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9  structures 96  species 1  interaction 678  sequences 20  architectures

Family: GBP_C (PF02841)

Summary: Guanylate-binding protein, C-terminal domain

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This is the Wikipedia entry entitled "Guanylate-binding protein". More...

Guanylate-binding protein Edit Wikipedia article

Guanylate-binding protein, N-terminal domain
PDB 1dg3 EBI.jpg
structure of human guanylate binding protein-1 in nucleotide free form
Identifiers
Symbol GBP
Pfam PF02263
Pfam clan CL0023
InterPro IPR015894
SCOP 1dg3
SUPERFAMILY 1dg3
Guanylate-binding protein, C-terminal domain
PDB 1dg3 EBI.jpg
structure of human guanylate binding protein-1 in nucleotide free form
Identifiers
Symbol GBP_C
Pfam PF02841
InterPro IPR003191
SCOP 1dg3
SUPERFAMILY 1dg3

In molecular biology, the guanylate-binding protein family is a family of GTPases that is induced by interferon (IFN)-gamma. GTPases induced by IFN-gamma (Interferon-inducible GTPase) are key to the protective immunity against microbial and viral pathogens. These GTPases are classified into three groups: the small 47-KD immunity-related GTPases (IRGs), the Mx proteins (MX1, MX2), and the large 65- to 67-kd GTPases. Guanylate-binding proteins (GBP) fall into the last class. In humans, there are seven GBPs (hGBP1-7).[1] Structurally, hGBP1 consists of two domains: a compact globular N-terminal domain harbouring the GTPase function, and an alpha-helical finger-like C-terminal domain.[2] Human GBP1 is secreted from cells without the need of a leader peptide, and has been shown to exhibit antiviral activity against Vesicular stomatitis virus and Encephalomyocarditis virus, as well as being able to regulate the inhibition of proliferation and invasion of endothelial cells in response to IFN-gamma.[3]

References[edit]

  1. ^ Tripal P, Bauer M, Naschberger E, Mortinger T, Hohenadl C, Cornali E, Thurau M, Sturzl M (January 2007). "Unique features of different members of the human guanylate-binding protein family". J. Interferon Cytokine Res. 27 (1): 44–52. doi:10.1089/jir.2007.0086. PMID 17266443. 
  2. ^ Prakash B, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C. Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. Nature. 2000 Feb 3;403(6769):567-71. http://www.nature.com/nature/journal/v403/n6769/full/403567a0.html
  3. ^ Naschberger E, Lubeseder-Martellato C, Meyer N, Gessner R, Kremmer E, Gessner A, Sturzl M (September 2006). "Human guanylate binding protein-1 is a secreted GTPase present in increased concentrations in the cerebrospinal fluid of patients with bacterial meningitis". Am. J. Pathol. 169 (3): 1088–99. doi:10.2353/ajpath.2006.060244. PMC 1698817. PMID 16936281. 

This article incorporates text from the public domain Pfam and InterPro IPR003191

This article incorporates text from the public domain Pfam and InterPro IPR015894

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.

Guanylate-binding protein, C-terminal domain Provide feedback

Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.

Literature references

  1. Prakash B, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C; , Nature 2000;403:567-571.: Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. PUBMED:10676968 EPMC:10676968


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003191

Guanylate-binding protein is a GTPase that is induced by interferon (IFN)-gamma. GTPases induced by IFN-gamma are key to the protective immunity against microbial and viral pathogens. These GTPases are classified into three groups: the small 47-kd GTPases, the Mx proteins, and the large 65- to 67-kd GTPases. Guanylate-binding proteins (GBP) fall into the last class. In humans, there are seven GBPs (hGBP1-7) [PUBMED:17266443]. Structurally, hGBP1 consists of two domains: a compact globular N-terminal domain harbouring the GTPase function (INTERPRO), and an alpha-helical finger-like C-terminal domain. Human GBP1 is secreted from cells without the need of a leader peptide, and has been shown to exhibit antiviral activity against Vesicular stomatitis virus and Encephalomyocarditis virus, as well as being able to regulate the inhibition of proliferation and invasion of endothelial cells in response to IFN-gamma [PUBMED:16936281].

Gene Ontology

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Domain organisation

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Alignments

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(23)
Full
(678)
Representative proteomes NCBI
(663)
Meta
(7)
RP15
(107)
RP35
(154)
RP55
(219)
RP75
(366)
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  Seed
(23)
Full
(678)
Representative proteomes NCBI
(663)
Meta
(7)
RP15
(107)
RP35
(154)
RP55
(219)
RP75
(366)
Alignment:
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Sequence:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(23)
Full
(678)
Representative proteomes NCBI
(663)
Meta
(7)
RP15
(107)
RP35
(154)
RP55
(219)
RP75
(366)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

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

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 HMMER3.

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Trees

This page displays the phylogenetic tree for this family's seed alignment. 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 alignment.

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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_4308 (release 5.2)
Previous IDs: none
Type: Domain
Author: Bateman A, Mian N, Griffiths-Jones SR
Number in seed: 23
Number in full: 678
Average length of the domain: 220.50 aa
Average identity of full alignment: 29 %
Average coverage of the sequence by the domain: 37.66 %

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 24.3 24.3
Trusted cut-off 24.3 24.3
Noise cut-off 24.2 24.2
Model length: 297
Family (HMM) version: 9
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

GBP

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 GBP_C domain has been found. There are 9 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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