| Number |
Known function /
Putative domain |
Description |
Related HVR clusters |
| 27 |
Actin-ADP-ribosylating toxin |
Function experimentally validated by Science. 2010 327(5969):1139-42. |
TCHC_076
TCHC_108
|
| 191 |
PTP_DSP_cys superfamily |
Cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases. |
TCHC_025
TCHC_042
|
| 164 |
DRAT superfamily |
Dinitrogenase reductase ADP-ribosyltransferase (DRAT); This family consists of several bacterial dinitrogenase reductase ADP-ribosyltransferase (DRAT) proteins. Members of this family seem to be specific to Rhodospirillum, Rhodobacter and Azospirillum species. Dinitrogenase reductase ADP-ribosyl transferase (DRAT) carries out the transfer of the ADP-ribose from NAD to the Arg-101 residue of one subunit of the dinitrogenase reductase homodimer, resulting in inactivation of that enzyme. Dinitrogenase reductase-activating glycohydrolase (DRAG) removes the ADP-ribose group attached to dinitrogenase reductase, thus restoring nitrogenase activity. The DRAT-DRAG system negatively regulates nitrogenase activity in response to exogenous NH4+ or energy limitation in the form of a shift to darkness or to anaerobic conditions. |
TCHC_089
|
| 163 |
YwqJ-deaminase superfamily |
YwqJ-like deaminase; A member of the nucleic acid/nucleotide deaminase superfamily prototyped by Bacillus YwqJ. Members of this family are present in a wide phyletic range of bacteria and a few basidiomycetes. Bacterial versions are predicted to function as toxins in bacterial polymorphic toxin systems. |
TCHC_019
TCHC_033
TCHC_050
TCHC_055
TCHC_083
TCHC_094
TCHC_106
TCHC_133
|
| 83 |
M35_like superfamily |
Peptidase M35 family; Family M35 Zn2+-metallopeptidase domain, also known as the deuterolysin family, contains fungal as well as bacterial metalloendopeptidases that include deuterolysin (EC2.4.24.39), peptidyl-Lys metalloendopeptidase (MEP), penicillolysin, as well as uncharacterized sequences. Typically, members of this family of extracellular peptidases contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand and is found in a GTXDXXYG motif C-terminal to the His zinc ligands. Deuterolysins are highly active towards basic nuclear proteins such as histones and protamines, with a preference for a Lys or Arg residue in the P1' subsite. MEPs specifically cleave peptidyl-lysine bonds (-X-Lys-) in proteins and peptides. Penicillolysin, a thermolabile protease from Penicillium citrinum, strongly hydrolyzes nuclear proteins such as clupeine, salmine and histone. Many members of the M35 peptidases display unusual thermostabilities. |
TCHC_032
TCHC_105
TCHC_116
TCHC_137
|
| 76 |
PRK15386 superfamily |
Type III secretion protein GogB; Provisional |
TCHC_088
TCHC_118
TCHC_144
TCHC_179
|
| 64 |
Gly_transf_sug superfamily |
Glycosyltransferase sugar-binding region containing DXD motif; The DXD motif is a short conserved motif found in many families of glycosyltransferases, which add a range of different sugars to other sugars, phosphates and proteins. DXD-containing glycosyltransferases all use nucleoside diphosphate sugars as donors and require divalent cations, usually manganese. The DXD motif is expected to play a carbohydrate binding role in sugar-nucleoside diphosphate and manganese dependent glycosyltransferases. |
TCHC_046
TCHC_056
TCHC_176
|
| 34 |
Enterotoxin_a superfamily |
Heat-labile enterotoxin alpha chain; Heat-labile enterotoxin alpha chain. |
TCHC_160
TCHC_180
|
| 31 |
EIID-AGA superfamily |
PTS system mannose/fructose/sorbose family IID component; PTS system mannose/fructose/sorbose family IID component. |
TCHC_066
|
| 31 |
T3SS_needle_F superfamily |
Type III secretion needle MxiH, YscF, SsaG, EprI, PscF, EscF; Type III secretion systems are essential virulence determinants for many gram-negative bacterial pathogens. MxiH is an extracellular alpha helical needle that is required for translocation of effector proteins into host cells. Once inside, the effector proteins subvert normal cell function to aid infection. The needle protein F, polymerizes to form a shaft. |
TCHC_146
TCHC_163
|
