| The pacifastin inhibitor family web site [Introduction] [Sequences] [Alignments] [Structures] [Phylogenetics] [References] Created and maintained by Zoltán Gáspári E-mail: szpari@para.chem.elte.hu Last modified: 10.02.2004 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Sequences Nomenclature Nomenclature of the sequences follows the rules described in Simonet et. al., (2002), i.e. 'Genus species pacifastin-related inhibitor n' or Genus species pacifastin-related domain n', according to whether the polypeptide is processed into individual monomers or not. Experimental evidence shows that the locust (Locusta migratoria and Schistocerca gregaria) inhibitors are processed, whereas the pacifastin light chain, containing 9 inhibitory domains, remains intact. In all other cases, we assumed that the polypeptide chains are not processed. But! see also the reasoning about processing in Simonet, G., Claeys, I., Franssens, V., De Loof, A., Vanden Broeck, J. (2003) Genomics, evolution and biological functions of the pacifastin peptide family: a conserved serine protease inhibitor family in arthropods. Peptides 24, 1633-1644. Module organization a) mrcliaicfivlarhcesgalkcspgtegpcaaeqeskdkpsqittddasavqemqs[BMPD1]ifte[BMPD2]stpkk feliq[BMPD3]iiep[BMPD4]ntpekseliq[BMPD5]inep[BMPD6]ntpkkseliq[BMPD7]idep[BMPD8]n nfgsgvtekletkgteipelrssqnttk[BMPD9]lpedgdedpenlnpkpat[BMPD10]eeknhtlsrkvrasqqetvkt b) mkallilvmtvaahgasleqpdptpasdlpd[PLD1]ykaaqg[PLD2]lakgmfasqte[PLD3]ingiglan[PLD4]v qspsvpavafrsggrtgkcrpdahddslpd[PLD5]epkpg[PLD6]pdgslpd[PLD7]ykpqpg[PLD8][PLD9]pt c) mnvavsvlalllvavgcsa[LMPI6]rr[LMPI7]rr[LMPI8]kr[LMPI9] d) mrafvglvvtlivaasaahasestdvewvfvdklsg[OSPD1]kpraaidknvpvvydwtf[OSPD2]vvfgyvq[OSPD3]g esvnavdhpvdsvhvvdqppssvhvvdhpvdsvhvvdhpsdsvqvadlprsavqvddsnipv?dgyiqgnqmssfsfhryl e) yskpggtimkilmlivatcvvg*alc[AGPD1]elsddsqvrldvqngeslssadekdeihvqtn[A*GPD2]akrsep ap[AGPD3]gffdqqklkqkrsvpaddlpqsaiapgap[AGPD4]ewExamples on the module organization of proteins with PLD-like domains. (a) Proposed module organization of a Bombyx mori protein containing pacifastin light chain domains based on EST data. The overlapping region of the ESTs used (accession numbers AU003615, AU005858, AU003467) is underlined. The highly similar module pairs BMPD3-BMPD4, BMPD5-BMPD6 and BMPD7-BMPD8 are separated by segments showing clear relationship. (b) Module organization of the pacifastin light chain (c) Modules on the Locusta migratoria PP3 gene (accession AJ419778) separated by dibasic cleavage sites. (d) PLD-like modules on the Oryza sativa EST CA766257 (e) Modules in the Anopheles gambiae genomic sequence. The position of introns is indicated by asterisk (*). The first intron (phase 1) is located before the first module, the second one (phase 0) interrupts the second PLD-like domain after the first conserved cysteine. Gene structure Only one sequence corresponding to a genomic region of the malaria mosquito Anpheles gambiae was found with similarity to pacifastin-related inhibitors (accession AAAB01008816). The predicted encoded protein corresponds to multiple ESTs (e.g. accession BM586029, BM605854). There are two introns interrupting the coding sequence, the first one (phase 1) before the first PLD-like domain while the second (phase 0) lies in the second module after the first conserved cysteine. Sequence files Sequence entries are available both as local files and as links to the NCBI GenBank entries. (From the very similar Anopheles clones, only the representative ones are presently listed.)
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