| Nucleic Acids Research |
Pages 215-219 |
|
The PROSITE database, its status in 1999
Background
Leading Concepts
Format And Document Files
Content Of The Current Release
How To Obtain A Local Copy Of Prosite
By CD-ROM
By anonymous FTP
By Email through the EBI network fileserver
How To Make Use Of Prosite
Computer programs
Email servers
Interactive access to PROSITE using the World Wide Web
References
The PROSITE database, its status in 1999
The PROSITE database, its status in 1999
Kay Hofmann, Philipp Bucher1,*, Laurent Falquet1 and Amos Bairoch2
MEMOREC, Stoffel GmbH, Stoeckheimer Weg 1, D-50829 Koeln, Germany, 1Swiss Institute of Bioinformatics (SIB), Swiss Institute for Experimental Cancer Research (ISREC), CH-1066 Epalinges/Lausanne, Switzerland and 2Swiss Institute of Bioinformatics (SIB), Department of Medical Biochemistry, University of Geneva, 1 rue Michel Servet, CH-1211 Geneva 4, Switzerland
Received October 16, 1998; Accepted October 21, 1998
ABSTRACT
The PROSITE database (http://www.expasy.ch/sprot/prosite.html ) consists of biologically significant patterns and profiles formulated in such a way that with appropriate computational tools it can help to determine to which known family of protein (if any) a new sequence belongs, or which known domain(s) it contains.
PROSITE (1,2) is a method of identifying what is the function of uncharacterized proteins translated from genomic or cDNA sequences. It consists of a database of biologically significant patterns and profiles formulated in such a way that with appropriate computational tools it can rapidly and reliably determine to which known family of protein (if any) the new sequence belongs, or which known domain(s) it contains.
In some cases the sequence of an unknown protein is too distantly related to any protein of known structure to detect its resemblance by overall sequence alignment. However, relationships can be revealed by the occurrence in its sequence of a particular cluster of residue types, which is variously known as a pattern, motif, signature or fingerprint. These motifs arise because specific region(s) of a protein which may be important, for example, for their binding properties or for their enzymatic activity are conserved in both structure and sequence. These structural requirements impose very tight constraints on the evolution of this small but important portion(s) of a protein sequence. The use of protein sequence patterns or profiles to determine the function of proteins is becoming very rapidly one of the essential tools of sequence analysis. Many authors (3,4) have recognized this reality. Based on these observations, we decided in 1988, to actively pursue the development of a database of regular expression-like patterns, which would be used to search against sequences of unknown function.
But, while sequence patterns are very useful, there are a number of protein families as well as functional or structural domains that cannot be detected using patterns due to their extreme sequence divergence. Typical examples of important functional domains, which are weakly conserved, are the globins, the immunoglobulin, and the SH2 and SH3 domains. In such domains there are only a few sequence positions which are well conserved. Any attempt to build a consensus pattern for such regions will either fail to pick up a significant proportion of the protein sequences that contain such a region (false negatives) or will pick up too many proteins that do not contain the region (false positives).
The use of techniques based on profiles or weight matrices (the two terms are used synonymously here) allows the detection of such proteins or domains. A profile is a table of position-specific amino acid weights and gap costs. These numbers (also referred to as scores) are used to calculate a similarity score for any alignment between a profile and a sequence, or parts of a profile and a sequence. An alignment with a similarity score higher than or equal to a given cut-off value constitutes a motif occurrence. As with patterns, there may be several matches to a profile in one sequence, but multiple occurrences in the same sequences must be disjoint (non-overlapping) according to a specific definition included in the profile. Another feature that distinguishes patterns from profiles is that the latter are usually not confined to small regions with high sequence similarity. Rather they attempt to characterize a protein family or domain over its entire length.
We therefore started in 1994 to complement the approach based on patterns by gradually adding to PROSITE profile entries. The profile structure (5,6) used in PROSITE is similar to but slightly more general than the one introduced by Gribskov and co-workers (7); additional parameters allow representation of other motif descriptors, including the currently popular hidden Markov models (8). Profiles can be constructed by a large variety of different techniques. The classical method developed by Gribskov and co-workers (9) requires a multiple sequence alignment as input and uses a symbol comparison table to convert residue frequency distributions into weights. Most profiles included in PROSITE are generated by this procedure applying recently described modifications (10,11). In some cases we also applied alternative profile construction methods including structure-based approaches and methods involving hidden Markov modelling.
The design of PROSITE follows five leading concepts.
Completeness. For such a compilation to be helpful in the determination of protein function, it is important that it contains as many biologically meaningful patterns and profiles as possible.High specificity. In the majority of cases we have chosen patterns or profiles that are specific enough that they do not detect too many unrelated sequences, yet they will detect most, if not all, sequences that clearly belong to the set in consideration.Documentation. Each of the entries in PROSITE is fully documented; the documentation includes a concise description of the protein family or domain that it is designed to detect as well as a summary of the reasons leading to the development of the pattern or profile.Periodic reviewing. It is important that each entry be periodically reviewed to ensure that it is still valid.A very tight relationship with the SWISS-PROT protein sequence data bank (12). Updating of PROSITE and of the annotations of the relevant SWISS-PROT entries are very often done in parallel. Software tools based on PROSITE are used to automatically update the feature table lines of SWISS-PROT entries relevant to the presence and extent of specific domains.
Figure 1. Sample data from PROSITE.
The core of the PROSITE database is composed of two ASCII (text) files. The first file (PROSITE.DAT) is a computer-readable file that contains all the information necessary for programs that make use of PROSITE to scan sequence(s) for the occurrence of the patterns and/or profiles. This file also includes, for each entry described, statistics on the number of hits obtained while scanning for that pattern or profile in SWISS-PROT. Cross-references to the corresponding SWISS-PROT entries are also present in the file. The second file (PROSITE.DOC), which we call the textbook, contains textual information that documents each pattern.
A sample textbook entry is shown (Fig. 1a); this particular entry is linked to two entries in the PROSITE.DAT file: a pattern and a profile (Fig. 1b).
Several document files are also distributed with the database:
| PROSUSER.TXT |
|
The database user's manual |
| PROFILE.TXT |
|
A detailed description of the syntax for the profiles |
| PROSITE.LIS |
|
A list of PROSITE documentation entries |
| PROSITE.GET |
|
A document on how to obtain a local copy of PROSITE |
| PROSITE.PRG |
|
A description of programs and electronic mail servers that make use of PROSITE |
| PAUTINDX.TXT |
|
An index of authors cited in the PROSITE.DOC file |
Release 15.0 of PROSITE (July 1998) contains 1014 documentation entries describing 1352 different patterns, rules and profiles/matrices. In addition to these entries, a collection of 241 preliminary profiles is available in the pre-release distribution from the FTP server of the ISREC group (see below). The list of the documentation entries that have been added since the last release of PROSITE (14.0) is provided in Table 1, furthermore, many entries were updated. The database requires ~5 Mb of disk storage space. The present distribution frequency is two releases per year. No restrictions are placed on use or redistribution of the data. Future releases of PROSITE will be copyright (releases up to number 15.0 are not).
PROSITE is distributed on CD-ROM by the EMBL Outstation-the European Bioinformatics Institute (EBI) (13). For all enquiries regarding the subscription and distribution of PROSITE one should contact: The EMBL Outstation-The European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, UK. Tel: +44 1223 494 444; Fax: +44 1223 494 468; Email: datalib@ebi.ac.uk
Table 1.
List of patterns documentation entries that have been added since the last release of PROSITE (14.0)
| DNA repair protein radC family signature |
| recR protein signature |
| ubiH/COQ6 monooxygenase family signature |
| ATP phosphoribosyltransferase signature |
| Prolipoprotein diacylglyceryl transferase signature |
| Phosphatidate cytidylyltransferase signature |
| Lipoate-protein ligase B signature |
| moaA / nifB / pqqE family signature |
| BCCT family of transporters signature |
| Flagellar motor protein motA family signature |
| Protein secA signatures |
| ATP1G1 / PLM / MAT8 family signature |
| Protein smpB signature |
| Uncharacterized protein family UPF0044 signature |
| Uncharacterized protein family UPF0047 signature |
| Uncharacterized protein family UPF0054 signature |
| Uncharacterized protein family UPF0057 signature |
If you have access to a computer system linked to the Internet you can obtain PROSITE using FTP (File Transfer Protocol), from the following file servers:
ExPASy (Expert Protein Analysis System) server, Swiss Institute of Bioinformatics (SIB); Internet address: ftp://www.expasy.ch/databases/prosite/
ISREC (Swiss Institute for Experimental Cancer Research) anonymous FTP server, Swiss Institute of Bioinformatics (SIB); Internet address: ftp://ftp.isrec.isb-sib.ch/sib-isrec/profiles/
EBI (European Bioinformatics Institute) anonymous FTP server; Internet address: ftp://ftp.ebi.ac.uk/pub/databases/prosite/
The pre-release collection of profiles is only available from the ISREC FTP server.
PROSITE can be obtained from the EBI network fileserver. Detailed instructions on how to make the best use of this service, and in particular on how to obtain PROSITE, can be obtained by sending to the network address netserv{at}ebi.ac.uk the following message:
HELP
HELP PROSITE
Many academic groups and commercial companies have developed computer programs that make use of the pattern entries in PROSITE. The `PROSITE.PRG' file contains a full list of these programs, their operating system specificity, characteristics as well as information on how to obtain them.
Two software packages are distributed to make use of profile entries:
(i) pftools (version 2.1 in FORTRAN77) written by Philipp Bucher. pfscan loads a sequence from a file and scans it with all (or one) of PROSITE profiles; pfsearch loads a profile from a file and scans for it in a SWISS-PROT database file. These tools are available by anonymous FTP from the server: ftp://ftp.isrec.isb-sib.ch/sib-isrec/pftools . Several versions are available, as well as executables compiled for many unix platforms and for Windows 95/98.
(ii) PrfLib (version 1.0 in ANSI C) written by Nicolas Moeri. scan4prf loads a sequence from a file and scans it with all (or one) of PROSITE profiles; srch4prf loads a profile from a file and scans for it in a SWISS-PROT database file. These tools are available from the server: http://mamac29.epfl.ch/
There are many Email servers that are available to molecular biologists (14). This an example of a server taking advantage of the PROSITE database:
| Name: |
|
MOTIF E-Mail Server on GenomeNet |
| Organization: |
|
Supercomputer Laboratory, Kyoto Institute for Chemical Research, Japan |
| Description: |
|
Allows to rapidly compare a new protein sequence against all patterns stored in PROSITE as well as in the MotifDic library (15). |
| Server email address: |
|
motif{at}genome.ad.jp |
| Address to report problems: |
|
motif-manager{at}genome.ad.jp |
The most efficient and user-friendly way to browse interactively in PROSITE as well as to analyze a sequence for the occurrence of a pattern or a profile is to use the World-Wide Web (WWW) molecular biology server ExPASy (16). Using a WWW browser, one has access to all the hypertext documents stored on the ExPASy server (as well as many other WWW servers) and also can make use of many sequence analysis software tools.
The ExPASy server may be accessed through its URL which is: http://www.expasy.ch/ . You can directly access to the `top' page of the section of ExPASy that allows you to browse through the PROSITE documentation and data entries by opening the URL: http://www.expasy.ch/sprot/prosite.html
To use the PROSITE patterns and profiles, you can make use of the following software tools.
ScanProsite. Allows the user to either scan a protein sequence-from SWISS-PROT or provided by the user-for the occurrence of patterns stored in PROSITE or to scan the SWISS-PROT and/or TrEMBL database-including weekly releases-for the occurrence of a pattern that can originate from PROSITE or be provided by the user. The URL for ScanProsite is: http://www.expasy.ch/sprot/scnpsite.html
ProfileScan. Allows the user to scan a protein sequence-from SWISS-PROT or provided by the user-for the occurrence of profiles stored in PROSITE. The URL for ProfileScan is: http://www.isrec.isb-sib.ch/software/PFSCAN_form.htmlFrameProfileScan. Allows the user to scan a DNA sequence (translated on the fly into protein)-from EMBL or provided by the user-for the occurrence of profiles stored in PROSITE. The URL for FrameProfileScan is: http://www.isrec.isb-sib.ch/software/PFRAMESCAN_form.html
1. Bairoch,A. and Bucher,P. (1994) Nucleic Acids Res., 22, 3583-3589. MEDLINE Abstract
2. Bairoch,A., Bucher,P. and Hofmann,K. (1997) Nucleic Acids Res., 25, 217-221. MEDLINE Abstract
3. Doolittle,R.F. (1986) Of URFs and ORFs: A Primer On How To Analyze Derived Amino Acid Sequences. University Science Books, Mill Valley, California.
4. Lesk,A.M. (1988) In Lesk,A.M. (ed.), Computational Molecular Biology. Oxford University Press, Oxford, pp. 17-26.
5. Bucher,P. and Bairoch,A. (1994) In Altman,R., Brutlag,D., Karp,P., Lathrop,R. and Searls,D. (eds), ISMB-94; Proceedings Second International Conference on Intelligent Systems for Molecular Biology. AAAI Press, Menlo Park, pp. 53-61.
6. Bucher,P., Karplus,K., Moeri,N. and Hofmann,K. (1996) Comput. Chem., 20, 3-23. MEDLINE Abstract
7. Gribskov,M., McLachlan,A.D. and Eisenberg,D. (1987) Proc. Natl Acad. Sci. USA, 84, 4355-4358. MEDLINE Abstract
8. Eddy,S.R. (1996) Curr. Opin. Struct. Biol., 6, 361-365. MEDLINE Abstract
9. Gribskov,M., Luethy,R. and Eisenberg,D. (1990) Methods Enzymol., 183, 146-159. MEDLINE Abstract
10. Luethy,R., Xenarios,I. and Bucher,P. (1994) Protein Sci., 3, 139-146.
11. Thompson,J.D., Higgins,D.G. and Gibson,T.J. (1994) Comput. Applic. Biosci., 10, 19-29.
12. Bairoch,A. and Apweiler,R. (1998) Nucleic Acids Res., 26, 38-42. MEDLINE Abstract
13. Stoesser,G., Moseley,M.A., Sleep,J., McGowran,M., Garcia-Pastor,M. and Sterk,P. (1998) Nucleic Acids Res., 26, 8-15. MEDLINE Abstract
14. Henikoff,S. (1993) Trends Biochem. Sci., 18, 267-268. MEDLINE Abstract
15. Ogiwara,A., Uchiyama,I., Seto,Y. and Kanehisa,M. (1992) Protein Engng, 5, 479-488.
16. Appel,R.D., Bairoch,A. and Hochstrasser,D.F. (1994) Trends Biochem. Sci., 19, 258-260. MEDLINE Abstract
*To whom correspondence should be addressed. Tel: +41 21 692 5892; Fax: +41 21 652 6933; Email: philipp.bucher@isrec.unil.ch
This page is run by Oxford University Press, Great Clarendon Street, Oxford OX2 6DP, as part of the OUP Journals
Comments and feedback: www-admin{at}oup.co.uk
Last modification: 9 Dec 1998
Copyright©Oxford University Press, 1998.

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tbCPSF30 Depletion by RNA Interference Disrupts Polycistronic RNA Processing in Trypanosoma brucei
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July 11, 2003;
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[Abstract]
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U. Johnsen, T. Hansen, and P. Schonheit
Comparative Analysis of Pyruvate Kinases from the Hyperthermophilic Archaea Archaeoglobus fulgidus, Aeropyrum pernix, and Pyrobaculum aerophilum and the Hyperthermophilic Bacterium Thermotoga maritima: UNUSUAL REGULATORY PROPERTIES IN HYPERTHERMOPHILIC ARCHAEA
J. Biol. Chem.,
July 3, 2003;
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R. Nair and B. Rost
LOC3D: annotate sub-cellular localization for protein structures
Nucleic Acids Res.,
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J. L. Gardy, C. Spencer, K. Wang, M. Ester, G. E. Tusnady, I. Simon, S. Hua, K. deFays, C. Lambert, K. Nakai, et al.
PSORT-B: improving protein subcellular localization prediction for Gram-negative bacteria
Nucleic Acids Res.,
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J. McDermott and R. Samudrala
Bioverse: functional, structural and contextual annotation of proteins and proteomes
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N. Delgado, J. Xue, J.-J. Yu, C.-Y. Hung, and G. T. Cole
A Recombinant {beta}-1,3-Glucanosyltransferase Homolog of Coccidioides posadasii Protects Mice against Coccidioidomycosis
Infect. Immun.,
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E. M. Hrabak, C. W.M. Chan, M. Gribskov, J. F. Harper, J. H. Choi, N. Halford, J. Kudla, S. Luan, H. G. Nimmo, M. R. Sussman, et al.
The Arabidopsis CDPK-SnRK Superfamily of Protein Kinases
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O. Nufer, S. Mitrovic, and H.-P. Hauri
Profile-based Data Base Scanning for Animal L-type Lectins and Characterization of VIPL, a Novel VIP36-like Endoplasmic Reticulum Protein
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E. Schondorf, U. Bahr, M. Handermann, and G. Darai
Characterization of the Complete Genome of the Tupaia (Tree Shrew) Adenovirus
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K. M. Fenster, K. L. Parkin, and J. L. Steele
Intracellular Esterase from Lactobacillus casei LILA: Nucleotide Sequencing, Purification, and Characterization
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M. Okamoto, J. J. Vidmar, and A. D. M. Glass
Regulation of NRT1 and NRT2 Gene Families of Arabidopsis thaliana: Responses to Nitrate Provision
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J. A. Stein, H. T. Broihier, L. A. Moore, and R. Lehmann
Slow as Molasses is required for polarized membrane growth and germ cell migration in Drosophila
Development,
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K. Fukami-Kobayashi, Y. Tateno, and K. Nishikawa
Parallel Evolution of Ligand Specificity Between LacI/GalR Family Repressors and Periplasmic Sugar-Binding Proteins
Mol. Biol. Evol.,
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C. Lindermayr, J. Fliegmann, and J. Ebel
Deletion of a Single Amino Acid Residue from Different 4-Coumarate:CoA Ligases from Soybean Results in the Generation of New Substrate Specificities
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R. I. Brinkworth, R. A. Breinl, and B. Kobe
From the Cover: Structural basis and prediction of substrate specificity in protein serine/threonine kinases
PNAS,
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O. Sasson, A. Vaaknin, H. Fleischer, E. Portugaly, Y. Bilu, N. Linial, and M. Linial
ProtoNet: hierarchical classification of the protein space
Nucleic Acids Res.,
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H. Boutselakis, D. Dimitropoulos, J. Fillon, A. Golovin, K. Henrick, A. Hussain, J. Ionides, M. John, P. A. Keller, E. Krissinel, et al.
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H.F. Vischer and J. Bogerd
Cloning and Functional Characterization of a Gonadal Luteinizing Hormone Receptor Complementary DNA from the African Catfish (Clarias gariepinus)
Biol Reprod,
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F. Alpy, C. Wendling, M.-C. Rio, and C. Tomasetto
MENTHO, a MLN64 Homologue Devoid of the START Domain
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A. Herbik, C. Bolling, and T. J. Buckhout
The Involvement of a Multicopper Oxidase in Iron Uptake by the Green Algae Chlamydomonas reinhardtii
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T. Hansen, B. Reichstein, R. Schmid, and P. Schonheit
The First Archaeal ATP-Dependent Glucokinase, from the Hyperthermophilic Crenarchaeon Aeropyrum pernix, Represents a Monomeric, Extremely Thermophilic ROK Glucokinase with Broad Hexose Specificity
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A. Muller, R. M. MacCallum, and M. J.E. Sternberg
Structural Characterization of the Human Proteome
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I. B. Muller, D. Domenicali-Pfister, I. Roditi, and E. Vassella
Stage-specific Requirement of a Mitogen-activated Protein Kinase by Trypanosoma brucei
Mol. Biol. Cell,
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C. Huang, X. Zhang, Q. Lin, X. Xu, and ChoyL. Hew
Characterization of a novel envelope protein (VP281) of shrimp white spot syndrome virus by mass spectrometry
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G. Wengler and G. Wengler
In vitro analysis of factors involved in the disassembly of Sindbis virus cores by 60S ribosomal subunits identifies a possible role of low pH
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S. La Fontaine, J. M. Quinn, S. S. Nakamoto, M. D. Page, V. Gohre, J. L. Moseley, J. Kropat, and S. Merchant
Copper-Dependent Iron Assimilation Pathway in the Model Photosynthetic Eukaryote Chlamydomonas reinhardtii
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J. K. Cusick, E. Hager, and R. E. Gill
Characterization of bcsA Mutations That Bypass Two Distinct Signaling Requirements for Myxococcus xanthus Development
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I. Rigoutsos, T. Huynh, A. Floratos, L. Parida, and D. Platt
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J. W. Scott and M. E. Rasche
Purification, Overproduction, and Partial Characterization of {beta}-RFAP Synthase, a Key Enzyme in the Methanopterin Biosynthesis Pathway{dagger}
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Y. Nishino, D. Kobasa, S. A. Rubin, M. V. Pletnikov, and K. M. Carbone
Enhanced Neurovirulence of Borna Disease Virus Variants Associated with Nucleotide Changes in the Glycoprotein and L Polymerase Genes
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J. A. Thanassi, S. L. Hartman-Neumann, T. J. Dougherty, B. A. Dougherty, and M. J. Pucci
Identification of 113 conserved essential genes using a high-throughput gene disruption system in Streptococcus pneumoniae
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C.-Y. Hung, J.-J. Yu, K. R. Seshan, U. Reichard, and G. T. Cole
A Parasitic Phase-Specific Adhesin of Coccidioides immitis Contributes to the Virulence of This Respiratory Fungal Pathogen
Infect. Immun.,
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A. Persson, K. Jacobsson, L. Frykberg, K.-E. Johansson, and F. Poumarat
Variable Surface Protein Vmm of Mycoplasma mycoides subsp. mycoides Small Colony Type
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V. Aragon, O. Rossier, and N. P. Cianciotto
Legionella pneumophila genes that encode lipase and phospholipase C activities
Microbiology,
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K. G. Hamil, Q. Liu, P. Sivashanmugam, S. Yenugu, R. Soundararajan, G. Grossman, R. T. Richardson, Y.-L. Zhang, M. G. O'Rand, P. Petrusz, et al.
Cystatin 11: A New Member of the Cystatin Type 2 Family
Endocrinology,
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Z. Xuan, W. R. McCombie, and M. Q. Zhang
GFScan: A Gene Family Search Tool at Genomic DNA Level
Genome Res.,
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H. Li, T. J. Ryan, K. J. Chave, and P. Van Roey
Three-dimensional Structure of Human gamma -Glutamyl Hydrolase. A CLASS I GLUTAMINE AMIDOTRANSFERASE ADAPTED FOR A COMPLEX SUBSTRATE
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P. Bradley, P. S. Kim, and B. Berger
From the Cover: TRILOGY: Discovery of sequence-structure patterns across diverse proteins
PNAS,
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T. Shibuya and I. Rigoutsos
Dictionary-driven prokaryotic gene finding
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A. Hasona, S. W. York, L. P. Yomano, L. O. Ingram, and K. T. Shanmugam
Decreasing the Level of Ethyl Acetate in Ethanolic Fermentation Broths of Escherichia coli KO11 by Expression of Pseudomonas putida estZ Esterase
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C. Wanner and J. Soppa
Functional Role for a 2-Oxo Acid Dehydrogenase in the Halophilic Archaeon Haloferax volcanii
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K. Endo, K. Hosono, T. Beppu, and K. Ueda
A novel extracytoplasmic phenol oxidase of Streptomyces: its possible involvement in the onset of morphogenesis
Microbiology,
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S.-H. Cheng, M. R. Willmann, H.-C. Chen, and J. Sheen
Calcium Signaling through Protein Kinases. The Arabidopsis Calcium-Dependent Protein Kinase Gene Family
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N. Saydam, T. K. Adams, F. Steiner, W. Schaffner, and J. H. Freedman
Regulation of Metallothionein Transcription by the Metal-responsive Transcription Factor MTF-1. IDENTIFICATION OF SIGNAL TRANSDUCTION CASCADES THAT CONTROL METAL-INDUCIBLE TRANSCRIPTION
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T. Petnicki-Ocwieja, D. J. Schneider, V. C. Tam, S. T. Chancey, L. Shan, Y. Jamir, L. M. Schechter, M. D. Janes, C. R. Buell, X. Tang, et al.
Genomewide identification of proteins secreted by the Hrp type III protein secretion system of Pseudomonas syringae pv. tomato DC3000
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T. Morishita, Y. Tsutsui, H. Iwasaki, and H. Shinagawa
The Schizosaccharomyces pombe rad60 Gene Is Essential for Repairing Double-Strand DNA Breaks Spontaneously Occurring during Replication and Induced by DNA-Damaging Agents
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R. Guerranti, J. C. Aguiyi, S. Neri, R. Leoncini, R. Pagani, and E. Marinello
Proteins from Mucuna pruriens and Enzymes from Echis carinatus Venom. CHARACTERIZATION AND CROSS-REACTIONS
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K. M. Jones and R. Haselkorn
Newly Identified Cytochrome c Oxidase Operon in the Nitrogen-Fixing Cyanobacterium Anabaena sp. Strain PCC 7120 Specifically Induced in Heterocysts
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M. Christmann, M. T. Tomicic, and B. Kaina
Phosphorylation of mismatch repair proteins MSH2 and MSH6 affecting MutS{alpha} mismatch-binding activity
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A. Johner and B. Lanzrein
Characterization of two genes of the polydnavirus of Chelonus inanitus and their stage-specific expression in the host Spodoptera littoralis
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D. Kihara, Y. Zhang, H. Lu, A. Kolinski, and J. Skolnick
Ab initio protein structure prediction on a genomic scale: Application to the Mycoplasma genitalium genome
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S. A. Goff, D. Ricke, T.-H. Lan, G. Presting, R. Wang, M. Dunn, J. Glazebrook, A. Sessions, P. Oeller, H. Varma, et al.
A Draft Sequence of the Rice Genome (Oryza sativa L. ssp. japonica)
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G. E. Allison, D. Angeles, N. Tran-Dinh, and N. K. Verma
Complete Genomic Sequence of SfV, a Serotype-Converting Temperate Bacteriophage of Shigellaflexneri
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A. J. Enright, S. Van Dongen, and C. A. Ouzounis
An efficient algorithm for large-scale detection of protein families
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J. Schug, S. Diskin, J. Mazzarelli, B. P. Brunk, and C. J. Stoeckert Jr.
Predicting Gene Ontology Functions from ProDom and CDD Protein Domains
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S. Bird, T. Wang, J. Zou, C. Cunningham, and C. J. Secombes
The First Cytokine Sequence Within Cartilaginous Fish: IL-1{beta} in the Small Spotted Catshark (Scyliorhinus canicula)
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H. P. Su, K. Nakada-Tsukui, A.-C. Tosello-Trampont, Y. Li, G. Bu, P. M. Henson, and K. S. Ravichandran
Interaction of CED-6/GULP, an Adapter Protein Involved in Engulfment of Apoptotic Cells with CED-1 and CD91/Low Density Lipoprotein Receptor-related Protein (LRP)
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L. Z. Scheifele, R. A. Garbitt, J. D. Rhoads, and L. J. Parent
Nuclear entry and CRM1-dependent nuclear export of the Rous sarcoma virus Gag polyprotein
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S. Agarwalla, J. T. Kealey, D. V. Santi, and R. M. Stroud
Characterization of the 23 S Ribosomal RNA m5U1939 Methyltransferase from Escherichia coli
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N. Kato, S. Suyama, M. Shirokane, M. Kato, T. Kobayashi, and N. Tsukagoshi
Novel {alpha}-Glucosidase from Aspergillus nidulans with Strong Transglycosylation Activity
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D. W.A. Buchan, A. J. Shepherd, D. Lee, F. M.G. Pearl, S. C.G. Rison, J. M. Thornton, and C. A. Orengo
Gene3D: Structural Assignment for Whole Genes and Genomes Using the CATH Domain Structure Database
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C. Huang, X. Zhang, Q. Lin, X. Xu, Z. Hu, and C.-L. Hew
Proteomic Analysis of Shrimp White Spot Syndrome Viral Proteins and Characterization of a Novel Envelope Protein VP466
Mol. Cell. Proteomics,
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C. Iavarone, C. Wolfgang, V. Kumar, P. Duray, M. Willingham, I. Pastan, and T. K. Bera
PAGE4 Is a Cytoplasmic Protein That Is Expressed in Normal Prostate and in Prostate Cancers
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M. Schubert, U. A. Petersson, B. J. Haas, C. Funk, W. P. Schroder, and T. Kieselbach
Proteome Map of the Chloroplast Lumen of Arabidopsis thaliana
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H. Chen, Y. Pan, E. A. Wong, J. R. Bloomquist, and K. E. Webb Jr.
Molecular Cloning and Functional Expression of a Chicken Intestinal Peptide Transporter (cPepT1) in Xenopus Oocytes and Chinese Hamster Ovary Cells
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M. Lin, D. R. Sutherland, W. Horsfall, N. Totty, E. Yeo, R. Nayar, X.-F. Wu, and A. C. Schuh
Cell surface antigen CD109 is a novel member of the alpha 2 macroglobulin/C3, C4, C5 family of thioester-containing proteins
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R. J. Kelso, A. M. Hudson, and L. Cooley
Drosophila Kelch regulates actin organization via Src64-dependent tyrosine phosphorylation
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703 - 713.
[Abstract]
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