The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Nucleic acid-binding protein domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 1: Baseplate hub subunit and tail lysozyme

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 5 GO terms relating to "molecular function"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Lysozyme activity GO:0003796
Catalysis of the hydrolysis of the beta-(1->4) linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan.
5 P16009 (/IDA) P16009 (/IDA) P16009 (/IDA) P16009 (/IDA) P16009 (/IDA)
Lysozyme activity GO:0003796
Catalysis of the hydrolysis of the beta-(1->4) linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan.
5 P16009 (/IMP) P16009 (/IMP) P16009 (/IMP) P16009 (/IMP) P16009 (/IMP)
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
5 P16009 (/IPI) P16009 (/IPI) P16009 (/IPI) P16009 (/IPI) P16009 (/IPI)
Peptidoglycan beta-N-acetylmuramidase activity GO:0033922
Catalysis of the hydrolysis of terminal, non-reducing N-acetylmuramic residues.
5 P16009 (/IDA) P16009 (/IDA) P16009 (/IDA) P16009 (/IDA) P16009 (/IDA)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
5 P16009 (/IMP) P16009 (/IMP) P16009 (/IMP) P16009 (/IMP) P16009 (/IMP)

There are 3 GO terms relating to "biological process"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Pathogenesis GO:0009405
The set of specific processes that generate the ability of an organism to induce an abnormal, generally detrimental state in another organism.
5 P16009 (/IMP) P16009 (/IMP) P16009 (/IMP) P16009 (/IMP) P16009 (/IMP)
Protein homotrimerization GO:0070207
The formation of a protein homotrimer, a macromolecular structure consisting of three noncovalently associated identical subunits.
5 P16009 (/IMP) P16009 (/IMP) P16009 (/IMP) P16009 (/IMP) P16009 (/IMP)
Entry into host via enzymatic degradation of host anatomical structure GO:0085027
Penetration by symbiont of a host anatomical structure which provides a barrier to symbiont entry, mediated by symbiont degradative enzymes.
5 P16009 (/IDA) P16009 (/IDA) P16009 (/IDA) P16009 (/IDA) P16009 (/IDA)

There are 3 GO terms relating to "cellular component"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Virion GO:0019012
The complete fully infectious extracellular virus particle.
5 P16009 (/IDA) P16009 (/IDA) P16009 (/IDA) P16009 (/IDA) P16009 (/IDA)
Virus tail GO:0098015
Part of the virion that may be used to recognize, attach and inject the viral genome and accessory proteins into the host cell.
5 P16009 (/IMP) P16009 (/IMP) P16009 (/IMP) P16009 (/IMP) P16009 (/IMP)
Virus tail, baseplate GO:0098025
Multiprotein component at the distal (head) end of the virus tail to which fibers of tailed viruses may be attached.
5 P16009 (/IDA) P16009 (/IDA) P16009 (/IDA) P16009 (/IDA) P16009 (/IDA)