This document provides an overview of several important protein databases: - SWISS-PROT is an annotated protein sequence database that is maintained collaboratively and contains over 1.29 million entries. TrEMBL is a computer-annotated supplement to SWISS-PROT containing sequences not yet in SWISS-PROT. - Structural databases like PDB, SCOP, and CATH provide protein structure information. PDB is an international repository for macromolecular structures. SCOP and CATH classify protein domains based on structural similarities and evolutionary relationships. - Other databases mentioned include InterPro, GOA, Proteome Analysis, and GenBank, which provide functional annotation, gene ontology assignments, proteome analysis

1. Protein Database
Presented by:-
Rajpal Choudhary
M.Sc. Biotechnology 2nd year
161103004

2. Protein database
• SWISS-PROT: Annotated Sequence Database
• TrEMBL: Database of EMBL nucleotide translated sequences
• InterPro: Integrated resource for protein families, domains and functional sites.
• CluSTr: Offers an automatic classification of SWISS-PROT and TrEMBL.
• IPI: A non-redundant human proteome set constructed from SWISS-PROT, TrEMBL, Ensembl and
RefSeq.
• GOA: Provides assignments of gene products to the Gene Ontology (GO) resource.
• Proteome Analysis: Statistical and comparative analysis of the predicted proteomes of fully
sequenced organisms
• Protein Profiles: Tables of SWISS-PROT and TrEMBL entries and alignments for the protein
families of the Protein Profile.

3. Swiss-Prot
• Annotated protein sequence database established in 1986 and
maintained collaboratively since 1987, by the Department of Medical
Biochemistry of the University of Geneva and EBI
• Complete, Curated, Non-redundant and cross-referenced with 34 other
databases
• Highly cross-referenced
• Available from a variety of servers and through sequence analysis
software tools
• More than 8,000 different species
• First 20 species represent about 42% of all sequences in the database
• More than 1,29,000 entries with 4.7 X 1010 amino acids
• More than 6,22,000 entries in TrEMBL

4. TrEMBL (Translation of EMBL)
• Computer-annotated supplement to SWISS-PROT, as it is impossible to
cope with the flow of data.
• Well-structure SWISS-PROT-like resource
• Derived from automated EMBL CDS translation maintained at the EBI,
UK.
• TrEMBL is automatically generated and annotated using software tools
(incompatible with the SWISS-PROT in terms of quality)
• TrEMBL contains all what is not yet in SWISS-PROT

5. SWISS-PROT file format

6. SWISS-PROT file format

7. SWISS-PROT file format

8. SWISS-PROT file format

9. GenBank
(http://www.ncbi.nlm.nih.gov/genbank/)
• The GenBank is a sequence database that stores nucleotide
sequences and the proteins obtained from them by translations. This
database is maintained by National Center for Biotechnology
Information (NCBI). As of April 2011, the GenBank contains
approximately 126,551,501,141 numbers of bases in 135,440,924
numbers of sequences. Each sequence submitted to GenBank is
assigned a unique GenBank identifier or GenBank accession number.

10. Structure Databases
•MSD: Macromolecular Structure Database - A relational database
representation of clean Protein Data Bank (PDB).
•3DSeq: 3D sequence alignment server- Annotation of the alignments
between sequence database and the PDB.
•FSSP: Based on exhaustive all-against-all 3D structure comparison of
protein structures currently in the Protein Data Bank (PDB)
•DALI: Fold Classification based on Structure-Structure Assignments.
•3Dee: Database of protein domain definitions wherein the domains
have been clustered on sequence and structural similarity.
•NDB: Nucleic Acid Structure Database

11. htttp://www.rcsb.org/pdb/

12. Protein Data Bank (PDB)
• Important in solving real problems in molecular biology
• Protein Databank
• PDB Established in 1972 at Brookhaven National Laboratory
(BNL)
• Sole international repository of macromolecular structure data
• Moved to Research Collaboratory for Structural Bioinformatics
http://www.rcsb.org/

13. Effective use of PDB
• Queries are of three types
• PDBid - As quoted in paper
• Search Lite - one or more keywords
• Search Fields - A detailed query form
• Query results
• Structure Explorer - details of the structure
• Query Result Browser - for multiple structures
• PDB Viewer

16. SCOP (Structural Classification of Protein)
(http://scop.mrc-lmb.cam.ac.uk/scop/)
• The Structural Classification of Proteins (SCOP) database is basically
a database with manual classification of protein structural
domains. The whole concept is based on similarities of the amino
acid sequences and three- dimensional structures of the proteins.
The database was originally published in 1995 and it is usually
updated at least once yearly by Alexei G. Murzin and his
colleagues.

17. • SCOP database uses the following protein structural hierarchy:
• Class—It is the general structural architecture of the protein domains.
• Fold—It represents similar arrangement of regular secondary
structures but without evidence of evolutionary relatedness.
• Superfamily—It represents whether the protein structures have
sufficient structural and functional similarities to each other to infer a
divergent evolutionary relation- ship but not necessarily a detectable
sequence homology.
• Family—Proteins belonging to the same family share some sequence
similarity.

18. • SCOP has the following classes:
• 1) Proteins with mostly α-helical domains;
• 2) Proteins with mostly β-sheet domains;
• 3) Proteins with α/β domains which contain beta- alpha-beta
structural units or motifs that form mainly parallel β-sheets;
• 4) Proteins with mostly α + β domains consisting of independent α-
helices and mainly antiparallel β-sheets;

19. CATH (Class Architecture Topology Homology)
(http://www.cathdb.info/)
• The CATH Protein Structure Classification method is a semi-automatic,
hierarchical classification of protein domains. The database was first
published in 1997 by Christine Orengo, Janet Thornton and their
colleagues. CATH carries many broad features with its principal rival,
SCOP. However there are also many areas in which the detailed
classifications in the two databases differ greatly.

20. • CATH clusters proteins at four major levels:
• 1) Class (C): Class is derived from secondary structure contents of proteins.
It is assigned for more than 90% of protein structures automatically.
• 2) Architecture (A): Architecture describes the gross orientation of
secondary structures, independent of connectivity in proteins.
• 3) Topology (T): Topology level of CATH clusters protein structures
according to their topological connections & numbers of secondary
structures.
• 4) Homologous Superfamily (H): Homologous super- families of CATH
cluster the proteins with highly similar structures & functions.

21. Conclusion
The different databases discussed here provide different information.
PDB gives both structural and sequence information of
macromolecules whereas SCOP & CATH have structures based on their
evolutionary relationships and folding classes. The structural
classifications of proteins are generally obtained from SCOP and CATH.
On the other hand, the UniProt/Swissprot database provides the
sequence annotations of proteins along with links to the external
databases like PDB. All these databases are increasing day by day. There
are other databases and some new databases are coming. But the
databases discussed here are considered to be the foundation stones
of bioinformatics.

22. REFERENCES
• G. Murzin, S. E. Brenner, T. Hubbard and C. Chothia, “SCOP: A Structural Classification of Proteins Database
for the Investigation of Sequences and Structures,” Jour- nal of Molecular Biology, Vol. 247, No. 4, 1995, pp.
536- 540. doi:10.1016/S0022-2836(05)80134-2
• L. Lo Conte, S. E. Brenner, T. J. Hubbard, C. Chothia and A. G. Murzin, “SCOP Database in 2002: Refinements
Accommodate Structural Genomics,” Nucleic Acids Re- search, Vol. 30, No. 1, 2002, pp. 264-267.
doi:10.1093/nar/30.1.264
• Andreeva, D. Howorth, S. E. Brenner, T. J. Hubbard, C. Chothia and A. G. Murzin, “SCOP Database in 2004: Re-
finements Integrate Structure and Sequence Family Data,” Nucleic Acids Research, Vol. 32, Suppl. 1, 2004,
pp. D226-D229. doi:10.1093/nar/gkh039
• R. Day, D. A. Beck, R. S. Armen and V. Daggett, “A Consensus View of Fold Space: Combining SCOP, CATH, and
the Dali Domain Dictionary,” Protein Scien- ce, Vol. 12, No. 10, 2003, pp. 2150-2160. doi:10.1110/ps.0306803

23. Thank you