Please note: Superfamily is currently under maintenance and some functionality may be limited. Please bear with us as we fix these problems.
PMP inhibitors superfamily
|General category ||Processes_IC|
|Detailed category ||Proteases|
Document: Function annotation of SCOP domain superfamilies
UniProtKB KeyWords (KW)(show details)
Highlighted in gray are those with FDR_all>0.001
Document: KW annotation of SCOP domains
|Cross references ||IPR008037 SSF57283 Protein matches|
This family of serine protease inhibitors belong to MEROPS inhibitor family I19, clan IW. They inhibit chymotrpsin, a peptidase belong to the S1 family .
They were first isolated from Locusta migratoria (migratory locust). These were HI, LMCI-1 (PMP-D2) and LMCI-2 (PMP-C) [1472051, 1740125, 10696590]; five additional members SGPI-1 to 5 were identified in Schistocerca gregaria (desert locust) [9475173, 11856311], and a heterodimeric serine protease inhibitor (pacifastin) was isolated from the hemolymph of Pacifastacus leniusculus (crayfish) .
Pacifastin is a 155-kDa composed of two covalently linked subunits, which are separately encoded. The heavy chain of pacifastin (105 kDa) is related to transferrins, containing three transferrin lobes, two of which seem to
be active for iron binding . A number of the members of the transferrin family are also serine peptidases belong to MEROPS peptidase family S60 . The light chain of pacifastin (44 kDa) is the proteinase inhibitory subunit, and has nine cysteine-rich inhibitory domains that are homologous to each other. The locust inhibitors share a conserved array of six cysteine residues with the pacifastin light chain. The structure of members of this family reveal that they are comprised of a triple-stranded antiparallel beta-sheet connected by three disulphide bridges .
The biological function(s) of the locust inhibitors is (are) not fully understood. LMCI-1 and LMCI-2 were shown to inhibit the endogenous proteolytic activating cascade of prophenoloxidase . Expression analysis shows that the genes encoding the SGPI precursors are differentially expressed in a time-, stage- and hormone-dependent manner.
PDBeMotif information about ligands, sequence and structure motifs
Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · UniProtKB KeyWords (KW) ]
Internal database links
Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry
out SCOP domain assignments to all genomes at the superfamily level.
Alignments of sequences to 6 models
in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical
are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.
Browse and view proteins in genomes which have
different domain combinations including a PMP inhibitors domain.
Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.
Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.
There are 6 hidden Markov models representing the PMP inhibitors superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.
Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · UniProtKB KeyWords (KW) · Internal database links ]