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3  structures 812  species 0  interactions 2605  sequences 39  architectures

Family: KilA-N (PF04383)

Summary: KilA-N domain

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This is the Wikipedia entry entitled "KilA-N domain". More...

KilA-N domain Edit Wikipedia article

KilA-N
PDB 1mb1 EBI.jpg
mbp1 from saccharomyces cerevisiae
Identifiers
Symbol KilA-N
Pfam PF04383
InterPro IPR018004
SCOP 1bm8
SUPERFAMILY 1bm8

In molecular biology, the KilA-N domain is a conserved protein domain.

It is a novel conserved DNA-binding domain is found at the N-terminus of the poxvirus D6R/NIR proteins. It is also found in a wide range of proteins of large bacterial and eukaryotic DNA viruses.[1] Putative proteins with homology to the KilA-N domain have also been identified in Maverick transposable elements of the parabasalid protozoa Trichomonas vaginalis.[2] The KilA-N domain has been suggested to be homologous to the fungal DNA-binding APSES domain. In all proteins shown to contain the KilA-N domain, it occurs at the extreme amino terminus accompanied by a wide range of distinct carboxy-terminal domains. These carboxy-terminal modules may be enzymes, such as the nuclease domains, or might mediate additional, specific interactions with nucleic acids or proteins, like the RING or CCCH fingers in the poxviruses.[1] The KilA-N domain is predicted to adopt an alpha-beta fold with four conserved strands and at least two conserved helices.[1] Some proteins known to contain a KilA-N domain are listed below:

  • Trichomonas vaginalis G3 Putative uncharacterised protein

[edit] References

  1. ^ a b c Iyer LM, Koonin EV, Aravind L (2002). "Extensive domain shuffling in transcription regulators of DNA viruses and implications for the origin of fungal APSES transcription factors". Genome Biol. 3 (3): RESEARCH0012. PMC 88810. PMID 11897024. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=88810. 
  2. ^ Pritham EJ, Putliwala T, Feschotte C (April 2007). "Mavericks, a novel class of giant transposable elements widespread in eukaryotes and related to DNA viruses". Gene 390 (1-2): 3–17. doi:10.1016/j.gene.2006.08.008. PMID 17034960. 

This article incorporates text from the public domain Pfam and InterPro IPR018004

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

KilA-N domain Provide feedback

The amino-terminal module of the D6R/N1R proteins defines a novel, conserved DNA-binding domain (the KilA-N domain) that is found in a wide range of proteins of large bacterial and eukaryotic DNA viruses. The KilA-N domain family also includes the previously defined APSES domain. The KilA-N and APSES domains may also share a common fold with the nucleic acid-binding modules of the LAGLIDADG nucleases and the amino-terminal domains of the tRNA endonuclease [1].

Literature references

  1. Iyer LM, Koonin EV, Aravind L; , Genome Biol 2002;3:RESEARCH0012.: Extensive domain shuffling in transcription regulators of DNA viruses and implications for the origin of fungal APSES transcription factors. PUBMED:11897024 EPMC:11897024

  2. Taylor IA, Treiber MK, Olivi L, Smerdon SJ; , J Mol Biol 1997;272:1-8.: The X-ray structure of the DNA-binding domain from the Saccharomyces cerevisiae cell-cycle transcription factor Mbp1 at 2.1 A resolution. PUBMED:9299332 EPMC:9299332


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR018004

The amino-terminal module of the poxvirus D6R/NIR proteins defines a novel conserved DNA-binding domain (the KilA-N domain) that is found in a wide range of proteins of large bacterial and eukaryotic DNA viruses [PUBMED:11897024]. Putative proteins with homology to the KilA-N domain have also been identified in Maverick transposable elements of the parabasalid protozoa Trichomonas vaginalis [PUBMED:17034960]. The KilA-N domain has been suggested to be homologous to the fungal DNA-binding APSES domain (see PROSITEDOC). In all proteins shown to contain the KilA-N domain, it occurs at the extreme amino terminus accompanied by a wide range of distinct carboxy-terminal domains. These carboxy-terminal modules may be enzymes, such as the nuclease domains, or might mediate additional, specific interactions with nucleic acids or proteins, like the RING (see PROSITEDOC) or CCCH fingers in the poxviruses [PUBMED:11897024]. The KilA-N domain is predicted to adopt an alpha-beta fold with four conserved strands and at least two conserved helices [PUBMED:11897024]. Some proteins known to contain a KilA-N domain are listed below:

Domain organisation

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  Seed
(139)
Full
(2605)
Representative proteomes NCBI
(2312)
Meta
(29)
RP15
(1330)
RP35
(1420)
RP55
(1504)
RP75
(1531)
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  Seed
(139)
Full
(2605)
Representative proteomes NCBI
(2312)
Meta
(29)
RP15
(1330)
RP35
(1420)
RP55
(1504)
RP75
(1531)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Seed source: Iyer LM
Previous IDs: none
Type: Domain
Author: Aravind L, Iyer LM, Bateman A
Number in seed: 139
Number in full: 2605
Average length of the domain: 103.00 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 37.07 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.0 19.7
Trusted cut-off 21.0 19.7
Noise cut-off 20.9 19.6
Model length: 111
Family (HMM) version: 8
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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the KilA-N domain has been found. There are 3 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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