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PMP inhibitors superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   Small proteins [ 56992] (90)
Fold:   PMP inhibitors [ 57282]
Superfamily:   PMP inhibitors [ 57283]
Families:   PMP inhibitors [ 57284] (4)

Superfamily statistics
Genomes (56) Uniprot 2018_03 genome PDB chains (SCOP 1.75)
Domains 255 1,058 6
Proteins 163 441 6

Functional annotation
General category Processes_IC
Detailed category Proteases

Function annotation of SCOP domain superfamilies

InterPro annotation
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 [PubMed14705960].

They were first isolated from Locusta migratoria (migratory locust). These were HI, LMCI-1 (PMP-D2) and LMCI-2 (PMP-C) [PubMed1472051, PubMed1740125, PubMed10696590]; five additional members SGPI-1 to 5 were identified in Schistocerca gregaria (desert locust) [PubMed9475173, PubMed11856311], and a heterodimeric serine protease inhibitor (pacifastin) was isolated from the hemolymph of Pacifastacus leniusculus (crayfish) [PubMed9192625].

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 [PubMed9192625]. 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 [PubMed9192625].

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 [PubMed11997226]. Expression analysis shows that the genes encoding the SGPI precursors are differentially expressed in a time-, stage- and hormone-dependent manner.

InterPro database

PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation ]

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 · Internal database links ]