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Conserved domains on  [gi|2541755729|ref|WP_297840678|]
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virulence protein RhuM/Fic/DOC family protein [Ignavibacterium sp.]

Protein Classification

virulence protein RhuM/Fic/DOC family protein( domain architecture ID 10373956)

bifunctional virulence protein RhuM and Fic (filamentation induced by cAMP)/DOC (death-on-curing) family protein may be involved in virulence/pathogenicity and/or may function as a type II toxin-antitoxin system death-on-curing family toxin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhuM COG3943
Uncharacterized protein RhuM, Salmonella virulence factor [Function unknown];
5-131 1.02e-75

Uncharacterized protein RhuM, Salmonella virulence factor [Function unknown];


:

Pssm-ID: 443143  Cd Length: 130  Bit Score: 228.47  E-value: 1.02e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541755729   5 DAPRGEIVIYKASDGSAQLDVKLEEESVWLTQAQMVILFQTTKQNVSLHINNIFKEGELSEKSVVKEYLTTAADGKK--- 81
Cdd:COG3943     1 RMSTSEILIYQTEDGETKIEVRLEDETVWLTQKQMAELFGVDVSNISKHLKNIFEEGELDEEATVRKFLTVASEGKRevt 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2541755729  82 YKTKYYNLDVIISVGYRVKSKRGTQFRIWANNVIKEYLVKGYALNEKRLK 131
Cdd:COG3943    81 RNVKHYNLDAIISVGYRVNSKRATQFRQWATQVLKEYLIKGFVLDDERLK 130
Doc COG3654
Prophage maintenance system killer protein [Mobilome: prophages, transposons];
215-328 4.27e-27

Prophage maintenance system killer protein [Mobilome: prophages, transposons];


:

Pssm-ID: 442871  Cd Length: 130  Bit Score: 103.40  E-value: 4.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541755729 215 FGGskLFGKEKDQSFRGTIGAIYQTFGKNEVYPSIEEKAAHLLYFTIKNHSFVDGNKRIAAALFLWFLEMNNYLYgkngr 294
Cdd:COG3654    21 YGG--LPGVRDEGLLESALARPRQTFFGEELYPDLFEKAAALLYGIAKNHPFVDGNKRTAFAAALVFLDLNGYEL----- 93

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2541755729 295 kRIADNALVALCLLIAESNPKEKDVIVKVVVNLI 328
Cdd:COG3654    94 -DADDDEAVDLVLAVAAGELDEEELAAWLRKHLE 126
 
Name Accession Description Interval E-value
RhuM COG3943
Uncharacterized protein RhuM, Salmonella virulence factor [Function unknown];
5-131 1.02e-75

Uncharacterized protein RhuM, Salmonella virulence factor [Function unknown];


Pssm-ID: 443143  Cd Length: 130  Bit Score: 228.47  E-value: 1.02e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541755729   5 DAPRGEIVIYKASDGSAQLDVKLEEESVWLTQAQMVILFQTTKQNVSLHINNIFKEGELSEKSVVKEYLTTAADGKK--- 81
Cdd:COG3943     1 RMSTSEILIYQTEDGETKIEVRLEDETVWLTQKQMAELFGVDVSNISKHLKNIFEEGELDEEATVRKFLTVASEGKRevt 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2541755729  82 YKTKYYNLDVIISVGYRVKSKRGTQFRIWANNVIKEYLVKGYALNEKRLK 131
Cdd:COG3943    81 RNVKHYNLDAIISVGYRVNSKRATQFRQWATQVLKEYLIKGFVLDDERLK 130
Virulence_RhuM pfam13310
Virulence protein RhuM family; There are currently no experimental data for members of this ...
 67-133 7.74e-35

Virulence protein RhuM family; There are currently no experimental data for members of this group or their homologs. However, these proteins are implicated in virulence/pathogenicity because RhuM is encoded in the SPI-3 pathogenicity island in Salmonella typhimurium.


Pssm-ID: 463842  Cd Length: 252  Bit Score: 127.20  E-value: 7.74e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541755729  67 SVVKEYLTTAADGKK---YKTKYYNLDVIISVGYRVKSKRGTQFRIWANNVIKEYLVKGYALNEKRLKEQ 133
Cdd:pfam13310   1 ATVRKFLTVAAEGKRevnRNVKHYNLDAIIAVGYRVNSKRGTQFRIWATQVLKEYIIKGFVMDDERLKNT 70
Doc COG3654
Prophage maintenance system killer protein [Mobilome: prophages, transposons];
215-328 4.27e-27

Prophage maintenance system killer protein [Mobilome: prophages, transposons];


Pssm-ID: 442871  Cd Length: 130  Bit Score: 103.40  E-value: 4.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541755729 215 FGGskLFGKEKDQSFRGTIGAIYQTFGKNEVYPSIEEKAAHLLYFTIKNHSFVDGNKRIAAALFLWFLEMNNYLYgkngr 294
Cdd:COG3654    21 YGG--LPGVRDEGLLESALARPRQTFFGEELYPDLFEKAAALLYGIAKNHPFVDGNKRTAFAAALVFLDLNGYEL----- 93

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2541755729 295 kRIADNALVALCLLIAESNPKEKDVIVKVVVNLI 328
Cdd:COG3654    94 -DADDDEAVDLVLAVAAGELDEEELAAWLRKHLE 126
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
 243-282 2.98e-10

Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and doc (death on curing). The Fic protein is involved in cell division and is suggested to be involved in the synthesis of PAB or folate, indicating that the Fic protein and cAMP are involved in a regulatory mechanism of cell division via folate metabolism. This family contains a central conserved motif HPFXXGNG in most members. The exact molecular function of these proteins is uncertain. P1 lysogens of Escherichia coli carry the prophage as a stable low copy number plasmid. The frequency with which viable cells cured of prophage are produced is about 10(-5) per cell per generation. A significant part of this remarkable stability can be attributed to a plasmid-encoded mechanism that causes death of cells that have lost P1. In other words, the lysogenic cells appear to be addicted to the presence of the prophage. The plasmid withdrawal response depends on a gene named doc (death on curing) that is represented by this family. Doc induces a reversible growth arrest of E. coli cells by targetting the protein synthesis machinery. Doc hosts the C-terminal domain of its antitoxin partner Phd (prevents host death) through fold complementation, a domain that is intrinsically disordered in solution but that folds into an alpha-helix on binding to Doc.This domain forms complexes with Phd antitoxins containing pfam02604.


Pssm-ID: 426907  Cd Length: 94  Bit Score: 56.32  E-value: 2.98e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2541755729 243 NEVYPSIEEKAAHLLYFTIKNHSFVDGNKRIAAALFLWFL 282
Cdd:pfam02661  55 DLDREHPLEKAAALHFGFAKIHPFRDGNGRTARLLANLFL 94
DOC_P1 TIGR01550
death-on-curing family protein; The characterized member of this family is the death-on-curing ...
 222-287 2.00e-04

death-on-curing family protein; The characterized member of this family is the death-on-curing (DOC) protein of phage P1. It is part of a two protein operon with prevents-host-death (phd) that forms an addiction module. DOC lacks homology to analogous addiction module post-segregational killing proteins involved in plasmid maintenance. These modules work as a combination of a long lived poison (e.g. this protein) and a more abundant but shorter lived antidote. Members of this family have a well-conserved central motif HxFx[ND][AG]NKR. A similar region, with K replaced by G, is found in the huntingtin interacting protein (HYPE) family. [Unknown function, General]


Pssm-ID: 273687  Cd Length: 121  Bit Score: 40.53  E-value: 2.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541755729 222 GKEKDQSFRGTIGAIYQTFGKNEVY---PSIEEKAAHLLYFTIKNHSFVDGNKRIAAALFLWFLEMNNY 287
Cdd:TIGR01550  20 GLEFGMSNPGRAEATIERVSERLSYeesTDIFEVSAVLLYALIRSHPFNNANKRTALNALLLFLELNGY 88
 
Name Accession Description Interval E-value
RhuM COG3943
Uncharacterized protein RhuM, Salmonella virulence factor [Function unknown];
5-131 1.02e-75

Uncharacterized protein RhuM, Salmonella virulence factor [Function unknown];


Pssm-ID: 443143  Cd Length: 130  Bit Score: 228.47  E-value: 1.02e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541755729   5 DAPRGEIVIYKASDGSAQLDVKLEEESVWLTQAQMVILFQTTKQNVSLHINNIFKEGELSEKSVVKEYLTTAADGKK--- 81
Cdd:COG3943     1 RMSTSEILIYQTEDGETKIEVRLEDETVWLTQKQMAELFGVDVSNISKHLKNIFEEGELDEEATVRKFLTVASEGKRevt 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2541755729  82 YKTKYYNLDVIISVGYRVKSKRGTQFRIWANNVIKEYLVKGYALNEKRLK 131
Cdd:COG3943    81 RNVKHYNLDAIISVGYRVNSKRATQFRQWATQVLKEYLIKGFVLDDERLK 130
Virulence_RhuM pfam13310
Virulence protein RhuM family; There are currently no experimental data for members of this ...
 67-133 7.74e-35

Virulence protein RhuM family; There are currently no experimental data for members of this group or their homologs. However, these proteins are implicated in virulence/pathogenicity because RhuM is encoded in the SPI-3 pathogenicity island in Salmonella typhimurium.


Pssm-ID: 463842  Cd Length: 252  Bit Score: 127.20  E-value: 7.74e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541755729  67 SVVKEYLTTAADGKK---YKTKYYNLDVIISVGYRVKSKRGTQFRIWANNVIKEYLVKGYALNEKRLKEQ 133
Cdd:pfam13310   1 ATVRKFLTVAAEGKRevnRNVKHYNLDAIIAVGYRVNSKRGTQFRIWATQVLKEYIIKGFVMDDERLKNT 70
Doc COG3654
Prophage maintenance system killer protein [Mobilome: prophages, transposons];
215-328 4.27e-27

Prophage maintenance system killer protein [Mobilome: prophages, transposons];


Pssm-ID: 442871  Cd Length: 130  Bit Score: 103.40  E-value: 4.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541755729 215 FGGskLFGKEKDQSFRGTIGAIYQTFGKNEVYPSIEEKAAHLLYFTIKNHSFVDGNKRIAAALFLWFLEMNNYLYgkngr 294
Cdd:COG3654    21 YGG--LPGVRDEGLLESALARPRQTFFGEELYPDLFEKAAALLYGIAKNHPFVDGNKRTAFAAALVFLDLNGYEL----- 93

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2541755729 295 kRIADNALVALCLLIAESNPKEKDVIVKVVVNLI 328
Cdd:COG3654    94 -DADDDEAVDLVLAVAAGELDEEELAAWLRKHLE 126
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
 243-282 2.98e-10

Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and doc (death on curing). The Fic protein is involved in cell division and is suggested to be involved in the synthesis of PAB or folate, indicating that the Fic protein and cAMP are involved in a regulatory mechanism of cell division via folate metabolism. This family contains a central conserved motif HPFXXGNG in most members. The exact molecular function of these proteins is uncertain. P1 lysogens of Escherichia coli carry the prophage as a stable low copy number plasmid. The frequency with which viable cells cured of prophage are produced is about 10(-5) per cell per generation. A significant part of this remarkable stability can be attributed to a plasmid-encoded mechanism that causes death of cells that have lost P1. In other words, the lysogenic cells appear to be addicted to the presence of the prophage. The plasmid withdrawal response depends on a gene named doc (death on curing) that is represented by this family. Doc induces a reversible growth arrest of E. coli cells by targetting the protein synthesis machinery. Doc hosts the C-terminal domain of its antitoxin partner Phd (prevents host death) through fold complementation, a domain that is intrinsically disordered in solution but that folds into an alpha-helix on binding to Doc.This domain forms complexes with Phd antitoxins containing pfam02604.


Pssm-ID: 426907  Cd Length: 94  Bit Score: 56.32  E-value: 2.98e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2541755729 243 NEVYPSIEEKAAHLLYFTIKNHSFVDGNKRIAAALFLWFL 282
Cdd:pfam02661  55 DLDREHPLEKAAALHFGFAKIHPFRDGNGRTARLLANLFL 94
DOC_P1 TIGR01550
death-on-curing family protein; The characterized member of this family is the death-on-curing ...
 222-287 2.00e-04

death-on-curing family protein; The characterized member of this family is the death-on-curing (DOC) protein of phage P1. It is part of a two protein operon with prevents-host-death (phd) that forms an addiction module. DOC lacks homology to analogous addiction module post-segregational killing proteins involved in plasmid maintenance. These modules work as a combination of a long lived poison (e.g. this protein) and a more abundant but shorter lived antidote. Members of this family have a well-conserved central motif HxFx[ND][AG]NKR. A similar region, with K replaced by G, is found in the huntingtin interacting protein (HYPE) family. [Unknown function, General]


Pssm-ID: 273687  Cd Length: 121  Bit Score: 40.53  E-value: 2.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541755729 222 GKEKDQSFRGTIGAIYQTFGKNEVY---PSIEEKAAHLLYFTIKNHSFVDGNKRIAAALFLWFLEMNNY 287
Cdd:TIGR01550  20 GLEFGMSNPGRAEATIERVSERLSYeesTDIFEVSAVLLYALIRSHPFNNANKRTALNALLLFLELNGY 88
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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