Unassembled WGS sequence.
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:UP000198397};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00325}.
FT DOMAIN 334..531
FT /note="DNA polymerase alpha/delta/epsilon subunit B"
FT /evidence="ECO:0000259|Pfam:PF04042"
FT REGION 62..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 64151 MW; 5186DC1DD218DEF4 CRC64;
MPLESTVRIV RELTERGYNA EREAVTLLAN AEQPGDAIDA VVEHAPDHAL RITADHVRSV
IEGRSEGGDP SPSFESTVAD IDDVDDGPAD PGARTDSTDT SSVPTDTSSV PTDTSSVSTD
TPSVSTGGKV PDDSGQTGGD GSGEIPVETK GSKRESEQGT ESEQEADSVG DSPDRCRSEH
RRDPSARELE IGNDMTGRST GTGEYDDFVR TFRDRYERLS KILRGRVNHR PATAIADMPG
GSDAAMIGLV NDVRSTKSGH WLIELEDTTG TFPALVMKNK GLADVVDEIL TDECIAVEGT
LADDAGILFV DSLHFPDVPH SRRPTLADRH VQAALISDVH VGSDEFMLEA WNRFTDWLHT
PEAAPVEYLL IAGDMVEGVG VYPNQDEELE IVDIYDQYEA FAEHLKDVPG DTEIVMIPGN
HDAVRLAEPQ PGFNDELRSI MDVHDARIVS NPATVSLEGV EILMYHGVSL DEVIAELPAE
KASYDEPEKA MCQLLKKRHV APQFGGRTRV APEERDYLVI ENVPDVFHAG HVHKLGWRKY
HNVLAVNSGC WQAQTDFQKS VNIDPDAGFA PILDLDTLEM TVRQFSRG
//
