0  structures 727  species 0  interactions 3421  sequences 52  architectures

Family: zf-C4_Topoisom (PF01396)

Summary

Topoisomerase DNA binding C4 zinc finger Add an annotation

No Pfam abstract.


Literature references

  1. Tse-Dinh YC, Beran-Steed RK; , J Biol Chem 1988;263:15857-15859.: Escherichia coli DNA topoisomerase I is a zinc metalloprotein with three repetitive zinc-binding domains. PUBMED:2846526

  2. Ahumada A, Tse-Dinh YC; , Biochem Biophys Res Commun 1998;251:509-514.: The Zn(II) binding motifs of E. coli DNA topoisomerase I is part of a high-affinity DNA binding domain. PUBMED:9792804


InterPro entry IPR013498

DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single- or double-strand breaks, crossing the strands through one another, then resealing the breaks. These enzymes have several functions: to remove DNA supercoils during transcription and DNA replication; for strand breakage during recombination; for chromosome condensation; and to disentangle intertwined DNA during mitosis PUBMED:12042765, PUBMED:11395412. DNA topoisomerases are divided into two classes: type I enzymes (; topoisomerases I, III and V) break single-strand DNA, and type II enzymes (; topoisomerases II, IV and VI) break double-strand DNA PUBMED:12596227.

Type I topoisomerases are ATP-independent enzymes (except for reverse gyrase), and can be subdivided according to their structure and reaction mechanisms: type IA (bacterial and archaeal topoisomerase I, topoisomerase III and reverse gyrase) and type IB (eukaryotic topoisomerase I and topoisomerase V). These enzymes are primarily responsible for relaxing positively and/or negatively supercoiled DNA, except for reverse gyrase, which can introduce positive supercoils into DNA.

This entry represents the zinc-finger domain found in type IA topoisomerases, including bacterial and archaeal topoisomerase I and III enzymes, and in eukaryotic topoisomerase III enzymes. Escherichia coli topoisomerase I proteins contain five copies of a zinc-ribbon-like domain at their C-terminus, two of which have lost their cysteine residues and are therefore probably not able to bind zinc PUBMED:10873443. This domain is still considered to be a member of the zinc-ribbon superfamily despite not being able to bind zinc.

More information about this protein can be found at Protein of the Month: DNA Topoisomerase PUBMED:.

Clan

This family is a member of clan Zn_Beta_Ribbon (CL0167), which contains the following 30 members:

A2L_zn_ribbon Auto_anti-p27 Baculo_LEF5_C CxxC_CxxC_SSSS DNA_RNApol_7kD DUF1407 DUF1610 DUF1936 DUF2387 Elf1 GATA Ogr_Delta PhnA_Zn_Ribbon Prim_Zn_Ribbon Ribosomal_S27 Ribosomal_S27e RNA_POL_M_15KD RRN7 Spt4 TF_Zn_Ribbon TFIIS_C Topo_Zn_Ribbon Transposase_35 Trm112p UPF0547 zf-C4_Topoisom zf-CHC2 zf-dskA_traR zf-GRF zf-NADH-PPase

Gene Ontology

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External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...

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Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.

Pfam alignments:
Full length sequences

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.

Pfam alignments:

HMM logo

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Trees

This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.

Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_1854 (release 3.0)
Previous IDs: none
Type: Family
Author: Bateman A
Number in seed: 27
Number in full: 3421
Average length of the domain: 39.50 aa
Average identity of full alignment: 34 %
Average coverage of the sequence by the domain: 6.35 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.5 20.5
Trusted cut-off 20.5 20.5
Noise cut-off 20.4 20.4
Model length: 39
Family (HMM) version: 12
Download: download the raw HMM for this family

Species distribution

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