SUPERFAMILY 1.75 HMM library and genome assignments server

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Myosin S1 fragment, N-terminal domain superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All beta proteins [ 48724] (174)
Fold:   SH3-like barrel [ 50036] (21)
Superfamily:   Myosin S1 fragment, N-terminal domain [ 50084]
Families:   Myosin S1 fragment, N-terminal domain [ 50085]


Superfamily statistics
Genomes (307) Uniprot 2018_03 genome PDB chains (SCOP 1.75)
Domains 540 0 0
Proteins 540 0 0


Functional annotation
General category Processes_IC
Detailed category Cell motility

Document:
Function annotation of SCOP domain superfamilies

UniProtKB KeyWords (KW)

(show details)
KW termFDR (all)SDKW levelAnnotation (direct or inherited)
Biological processTransport0.0001585Least InformativeDirect
Biological processCell cycle0.000000851Moderately InformativeDirect
Biological processProtein transport0.0000223Moderately InformativeDirect
DomainCoiled coil0Moderately InformativeDirect
Molecular functionNucleotide-binding0Least InformativeDirect
Post-translational modificationActin-binding0InformativeDirect
Post-translational modificationCalmodulin-binding0InformativeDirect
Post-translational modificationMyosin0Highly InformativeDirect
Post-translational modificationPhosphoprotein0.0000001088Least InformativeDirect
Post-translational modificationMethylation0.00000003165Moderately InformativeDirect

Document: KW annotation of SCOP domains

InterPro annotation
Cross references IPR008989 SSF50084 Protein matches
Abstract

Myosin is a molecular motor that undergoes ATP-driven conformational changes during force production and motility. The S1 fragment myosin head consists of both the globular motor domain, containing the ATP- and actin-binding sites, and the lever arm, which amplifies small conformational changes in the motor domain into larger motions by which myosin moves actin. The motor domain contains four major subdomains linked by three single-stranded joints: the N-terminal subdomain, the upper 50-kDa subdomain, the lower 50-kDa subdomain, and the C-terminal converter subdomain [PubMed11016966]. The N-terminal subdomain has an SH3-like partly opened beta barrel topology, with the last strand being interrupted by a 3-10 helical turn. The N-terminal and upper 50-kDa subdomains together form the nucleotide-binding pocket. The binding of specific nucleotides alters the structural state of the myosin head during the contractile cycle.


InterPro database


PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · UniProtKB KeyWords (KW) ]

Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 6 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a Myosin S1 fragment, N-terminal domain domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 6 hidden Markov models representing the Myosin S1 fragment, N-terminal domain superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · UniProtKB KeyWords (KW) · Internal database links ]