{"title":"Tomato and Aspergillus niger pectinesterases. Correlation of differences in existing reports: large species variations.","authors":"O Markovic, H Jörnvall","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Existing reports on the enzyme tomato pectinesterase differ in alignments of two internal segments and in many single-residue replacements. The alignment from cDNA data, with a 317-residue mature protein, is correct, but protein analyses also show at least 18 single-residue replacements, suggesting the presence of many native or (less likely) cloning-derived microheterogeneities. Purification of Aspergillus niger pectinesterase and N-terminal sequence analysis of this enzyme reveal a different structure and indicate an extensive protein divergence.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"3 6","pages":"513-5"},"PeriodicalIF":0.0,"publicationDate":"1990-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13244801","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Weak sequence homologies among chitinases detected by clustering analysis.","authors":"B Henrissat","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The amino acid sequences of various endo-N-acetyl-glucosaminidases (chitinases) have been subjected to hydrophobic cluster analysis. A domain of approximately 145 residues was found to be weakly conserved in chitinase A and B from the bacterium Serriata marcescens, in a chitinase from cucumber (Cucumis sativis) and in the endo-N-acetyl-glucosaminidase H of Streptomyces plicatus. A prediction of the putative active site region was made upon analysis of invariant acidic amino acids. On the basis of primary structure homologies, a classification into families of structurally related proteins is proposed for the enzymes hydrolyzing beta-1,4-N-acetyl-glucosamine linkages.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"3 6","pages":"523-6"},"PeriodicalIF":0.0,"publicationDate":"1990-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13244803","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Bair, D A Ferrick
{"title":"The following protein sequences were reprinted from the Protein Sequence Database of the Protein Identification Resource (PIR).","authors":"W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Bair, D A Ferrick","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"3 6","pages":"527-636"},"PeriodicalIF":0.0,"publicationDate":"1990-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13244804","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Bair, D A Ferrick
{"title":"The following protein sequences were reprinted from the protein sequence database of the Protein Identification Resource (PIR).","authors":"W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Bair, D A Ferrick","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"3 5","pages":"407-512"},"PeriodicalIF":0.0,"publicationDate":"1990-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13411664","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"NRL-3D: a sequence-structure database derived from the protein data bank (PDB) and searchable within the PIR environment.","authors":"N Pattabiraman, K Namboodiri, A Lowrey, B P Gaber","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The protein identification resource (PIR) and the Brookhaven National Laboratory protein data bank (PDB) are well-known databases for primary sequences and three-dimensional structures of proteins, respectively. Lesk et al, have compared the primary sequences in these two databases and concluded that the sequences in them are not redundant. Moreover, PIR programs can not be used directly on PDB files to access primary sequences because the FORMATS of these two data bases are different. We have developed a sequence-structure database, called NRL-3D, from the sequences, chain identification and the residue numbers of proteins in the PDB. This new database is designed such that it can be used in conjunction with PIR programs to search and extract sequences of interest and the corresponding three-dimensional coordinates from the structures in PDB.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"3 5","pages":"387-405"},"PeriodicalIF":0.0,"publicationDate":"1990-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13411663","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Deduced amino acid sequence of heme binding region of chicken cholesterol side chain cleavage cytochrome P450.","authors":"P A Mathew, N Kagawa, C R Bhasker, M R Waterman","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The primary structure of the carboxy terminal 296 amino acids of chicken cholesterol side chain cleavage cytochrome P450 (P450scc) was deduced from a partial cDNA clone isolated from a chicken ovarian cDNA library. The sequence contained putative steroid binding and heme binding regions. Comparison of this sequence with the corresponding sequences of three mammalian forms of P450scc shows greater than 50% homology. The heme binding region of the avian P450scc shows 76% homology with the heme binding regions of rat and human P450scc and 81% homology with that of bovine P450scc.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"3 4","pages":"323-5"},"PeriodicalIF":0.0,"publicationDate":"1990-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13389929","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Reorganization and merging of the EMBL and GenBank keyword indexes in a tree structure for more efficient retrieval of nucleic acid sequences.","authors":"A Tullo, S Liuni, M Attimonelli","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>EMBL and GenBank keyword indexes have no hierarchical structure. In this paper we present a method for merging and reorganizing them in a tree structure whose primary roots are the keywords 'protein', 'DNA', 'RNA', and 'unclassified'. Synonymous keywords have been grouped together and erroneous keywords have been corrected. This taxonomic organization of keywords results in a more extensive and efficient retrieval which is further aided by \"synonyms declaration\". The tree has been produced using the computer programs GENPOINT and CREANET.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"3 4","pages":"327-34"},"PeriodicalIF":0.0,"publicationDate":"1990-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13389930","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Species comparison of calmodulin sequences.","authors":"F Friedberg","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>No amino acid substitutions can be located when the calmodulin produced in various vertebrate species (human, rat, chicken, toad) are compared. However, multiple substitutions exist in calmodulin derived from non-vertebrates. Here, we have determined the residues for which no alterations in sequence are allowed. The protein from each species exhibits a sequence identity from residue 27 to residue 53, i.e., residues spanning a small part of the Ca2+ binding loop I and the adjacent interloop region. The analogous sequence (residues 100 to 129) abutting the Ca2+ binding loop III also exhibits only a few differences. Furthermore, negatively charged side chains at residues 82-84 in the central alpha-helix are conserved.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"3 4","pages":"335-7"},"PeriodicalIF":0.0,"publicationDate":"1990-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13389931","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Bair, D A Ferrick
{"title":"The following protein sequences were reprinted from the protein sequence database of the Protein Identification Resource (PIR).","authors":"W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Bair, D A Ferrick","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"3 4","pages":"339-85"},"PeriodicalIF":0.0,"publicationDate":"1990-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13389932","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
T P King, D Moran, D F Wang, L Kochoumian, B T Chait
{"title":"Structural studies of a hornet venom allergen antigen 5, Dol m V and its sequence similarity with other proteins.","authors":"T P King, D Moran, D F Wang, L Kochoumian, B T Chait","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The primary structures and the disulfide-bond pairings of two chromatographic forms A and B of a venom protein from white-faced hornet (Dolichovespula maculata) were determined. This protein, designated as antigen 5 (Dol m V), has 204-205 amino acid residues and it contains 4 disulfide bonds. This protein is an allergen in man but its biologic function in hornet is not yet known. Dol m V is found to have partial sequence similarity with pathogenesis-related proteins from tobacco and tomato leaves and with a sperm-coating protein from rat epididymis.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"3 3","pages":"263-6"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13551772","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}