Summary: Scytalone dehydratase
Scytalone dehydratase Provide feedback
Scytalone dehydratases are structurally related to the NTF2 family (see PF02136).
Nakasako M, Motoyama T, Kurahashi Y, Yamaguchi I; , Biochemistry 1998;37:9931-9939.: Cryogenic X-ray crystal structure analysis for the complex of scytalone dehydratase of a rice blast fungus and its tight-binding inhibitor, carpropamid: the structural basis of tight-binding inhibition. PUBMED:9665698 EPMC:9665698
Internal database links
|Similarity to PfamA using HHSearch:||SnoaL_4|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR004235
Scytalone dehydratase is a member of the group of enzymes involved in fungal melanin biosynthesis. It was first identified in a phytopathogenic fungus, Magnaporthe grisea (Rice blast fungus), which causes rice blast disease. Scytalone dehydratase is a molecular target of inhibitor design efforts aimed at protecting rice plants from fungal disease [PUBMED:9922139, PUBMED:14716498].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||scytalone dehydratase activity (GO:0030411)|
|Biological process||melanin metabolic process (GO:0006582)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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This superfamily contains a variety of enzymes such as Scytalone dehydratase, Delta-5-3-ketosteroid isomerase, Limonene-1,2-epoxide hydrolase among others. The family also includes presumed non-enzymatic homologues such as NTF2.
The clan contains the following 38 members:CaMKII_AD DUF1348 DUF2358 DUF3225 DUF3804 DUF3828 DUF3887 DUF4348 DUF4440 DUF4467 DUF4518 DUF4783 DUF4829 DUF4864 DUF4878 DUF4904 DUF5104 DUF5105 Endopep_inhib LEH Lumazine_bd_2 MBA1 MecA_N MlaC Mtr2 NTF2 PHZA_PHZB Ring_hydroxyl_B Scytalone_dh SnoaL SnoaL_2 SnoaL_3 SnoaL_4 T4BSS_DotI_IcmL Tim44 TpcC VirB8 WI12
We make a range of alignments for each Pfam-A family:
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- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the UniProtKB sequence database using the family HMM
- alignment generated by searching the NCBI sequence database using the family HMM
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Curation and family details
|Seed source:||Structural domain|
|Number in seed:||3|
|Number in full:||292|
|Average length of the domain:||153.50 aa|
|Average identity of full alignment:||45 %|
|Average coverage of the sequence by the domain:||80.74 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Scytalone_dh domain has been found. There are 20 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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