A Ubasawa, F Okibayashi, C S Jone, M Ikehara, D G George, A Tsugita
{"title":"A variant database.","authors":"A Ubasawa, F Okibayashi, C S Jone, M Ikehara, D G George, A Tsugita","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Variant biomacromolecules, either natural or artificially created, are proving to be useful in determining structure-function relationships. Research in this field would be facilitated by the compilation of data of variants into a central and widely available repository. The Variant Database acts as a repository for data concerning variant molecules. It complements the Biological Activity and the Physicochemical Property Databases as well as provides variant sequences.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 6","pages":"341-7"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12974204","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":"Index of the protein sequences added in 1990 to the Protein Sequence Database of the International Association of Protein Sequence Databanks. Volume 4, Numbers 3-5, 1991.","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 3-5","pages":"127-316"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12944128","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":"Methanog: a specialized database on methanogenic bacteria.","authors":"A R Thakur, C Ramu, P K Parrack, S Mukhopadhyay","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A specialized, interdisciplinary database on various types of related information on methanogenic bacteria is described. Derived from other sequence databases etc., this database collects information from many sources, including unpublished work from research laboratories working in this field, and makes them accessible from a single source, to interested scientists, free of cost. It is presently held in eight 48 T.P.I. floppy disks and can be run on any IBM PC under DOS 3.0 or above, making this database of particular interest to researchers with limited resources and on-line search/access facilities.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 6","pages":"363-6"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12974133","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}
C S Jone, A Tsugita, K Satake, F Okibayashi, K Imai, T Yagi, K Takahashi, L S Yeh
{"title":"Non-sequence databases for biological activity and physicochemical properties.","authors":"C S Jone, A Tsugita, K Satake, F Okibayashi, K Imai, T Yagi, K Takahashi, L S Yeh","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A biological activity database and a physicochemical property database are described. They are intended to complement the protein sequence database of PIR-International. The Biological Activity Database and the Physicochemical Property Database contain information regarding the biological activity and the physicochemical properties of proteins, respectively. In addition they also provide information about wild-type molecules with which information concerning variant molecules may be compared. Data on artificial variant molecules are stored in the Artificial Variant Database which is described separately.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 6","pages":"367-74"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12974134","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":"Distinction by sequence analysis between cdc2 protein kinases involved in cell cycle control and closely related proteins.","authors":"M A Guerrucci, P Goujon, R Bellé","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Cdc2 proteins are well characterized as protein kinases and are functionally involved in the control of the G2 to M transition during cell division. cdc2 proteins (cdc2Sp, CDC28 and CDC2Gg) and proteins sharing a high degree of similarity with cdc2 proteins (EG1 and DM2C), and therefore belonging to the same structural family, were analyzed using Fourier transform of the coded sequences. Characteristic code/frequency pairs (0.140, 0.148 and 0.238) distinguish the cdc2 proteins from the related proteins. The frequencies 0.140, 0.148 and 0.238 (and the associated codes) allow discrimination between all cdc2 proteins (cdc2Sp, CDC28, CDC2Gg, CDC2Hs, CDC2Mm, CDC2Dm, CDC2Ms) and related proteins (EG1, DM2C, MO15, GTA, PHO85, KSS1, PSKJ3, FUS3, KIN28), thus providing the first evidence for predicting cdc2 function from a sequence. A rice cdc2 homolog (R2) did not match the cdc2 proteins and is, therefore, unlikely to be a cdc2 protein. Pertinent patterns in the cdc2 proteins were searched, and mapped to the 90-210 region (numbering from cdc2 of S. pombe) which correlates well with the putative cyclin binding domain of the cdc2 proteins.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 6","pages":"337-40"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12974203","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":"Amino acid sequence of 10-kDa protein in photosystem I reaction-center complex from a thermophilic cyanobacterium, Synechococcus elongatus Naegeli.","authors":"N Kotani, A Tsugita, K Kondo, K Aso, I Enami","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Four small subunits (14, 13, 10, and 8 kDa) of the photosystem I reaction-center complex were isolated from a thermophilic cyanobacterium Synechococcus elongatus. The complete amino acid sequence of the 10-kDa subunit was determined to consist of 80 amino acid residues giving a molecular mass of 8855.3, excluding iron and sulfur atoms, and containing two special sequences of cysteine residues, Cys-X-X-Cys-X-X-Cys-X-X-X-Cys-Pro, at residues 10-21 and 47-58, which indicates that the subunit is an apoprotein carrying two iron-sulfur centers, FA and FB, assigned as [4Fe-4S] clusters. The amino acid sequence indicated an 87.5% identity compared with those deduced from the nucleotide sequences of chloroplast gene psa C from several plants.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 2","pages":"93-6"},"PeriodicalIF":0.0,"publicationDate":"1991-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13104915","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":"Sequence analysis of firefly luciferase family reveals a conservative sequence motif.","authors":"H Toh","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A conservative sequence motif was extracted from an alignment of the firefly luciferase family. AngR derived from a pathogenic bacterium and acetyl-CoA synthetases derived from two ascomycete fungi were identified as members of the firefly luciferase family by a homology search with the motif and other sequence comparison analyses. The motif sequence shares several characteristics with the phosphate-binding sites of phosphoproteins and nucleotide-binding proteins. A multiple alignment and an unrooted phylogenetic tree were constructed for the investigation of evolutionary relationships within the firefly luciferase family.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 2","pages":"111-7"},"PeriodicalIF":0.0,"publicationDate":"1991-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13105015","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":"The amino acid sequence of the beta chain of hemerythrin from Lingula unguis.","authors":"H Yano, K Satake, Y Ueno, A Tsugita","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The amino acid sequence of the beta chain of hemerythrin from Lingula unguis was determined. The sequence consists of 117 amino acid residues. The sequence shares 25 amino acid residues in common with other known hemerythrin sequences, including myohemerythrin, with which it shares an insertion of 5 amino acids. This is the first complete sequence from a heteropolymeric hemerythrin.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 2","pages":"87-91"},"PeriodicalIF":0.0,"publicationDate":"1991-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13104914","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":"Prediction of the site of signal peptidase cleavage in normal and variant human preproalbumin.","authors":"R J Peach, D R Boswell, S O Brennan","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>We describe the use of a template for the recognition site of signal peptidase to give score predictions for cleavage at normal and aberrant sites in human and chicken preproalbumin. As expected, the highest score obtained for human preproalbumin was at the normal cleavage site between -7 Ser and -6 Arg. The mutation in preproalbumin Kaikoura (-2 Arg----Cys) introduced an aberrant cleavage site in the propeptide between the new -2 Cys and -1 Arg. Although the new site had a lower template score (6.88) than the normal site (9.99), it is cleaved in vivo about five times faster. The presence of minor proportions of des-Asp and des-Asp-Ala-albumin in normal human plasma was not found to correlate with possible aberrant signal peptidase cleavage. These truncated albumin species, therefore, appear to be generated through cleavage of mature albumin in circulation. Chicken preproalbumin had only one probably signal peptidase cleavage site, the one utilised in vivo. Template scores should be regarded as qualitative predictions rather than definitive quantitative indicators.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 2","pages":"123-6"},"PeriodicalIF":0.0,"publicationDate":"1991-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13104909","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":"Complete amino acid sequence of equine miniplasminogen.","authors":"J Schaller, C Straub, U Kämpfer, E E Rickli","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The complete amino acid sequence of equine miniplasminogen (Mr 37,132, 338 residues) was determined with the aid of fragments obtained by cleavage with 2-(2-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine, cyanogen bromide or clostripain. The fragments were aligned with overlapping sequences. Sequence comparison with other species gave identities in the range of 76% (bovine) and 81% (canine), indicating the presence of the same structural and functional domains as in the other species. Sequence comparison of different miniplasminogens showed that positions 49 (Arg), 83 (Arg) and 161 (Ser) may play a role in the interaction between plasminogen and streptokinase.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 2","pages":"69-74"},"PeriodicalIF":0.0,"publicationDate":"1991-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13104911","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}