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0DPOLL_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePOLL
DescriptionDna polymerase lambda (ec 2.7.7.7) (ec 4.2.99.-) (pol lambda) (dna polymerase kappa) (dna polymerase beta-2) (pol beta2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (NAS)
0003677 DNA binding (NAS)
0016449 lambda DNA polymerase activity (NAS)
0006260 DNA replication (NAS)
0006289 nucleotide-excision repair (IDA)
0016446 somatic hypermutation of antibody genes (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The HhH motif is an around 20 amino acids domain present in prokaryotic andeukaryotic non-sequence-specific DNA binding proteins . The HhH motif is similar to.ut distinct from.he HtH motif. Both of thesemotifs have two helices connected by a short turn. In the HtH motif the secondhelix binds to DNA with the helix in the major groove. This allow the contactbetween specific base and residues throughout the protein. In the HhH motifthe second helix does not protrude from the surface of the protein andtherefore cannot lie in the major groove of the DNA. Crystallographic studiessuggest that the interaction of the HhH domain with DNA is mediated by aminoacids located in the strongly conserved loop (L-P-G-V) and at the N-terminalend of the second helix . This interaction could involve the formation ofhydrogen bonds between protein backbone nitrogens and DNA phosphate groups. The structural difference between the HtH and HhH domains is reflected at thefunctional level: whereas the HtH domain.ound primarily in gene regulatoryproteins.inds DNA in a sequence specific manner.he HhH domain is ratherfound in proteins involved in enzymatic activities and binds DNA with nosequence specificity .
  IPR003583:Helix-hairpin-helix DNA-binding, class 1
DNA carries the biological information that instructs cells how to existin an ordered fashion: accurate replication is thus one of the mostimportant events in the cell life cycle. This function is mediated byDNA-directed DNA-polymerases.hich add nucleotide triphosphate (dNTP)residues to the 5-end of the growing DNA chain.sing a complementary DNA as template. Small RNA molecules are generally used as primers forchain elongation.lthough terminal proteins may also be used. Three motifs.. and C.s defined by Delarue et al. .re seen to be conserved across all DNA-polymerases.ith motifs A and C also seen in RNA- polymerases. They are centered on invariant residues.nd their structural significance was implied from the Klenow (Escherichia coli) structure: motif A contains a strictly-conserved aspartate at the junction of a beta-strand and an alpha-helix; motif B contains an alpha-helix with positive charges; and motif C has a doublet of negative charges.ocated in a beta-turn-beta secondary structure .DNA polymerases () can be classified.n the basis of sequencesimilarity into at least four different groups: A.. and X. Members of family X are small (about 40 kDa) compared with other polymerases and encompass two distinct polymerase enzymes that have similar functionality: vertebrate polymerase beta (same as yeast pol 4).nd terminal deoxynucleotidyl-transferase (TdT) (). The former functions in DNA repair.hilethe latter terminally adds single nucleotides to polydeoxynucleotide chains.Both enzymes catalyse addition of nucleotides in a distributive manner..e. theydissociate from the template-primer after addition of each nucleotide.DNA-polymerases show a degree of structural similarity with RNA-polymerases.
  IPR002008:DNA-directed DNA polymerase X, beta-like
DNA carries the biological information that instructs cells how to existin an ordered fashion: accurate replication is thus one of the mostimportant events in the cell life cycle. This function is mediated byDNA-directed DNA-polymerases.hich add nucleotide triphosphate (dNTP)residues to the 5-end of the growing DNA chain.sing a complementary DNA as template. Small RNA molecules are generally used as primers forchain elongation.lthough terminal proteins may also be used. Three motifs.. and C.s defined by Delarue et al. .re seen to be conserved across all DNA-polymerases.ith motifs A and C also seen in RNA- polymerases. They are centered on invariant residues.nd their structural significance was implied from the Klenow (Escherichia coli) structure: motif A contains a strictly-conserved aspartate at the junction of a beta-strand and an alpha-helix; motif B contains an alpha-helix with positive charges; and motif C has a doublet of negative charges.ocated in a beta-turn-beta secondary structure .DNA polymerases () can be classified.n the basis of sequencesimilarity into at least four different groups: A.. and X. Members of family X are small (about 40 kDa) compared with other polymerases and encompass two distinct polymerase enzymes that have similar functionality: vertebrate polymerase beta (same as yeast pol 4).nd terminal deoxynucleotidyl-transferase (TdT) (). The former functions in DNA repair.hilethe latter terminally adds single nucleotides to polydeoxynucleotide chains.Both enzymes catalyse addition of nucleotides in a distributive manner..e. theydissociate from the template-primer after addition of each nucleotide.DNA-polymerases show a degree of structural similarity with RNA-polymerases.
  IPR002054:DNA polymerase X
Mammalian DNA polymerase beta (polB. is a 39-kDa protein with both nucleotidyltransferase and 5-deoxyribose phosphodiesterase activities.laying a role in both excision repair and meiosis. polB has a modular organisation with an 8-kDa N-terminal domain (NTD) connected to the 31-kDa C-terminal domain by a protease-hypersensitive hinge region. The NTD acts as a single-stranded DNA binding domain.nteracting most efficiently with the 5-phosphate of the downstream primer of the gapped DNA. This interaction is mediated by a helix-hairpin-helix motif (HhH).hich is also found in several other DNA repair enzymes. The residue threonine 79 (T79).hich is located within the NTD.as identified as being critical to polB function.ven though it makes no contact with either DNA template or dNTP substrate; T79 is located between two HhH motifs.nd acts as a hinge residue that is important for positioning the DNA within the active site .The catalytic core (residues 148-242) of murine terminal deoxynucleotidyl transferase (TdT. displays a structural fold that is similar to polB.nd shares a common two-metal ion mechanism of nucleotidyl transfer with polB . TdT elongates DNA strands in a template-independent manner.nd belongs to the pol X family of polymerases. TdT has only been found in vertebrates.here it is highly conserved. TdT brings additional diversity in the immune repertoire by adding nucleotides.alled N regions.o the V(D)J recombination junction sites of immunoglobulin and T-cell receptor genes.
  IPR010996:DNA polymerase beta, N-terminal-like
IPR002054:POLXc 
Evalue:-85.3187587626244 
Location:251-574IPR001357:BRCT 
Evalue:0 
Location:36-132
SequencesProtein: DPOLL_HUMAN (575 aa)
mRNA: NM_013274
Local Annotation
Synapse Ontology
the generation of action potential at soma of neurons.
sdb:0313 generation of AP at soma  (Evidence:keywords)
KO assignmentK03512
  Level 3 annotation:
    DNA polymerase lambda subunit
  Level 2 annotation:
    DNA polymerase
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 312 residues, 103328630-103329564Exon2: 58 residues, 103329994-103330163Exon3: 45 residues, 103332509-103332638Exon4: 60 residues, 103333254-103333428Exon5: 108 residues, 103334348-103334666Exon6: 56 residues, 103335062-103335225Exon7: 100 residues, 103335608-103335903Exon8: 55 residues, 103336992-103337153Exon9: 112 residues, 103337631-103337963Exon10: 2 residues, -Jump to DPOLL_HUMAN  
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