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MegaMotifbase

Structural motifs in protein families and superfamilies

Description

More detailed information about this field from each metasource.

Structural motifs in protein families and superfamilies

metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

Webpage:

http://caps.ncbs.res.in/MegaMotifbase/index.html

Webpage

More detailed information about this field from each metasource.

http://caps.ncbs.res.in/MegaMotifbase/index.html

metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

Tags:

Tags
More detailed information about this field from each metasource.

protein sequence databases
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

protein properties
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

structure databases
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

protein structure
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

protein sequence protein properties structure protein structure

More to explore:

1/20

LenVarDB

Database of length variantion in protein domains

MALISAM

Manual alignments for structurally analogous motifs in proteins

GenDiS

Genomic distribution of protein structural superfamilies

SMoS.2: Update of database of Structural Motifs in Superfamilies

Remote homology detection, namely the accumulation of reliable but distantly related sequences of a protein family, remains a challenging problem in biology. Early realisation of such relationships ca ...

PASS2

PASS2 contains alignments of structural motifs of protein superfamilies. PASS2 is an automatic version of the original superfamily alignment database, CAMPASS (CAMbridge database of Protein Alignments ...

IMOTdb

Structural motifs are central to the integrity of the fold and require careful analysis for their identification. IMOTdb is a repertoire of spatially interacting motifs in single protein structures as ...

DSDBASE

DSDBASE is a database of disulphide bonds in proteins that provides information on native disulphides and those that are stereochemically possible between pairs of residues for all known protein struc ...

SPROUTS

Structural Prediction for pRotein fOlding UTility System

PIDD

PIDD is a dedicated database and structural bio-informatics system for distance based protein modeling. The database is developed to host and analyze the statistical data for protein inter-atomic dist ...

CoPS

Comprehensive peptide signature database

TOPPR

The Online Protein Processing Resource

PDBflex

Flexibility in protein structures

3DSwap: Database of Proteins involved in 3D domain Swapping

Protein oligomerization is a key biochemical step to perform the designated function of proteins. 3D domain swapping is a unique protein oligomerization phenomenon observed in a wide array of proteins ...

eProS

Energy profiles of protein structures

InterDom

Putative protein domain interactions

Dockground

Protein-protein interfaces in co-crystallized protein structures

Sequence-Structural Templates of Single-member Superfamilies

SSToSS is a database which provides sequence-structural templates of single member protein domain superfamilies like PASS2. Sequence-structural templates are recognized by considering the content and ...

ProSAS

Protein Structure and Alternative Splicing: effects of alternative splicing events on protein structure

PPT-DB

Protein Property Prediction and Testing Database

PRTAD

PRTAD is a dedicated database and structural bioinformatics system for protein analysis and modeling. The database is developed to host and analyze the statistical data for protein residue level "virt ...

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Data is amalgamated and only retrieved periodically.
Some of the resources used by the system:

® FAIRsharing.org
® Bioontology/Bioportal Terms
® Nucleic Acid Research - Database
® re3data.org
® bio.tools
® PubMed - Courtesy of the U.S. National Library of Medicine