(data stored in SCRATCH3701 zone)

SWISSPROT: D5E8N2_METMS

ID   D5E8N2_METMS            Unreviewed;       486 AA.
AC   D5E8N2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 50.
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=Mmah_0003 {ECO:0000313|EMBL:ADE35541.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35541.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35541.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) 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|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; Evidence={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:11130,
CC         Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:83828; EC=2.7.7.7; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00325};
CC   -!- SUBUNIT: Heterodimer of a large subunit and a small subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_00325}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase delta/II small subunit
CC       family. {ECO:0000256|HAMAP-Rule:MF_00325}.
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DR   EMBL; CP001994; ADE35541.1; -; Genomic_DNA.
DR   RefSeq; WP_013036484.1; NC_014002.1.
DR   EnsemblBacteria; ADE35541; ADE35541; Mmah_0003.
DR   GeneID; 8982134; -.
DR   KEGG; mmh:Mmah_0003; -.
DR   eggNOG; arCOG04455; Archaea.
DR   eggNOG; COG1311; LUCA.
DR   HOGENOM; HOG000226289; -.
DR   KO; K02323; -.
DR   OMA; YHGRSFD; -.
DR   OrthoDB; 24499at2157; -.
DR   BioCyc; MMAH547558:G1GHT-3-MONOMER; -.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
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:0008852; F:exodeoxyribonuclease I activity; IEA:UniProtKB-EC.
DR   GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-UniRule.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR011149; Pol2_small_arc.
DR   PANTHER; PTHR10416; PTHR10416; 1.
DR   Pfam; PF04042; DNA_pol_E_B; 1.
DR   PIRSF; PIRSF000803; Arc_Pol2_small; 2.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E8N2.
DR   SWISS-2DPAGE; D5E8N2.
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00325};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00325};
KW   DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_00325,
KW   ECO:0000313|EMBL:ADE35541.1};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_00325};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00325};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00325};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00325};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00325,
KW   ECO:0000313|EMBL:ADE35541.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00325, ECO:0000313|EMBL:ADE35541.1}.
FT   DOMAIN          297..432
FT                   /note="DNA_pol_E_B"
FT                   /evidence="ECO:0000259|Pfam:PF04042"
SQ   SEQUENCE   486 AA;  54484 MW;  C8146219E55E777C CRC64;
     MQEMSFLSDL LEAGYQVSPQ AAELITSHNN PRALINHILG SVDDSVFVID VDDIDFTGFE
     EVKDVEVPCK QEPVANTTSA NPISVLCDIT DCSTCVGEYM EFVQYFRNRY SRLSEMIRGR
     VNARPMESLK GNRRVPGDEI SIIGMVSEIK NTSNGHRLVR FEDPTGSFQV LFSMNDKDIY
     EQSNKLVLDD VVGVSGNLTN DGKLLIAKKL VFPDLPNMGL SKNGSQGKAL FISDVHIGSN
     TFLQGQWDDF MTFVKRESDN PELNKLAQQL RYIVVAGDIV DGVGIYPGQE EELTIPDIYD
     QYEEVAHYFN QIPSDITVVI GPGNHDAVRQ AEPQPTFPER IRKMFDPRIK FVGNPALVDL
     DGVLVLMYHG RSIDDFVSSI QGISYSEPEK AMLEMVKRRH LSPTYGSRVS IAPEKTDHFV
     IDHIPDILHC GHVHTVGVKQ YRGTLLINSG TWQDQTEFQK RVNVVPEPAR VPVVDLATFQ
     PTMLQF
//

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