The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Gp5 N-terminal 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 2220: Rhs element Vgr protein

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 7 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
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
1 A0A0H3AIG7 (/IDA)
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
1 Q9KS45 (/ISS)
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).
1 Q9KN42 (/IPI)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 A0A0H3AIG7 (/IDA)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 Q9KS45 (/ISS)
Acid-amino acid ligase activity GO:0016881
Catalysis of the ligation of an acid to an amino acid via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate.
1 A0A0H3AIG7 (/IDA)
Acid-amino acid ligase activity GO:0016881
Catalysis of the ligation of an acid to an amino acid via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate.
1 Q9KS45 (/ISS)

There are 8 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
Protein secretion by the type VI secretion system GO:0033103
The process in which proteins are transferred into the extracellular milieu or directly into host cells by the type VI secretion system. Proteins secreted by this system do not require an N-terminal signal sequence.
8 Q9HTT3 (/IGC) Q9HU93 (/IGC) Q9HYC3 (/IGC) Q9HYU9 (/IGC) Q9I1A6 (/IGC) Q9I3K1 (/IGC) Q9I6M7 (/IGC) Q9I741 (/IGC)
Protein secretion by the type VI secretion system GO:0033103
The process in which proteins are transferred into the extracellular milieu or directly into host cells by the type VI secretion system. Proteins secreted by this system do not require an N-terminal signal sequence.
3 Q9I0F3 (/IMP) Q9I737 (/IMP) Q9I741 (/IMP)
Actin filament depolymerization GO:0030042
Disassembly of actin filaments by the removal of actin monomers from a filament.
2 A0A0H3AIG7 (/IDA) Q9KS45 (/IDA)
Protein secretion by the type VI secretion system GO:0033103
The process in which proteins are transferred into the extracellular milieu or directly into host cells by the type VI secretion system. Proteins secreted by this system do not require an N-terminal signal sequence.
2 Q9I0F3 (/IDA) Q9I741 (/IDA)
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.
1 Q9KS45 (/IDA)
Isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine GO:0018153
The formation of an isopeptide cross-link between peptidyl-lysine and peptidyl-glutamine to produce N6-(L-isoglutamyl)-L-lysine.
1 A0A0H3AIG7 (/IDA)
Isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine GO:0018153
The formation of an isopeptide cross-link between peptidyl-lysine and peptidyl-glutamine to produce N6-(L-isoglutamyl)-L-lysine.
1 Q9KS45 (/ISS)
Isopeptide cross-linking GO:0018262
The formation of a covalent cross-link between or within peptide chains, where either the amino group or the carboxyl group, or both, are not attached to the alpha carbon.
1 Q9KS45 (/IDA)

There are 4 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
Type VI protein secretion system complex GO:0033104
A complex of proteins that permits the transfer of proteins into the extracellular milieu or directly into host cells via the type VI secretion system. Proteins secreted by this complex do not require an N-terminal signal sequence.
8 Q9HTT3 (/IGC) Q9HU93 (/IGC) Q9HYC3 (/IGC) Q9HYU9 (/IGC) Q9I1A6 (/IGC) Q9I3K1 (/IGC) Q9I6M7 (/IGC) Q9I741 (/IGC)
Type VI protein secretion system complex GO:0033104
A complex of proteins that permits the transfer of proteins into the extracellular milieu or directly into host cells via the type VI secretion system. Proteins secreted by this complex do not require an N-terminal signal sequence.
3 Q9I0F3 (/IMP) Q9I737 (/IMP) Q9I741 (/IMP)
Type VI protein secretion system complex GO:0033104
A complex of proteins that permits the transfer of proteins into the extracellular milieu or directly into host cells via the type VI secretion system. Proteins secreted by this complex do not require an N-terminal signal sequence.
2 Q9I0F3 (/IDA) Q9I741 (/IDA)
Host cell cytoplasm GO:0030430
The cytoplasm of a host cell.
1 Q9KS45 (/IDA)