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Database: UniProt
Entry: G0QD75_NANSJ
LinkDB: G0QD75_NANSJ
Original site: G0QD75_NANSJ 
ID   G0QD75_NANSJ            Unreviewed;       515 AA.
AC   G0QD75;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=J07AB56_09510 {ECO:0000313|EMBL:EGQ40223.1};
OS   Nanosalinarum sp. (strain J07AB56).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Nanohaloarchaea;
OC   Nanosalinarum.
OX   NCBI_TaxID=889962 {ECO:0000313|EMBL:EGQ40223.1, ECO:0000313|Proteomes:UP000009382};
RN   [1] {ECO:0000313|EMBL:EGQ40223.1, ECO:0000313|Proteomes:UP000009382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Narasingarao P., Podell S., Ugalde J.A., Brochier-Armanet C., Emerson J.B.,
RA   Brocks J.J., Heidelberg K.B., Banfield J.F., Allen E.E.;
RT   "De novo metagenomic assembly reveals abundant novel major lineage of
RT   Archaea in hypersaline microbial communities.";
RL   ISME J. 0:0-0(2011).
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; GL982569; EGQ40223.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0QD75; -.
DR   HOGENOM; CLU_027850_1_0_2; -.
DR   Proteomes; UP000009382; 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   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:UP000009382};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00325}.
FT   DOMAIN          257..459
FT                   /note="DNA polymerase alpha/delta/epsilon subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF04042"
FT   REGION          63..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   515 AA;  58348 MW;  47052C3E54DB7162 CRC64;
     MNREALRQLT EIGINVAPEA AQRLEENDIE RIQRLDTDPM YLSGPMLDRL REAVDLPSEV
     EVESKDQVVV QSQSDGQQNA GGAKQETHTD SDSARNVGGG IELEDSGRRN SLETKVEILD
     DHEITKKEKD VPEFLEYYND RYDRMKEMLT RRKELQSATT LNRLSRRDEG EQAAAIGLVS
     DKYSTNSGRY IVELQDKTGS FKVLVDGDEG DRLVPDEVIG VTGSMGDDIV FANQVVHPDL
     PIPDGVNTTQ QEVQAAYISD LHIGSQDTMH DALDRFGDWL RSDEASNIGY LVIAGDIVEG
     VGVYPGQEEE LEITDVYRQY RRFEEWAEKL PDRIELIIGP GNHDVVRLAE PQPTLPEKAF
     DNIHTWDNVH LVQNPQTVRL HGIRSQGIKH LMYHGMSYDD HVSRIKELRE NAYDQPEYVM
     EDLLKRRHVA PSYGSNPLSP EGTDAMVIEH EPDVFVSGHF HSHCDESYKG VNMICSSSFQ
     SQTDYQKRVG HQPQPGIVTI MDFETRKTTT KKFKQ
//
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