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0  structures 346  species 0  interactions 3195  sequences 445  architectures

Family: PLAC (PF08686)

Summary: PLAC (protease and lacunin) domain

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The Pfam group coordinates the annotation of Pfam families in Wikipedia, but we have not yet assigned a Wikipedia article to this family. If you think that a particular Wikipedia article provides good annotation, please let us know.

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.

PLAC (protease and lacunin) domain Provide feedback

The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin [1].

Literature references

  1. Nardi JB, Martos R, Walden KK, Lampe DJ, Robertson HM; , Insect Biochem Mol Biol. 1999;29:883-897.: Expression of lacunin, a large multidomain extracellular matrix protein, accompanies morphogenesis of epithelial monolayers in Manduca sexta. PUBMED:10528409 EPMC:10528409


This tab holds annotation information from the InterPro database.

InterPro entry IPR010909

The PLAC (protease and lacunin) domain is a six-cysteine region of about 40 residues that is present at or near the C-terminal of various enzymes and matrix proteins, including: mammalian PACE4 (paired basic amino acid cleaving enzyme 4), mammalian PCSK5 (proprotein convertase subtilisin/kexin type 5), mammalian metalloproteinases ADAMTS-2, -3, -10, -12, -14, -16, -17, and -19, and manduca Sexta matrix protein lacunin [ PUBMED:11867212 ]. The PLAC domain is often associated with other domains, such as the thrombospondin type I repeat (TSP1) ( INTERPRO ), the Kunitz proteinase inhibitor domain ( INTERPRO ), the Ig-like domain ( INTERPRO ), the WAP domain ( INTERPRO ), the subtilase domain ( INTERPRO ), or the ADAM-type metalloprotease domain ( INTERPRO ).

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
(88)
Full
(3195)
Representative proteomes UniProt
(5201)
RP15
(343)
RP35
(1008)
RP55
(2725)
RP75
(3746)
Jalview View  View  View  View  View  View  View 
HTML View  View           
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
(88)
Full
(3195)
Representative proteomes UniProt
(5201)
RP15
(343)
RP35
(1008)
RP55
(2725)
RP75
(3746)
Alignment:
Format:
Order:
Sequence:
Gaps:
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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
(88)
Full
(3195)
Representative proteomes UniProt
(5201)
RP15
(343)
RP35
(1008)
RP55
(2725)
RP75
(3746)
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: Rawlings ND
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Mistry J , Rawlings ND
Number in seed: 88
Number in full: 3195
Average length of the domain: 32.30 aa
Average identity of full alignment: 41 %
Average coverage of the sequence by the domain: 2.98 %

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 26.4 26.4
Trusted cut-off 26.6 26.5
Noise cut-off 26.3 26.3
Model length: 31
Family (HMM) version: 13
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
A0A0G2K229 View 3D Structure Click here
A0A0G2KZR4 View 3D Structure Click here
A0A2R8QMQ5 View 3D Structure Click here
B0S6F1 View 3D Structure Click here
D3Z1A5 View 3D Structure Click here
D3Z8G4 View 3D Structure Click here
D3ZD40 View 3D Structure Click here
D3ZLL7 View 3D Structure Click here
D4A065 View 3D Structure Click here
D4A4X6 View 3D Structure Click here
E7FBX1 View 3D Structure Click here
E7FCQ4 View 3D Structure Click here
E7FE04 View 3D Structure Click here
E7FEJ5 View 3D Structure Click here
E7FFX0 View 3D Structure Click here
E7FFY5 View 3D Structure Click here
F1R027 View 3D Structure Click here
F6XJP7 View 3D Structure Click here
G3UXC7 View 3D Structure Click here
O76840 View 3D Structure Click here
O95428 View 3D Structure Click here
P29122 View 3D Structure Click here
P58459 View 3D Structure Click here
P82987 View 3D Structure Click here
Q3UTY6 View 3D Structure Click here
Q4FZU4 View 3D Structure Click here
Q4VC17 View 3D Structure Click here
Q63415 View 3D Structure Click here
Q69Z28 View 3D Structure Click here
Q6UY14 View 3D Structure Click here
Q6ZMP0 View 3D Structure Click here
Q7TSK7 View 3D Structure Click here
Q80T21 View 3D Structure Click here
Q86TH1 View 3D Structure Click here
Q8BLI0 View 3D Structure Click here
Q8N6G6 View 3D Structure Click here
Q8TE57 View 3D Structure Click here
Q8TE60 View 3D Structure Click here
Q9EPX2 View 3D Structure Click here
Q9H324 View 3D Structure Click here
Q9UKP5 View 3D Structure Click here
Q9VKV3 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;