ID E3GWQ4_METFV Unreviewed; 470 AA.
AC E3GWQ4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=Mfer_1187 {ECO:0000313|EMBL:ADP77973.1};
OS Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanothermaceae; Methanothermus.
OX NCBI_TaxID=523846 {ECO:0000313|EMBL:ADP77973.1, ECO:0000313|Proteomes:UP000002315};
RN [1] {ECO:0000313|EMBL:ADP77973.1, ECO:0000313|Proteomes:UP000002315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S
RC {ECO:0000313|Proteomes:UP000002315};
RX PubMed=21304736;
RA Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S.,
RA Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M.,
RA Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Methanothermus fervidus type strain (V24S).";
RL Stand. Genomic Sci. 3:315-324(2010).
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; CP002278; ADP77973.1; -; Genomic_DNA.
DR RefSeq; WP_013414251.1; NC_014658.1.
DR AlphaFoldDB; E3GWQ4; -.
DR STRING; 523846.Mfer_1187; -.
DR GeneID; 9962934; -.
DR KEGG; mfv:Mfer_1187; -.
DR HOGENOM; CLU_027850_1_0_2; -.
DR OrthoDB; 372039at2157; -.
DR Proteomes; UP000002315; 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
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 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|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:UP000002315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00325}.
FT DOMAIN 130..186
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
FT DOMAIN 214..411
FT /note="DNA polymerase alpha/delta/epsilon subunit B"
FT /evidence="ECO:0000259|Pfam:PF04042"
SQ SEQUENCE 470 AA; 53155 MW; 902142B8F70938C9 CRC64;
MGSNLLEELS KNDILITPEA YEKLKDLDNS DKEIISKLKD YVERNLEFPL ITNEIVEEVF
IEKKPQVPKI KIKKKRSKLE IIKNIESLNS DGDIKNLLNY FHNRYEKLRG LLEKRLGKIV
DIKDIGDNEV KIAGIVNEVR TTKKNHKIIE LEDKTGKCIV FVNKDGDLFK KTENIVQDEV
IGVIGKKNGR FVTASEIIQP GIPRIEEKNS NCTILFLSDL HIGSSKFLEN SFEKLISWIN
EGGNIAGEIE YIIIAGDIVD GVGIYPGQEK ELAIKDIEGQ YEEAARLLGE IRKDIKIIIA
PGNHDASRIA EPQQPLEKEY AKALYDLPNA EFVSNPSIIC IDGLKIMIYH GRSFDDMAIS
ANFSHDKPAE IMAELLEKRH LAPIYGLRTP IAPEPEDHLV IDTIPDIFHA GHVHINDYKK
YKGIHLINSG TFQEQTEFQK IHNIRPTPGQ VPVLHNSKIK VLSVEKLPAT
//
