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0  structures 584  species 0  interactions 4141  sequences 197  architectures

Family: zf-Di19 (PF05605)

Summary: Drought induced 19 protein (Di19), zinc-binding

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Drought induced 19 protein (Di19), zinc-binding Provide feedback

This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought [1]. This domain is a zinc-binding domain.

Literature references

  1. Gosti F, Bertauche N, Vartanian N, Giraudat J; , Mol Gen Genet 1995;246:10-18.: Abscisic acid-dependent and -independent regulation of gene expression by progressive drought in Arabidopsis thaliana. PUBMED:7823904 EPMC:7823904


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR008598

This zinc-binding domain is found in plant drought induced 19 (Di19) proteins, animal E3 ubiquitin-protein ligases (RNF114/KCMF1/RNF138/RNF125) and transcriptional repressors (ZEB1/ZEB2). Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought [ PUBMED:7823904 ]. KCMF1 and RNF114 are E3 ubiquitin-protein ligases [ PUBMED:15581609 , PUBMED:23645206 ], while ZEB1 represses transcription by binding to the E box (5'-CANNTG-3') [ PUBMED:19935649 ].

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

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(42)
Full
(4141)
Representative proteomes UniProt
(6718)
RP15
(500)
RP35
(1654)
RP55
(3395)
RP75
(4657)
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PP/heatmap 1 View           

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(42)
Full
(4141)
Representative proteomes UniProt
(6718)
RP15
(500)
RP35
(1654)
RP55
(3395)
RP75
(4657)
Alignment:
Format:
Order:
Sequence:
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Download options

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
(42)
Full
(4141)
Representative proteomes UniProt
(6718)
RP15
(500)
RP35
(1654)
RP55
(3395)
RP75
(4657)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped 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.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

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.

Note: You can also download the data file for the tree.

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_8581 (release 8.0)
Previous IDs: Di19;
Type: Domain
Sequence Ontology: SO:0000417
Author: Moxon SJ
Number in seed: 42
Number in full: 4141
Average length of the domain: 56.70 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 11.52 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.5 27.5
Trusted cut-off 27.5 27.5
Noise cut-off 27.4 27.4
Model length: 54
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

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Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0G2JX46 View 3D Structure Click here
A0A0G2JXY7 View 3D Structure Click here
A0A0R0EGG7 View 3D Structure Click here
A0A0R0FNZ3 View 3D Structure Click here
A0A0R0KH28 View 3D Structure Click here
A0A1D6FLX3 View 3D Structure Click here
A0A1D6H7M4 View 3D Structure Click here
A0A1D6IW21 View 3D Structure Click here
A0A1D6MRV2 View 3D Structure Click here
A0A286Y942 View 3D Structure Click here
A0A286YB49 View 3D Structure Click here
B4FDK3 View 3D Structure Click here
B4FJS2 View 3D Structure Click here
B7FA64 View 3D Structure Click here
C0P4W3 View 3D Structure Click here
C0PC01 View 3D Structure Click here
C4JAZ0 View 3D Structure Click here
C6SY55 View 3D Structure Click here
C6T0D8 View 3D Structure Click here
C6T3G5 View 3D Structure Click here
E7FEA4 View 3D Structure Click here
E9PTC3 View 3D Structure Click here
F1QPM7 View 3D Structure Click here
F1R6J7 View 3D Structure Click here
I1JQP5 View 3D Structure Click here
I1K047 View 3D Structure Click here
I1KCA9 View 3D Structure Click here
I1KLP2 View 3D Structure Click here
I1LB68 View 3D Structure Click here
I1M073 View 3D Structure Click here
I1MUI9 View 3D Structure Click here
K7N2R2 View 3D Structure Click here
O04259 View 3D Structure Click here
O60315 View 3D Structure Click here
P34664 View 3D Structure Click here
P37275 View 3D Structure Click here
Q39083 View 3D Structure Click here
Q3U9F6 View 3D Structure Click here
Q54WQ0 View 3D Structure Click here
Q5JME8 View 3D Structure Click here
Q5QMP3 View 3D Structure Click here
Q5W794 View 3D Structure Click here
Q62947 View 3D Structure Click here
Q64318 View 3D Structure Click here
Q688X9 View 3D Structure Click here
Q6H6E6 View 3D Structure Click here
Q6J0N1 View 3D Structure Click here
Q6J1I7 View 3D Structure Click here
Q6J2U6 View 3D Structure Click here
Q6NM26 View 3D Structure Click here
Q75JS0 View 3D Structure Click here
Q7KT86 View 3D Structure Click here
Q7T321 View 3D Structure Click here
Q7XBA5 View 3D Structure Click here
Q80UY2 View 3D Structure Click here
Q84J70 View 3D Structure Click here
Q8GWK1 View 3D Structure Click here
Q8VXU6 View 3D Structure Click here
Q8VZ42 View 3D Structure Click here
Q8WVD3 View 3D Structure Click here
Q95RX5 View 3D Structure Click here
Q96A37 View 3D Structure Click here
Q96EQ8 View 3D Structure Click here
Q9CQE0 View 3D Structure Click here
Q9D9M9 View 3D Structure Click here
Q9D9R0 View 3D Structure Click here
Q9ET26 View 3D Structure Click here
Q9FJ17 View 3D Structure Click here
Q9P0J7 View 3D Structure Click here
Q9R0G7 View 3D Structure Click here
Q9VJT3 View 3D Structure Click here
Q9W4V2 View 3D Structure Click here
Q9Y508 View 3D Structure Click here

trRosetta Structure

The structural model below was generated by the Baker group with the trRosetta software using the Pfam UniProt multiple sequence alignment.

The InterPro website shows the contact map for the Pfam SEED alignment. Hovering or clicking on a contact position will highlight its connection to other residues in the alignment, as well as on the 3D structure.

Improved protein structure prediction using predicted inter-residue orientations. Jianyi Yang, Ivan Anishchenko, Hahnbeom Park, Zhenling Peng, Sergey Ovchinnikov, David Baker Proceedings of the National Academy of Sciences Jan 2020, 117 (3) 1496-1503; DOI: 10.1073/pnas.1914677117;