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Conserved domains on  [gi|446522393|ref|WP_000599739|]
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MULTISPECIES: protein adenylyltransferase Fic [Bacteria]

Protein Classification

Fic/DOC family protein( domain architecture ID 11450684)

Fic/DOC family protein similar to cell filamentation protein Fic, which may act as a denylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FIDO COG2184
Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];
1-176 2.63e-58

Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];


:

Pssm-ID: 441787 [Multi-domain]  Cd Length: 196  Bit Score: 181.66  E-value: 2.63e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393   1 MILENKLGLTNQVELAKVEEKLSKQKAKELYDcgkINEIEVGTFKGLSEIHEFLFSDIYDFAGKIRSVNIAKGNFRFAPV 80
Cdd:COG2184   13 TVLRNKLGITDAAELDEAEAELTALRAAELFE---RPPPGVFDLAHLKAIHRRLFGDVYDWAGQIRTVNISKGGTRFAPP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393  81 MYLEHSLQHIDQ-----------MPQTSFEEIIKKYVEMNIAHPFREGNGRSTRIWLDLILkEELQKVVDWNLIDKADYL 149
Cdd:COG2184   90 SFIERELEALFDdlreenylrglDREEFAERLARFHGELNVIHPFREGNGRTQRLFFDQLA-RQAGYPLDWSRVDKEEYL 168

                        170       180
                 ....*....|....*....|....*...
gi 446522393 150 SAMERSPINDLE-IRYLISNALTDKIDD 176
Cdd:COG2184  169 EALIAADNGDYSpLKALFRDALTPARES 196
 
Name Accession Description Interval E-value
FIDO COG2184
Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];
1-176 2.63e-58

Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];


Pssm-ID: 441787 [Multi-domain]  Cd Length: 196  Bit Score: 181.66  E-value: 2.63e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393   1 MILENKLGLTNQVELAKVEEKLSKQKAKELYDcgkINEIEVGTFKGLSEIHEFLFSDIYDFAGKIRSVNIAKGNFRFAPV 80
Cdd:COG2184   13 TVLRNKLGITDAAELDEAEAELTALRAAELFE---RPPPGVFDLAHLKAIHRRLFGDVYDWAGQIRTVNISKGGTRFAPP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393  81 MYLEHSLQHIDQ-----------MPQTSFEEIIKKYVEMNIAHPFREGNGRSTRIWLDLILkEELQKVVDWNLIDKADYL 149
Cdd:COG2184   90 SFIERELEALFDdlreenylrglDREEFAERLARFHGELNVIHPFREGNGRTQRLFFDQLA-RQAGYPLDWSRVDKEEYL 168

                        170       180
                 ....*....|....*....|....*...
gi 446522393 150 SAMERSPINDLE-IRYLISNALTDKIDD 176
Cdd:COG2184  169 EALIAADNGDYSpLKALFRDALTPARES 196
PRK10347 PRK10347
putative adenosine monophosphate-protein transferase Fic;
2-160 6.94e-20

putative adenosine monophosphate-protein transferase Fic;


Pssm-ID: 182396 [Multi-domain]  Cd Length: 200  Bit Score: 82.93  E-value: 6.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393   2 ILENKLGLTNQVELAKVEEKLSKQKAKElydcgkineIEVGTFK----GLSEIHEFLFSDIYDFAGKIRSVNIAKGNFRF 77
Cdd:PRK10347  19 VMRNRLNIHQAQRLEQAAYEMTALRAAT---------IELGPLVrglpHLCAIHRQLYQDIFDWAGQLREVDIYQGDTPF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393  78 APVMYLEHS----LQHIDQ------MPQTSF-EEIIKKYVEMNIAHPFREGNGRSTRIWLDLiLKEELQKVVDWNLIDKA 146
Cdd:PRK10347  90 CHFAYIEKEgnalMQDLEEegylvgLEKAKFvERLAHYYCEINVLHPFRVGSGLAQRIFFEQ-LAIHAGYQLSWQGIEKE 168

                        170
                 ....*....|....
gi 446522393 147 DYLSAMERSPINDL 160
Cdd:PRK10347 169 AWNQANQSGAMGDL 182
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
 49-130 1.86e-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: 55.55  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393   49 EIHEFLFSDiYDFAGKIRSVNIA-KGNFRFAPVMYLEHSLQHIDQMPQTSFEEIIKK----YVEMNIAHPFREGNGRSTR 123
Cdd:pfam02661   9 ALHRLLIER-HGGAGGARDVNVSgLLESALARPEQIPFGLEELLLYPDLDREHPLEKaaalHFGFAKIHPFRDGNGRTAR 87


                  ....*..
gi 446522393  124 IWLDLIL 130
Cdd:pfam02661  88 LLANLFL 94
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
 46-175 7.19e-05

mobile mystery protein B; Members of this protein family, which we designate mobile mystery protein B, are found in mobization-related contexts more often than not, including within a CRISPR-associated gene region in Geobacter sulfurreducens PCA, and on plasmids in Agrobacterium tumefaciens and Coxiella burnetii, always together with mobile mystery protein A (TIGR02612), a member of the family of helix-turn-helix DNA binding proteins (pfam01381). This protein is encoded by the downstream member of the gene pair and belongs to the Fic protein family (pfam02661), where Fic (filamentation induced by cAMP) is a regulator of cell division. The characteristics of having a two-gene operon in a varied context and often on plasmids, with one member affecting cell division and the other able to bind DNA, suggests similarity to addiction modules.


Pssm-ID: 131662  Cd Length: 186  Bit Score: 41.74  E-value: 7.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393   46 GLSEIHEFLFSDIYDFAGKIRSV--NIAKGNFRFAPVMY-----LEHSLQHIDQMPqtsfEEI-IKKYVEMNIAHPFREG 117
Cdd:TIGR02613  53 FLRRLHRRMFGDVWRWAGDFRTTqkNIGVSPLQIPSELAillddVRYWLQNGTFSP----DEIaIRFHHRLVAIHPFPNG 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446522393  118 NGRSTRIWLDLILKEELQKVVDWNLIDKADylsamerspINDLEIRYLISNALTDKID 175
Cdd:TIGR02613 129 NGRHARLATDLLLEQQGYSPFTWGSGSLAL---------VGDLRKEYIAALKAADRHD 177
 
Name Accession Description Interval E-value
FIDO COG2184
Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];
1-176 2.63e-58

Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];


Pssm-ID: 441787 [Multi-domain]  Cd Length: 196  Bit Score: 181.66  E-value: 2.63e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393   1 MILENKLGLTNQVELAKVEEKLSKQKAKELYDcgkINEIEVGTFKGLSEIHEFLFSDIYDFAGKIRSVNIAKGNFRFAPV 80
Cdd:COG2184   13 TVLRNKLGITDAAELDEAEAELTALRAAELFE---RPPPGVFDLAHLKAIHRRLFGDVYDWAGQIRTVNISKGGTRFAPP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393  81 MYLEHSLQHIDQ-----------MPQTSFEEIIKKYVEMNIAHPFREGNGRSTRIWLDLILkEELQKVVDWNLIDKADYL 149
Cdd:COG2184   90 SFIERELEALFDdlreenylrglDREEFAERLARFHGELNVIHPFREGNGRTQRLFFDQLA-RQAGYPLDWSRVDKEEYL 168

                        170       180
                 ....*....|....*....|....*...
gi 446522393 150 SAMERSPINDLE-IRYLISNALTDKIDD 176
Cdd:COG2184  169 EALIAADNGDYSpLKALFRDALTPARES 196
PRK10347 PRK10347
putative adenosine monophosphate-protein transferase Fic;
2-160 6.94e-20

putative adenosine monophosphate-protein transferase Fic;


Pssm-ID: 182396 [Multi-domain]  Cd Length: 200  Bit Score: 82.93  E-value: 6.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393   2 ILENKLGLTNQVELAKVEEKLSKQKAKElydcgkineIEVGTFK----GLSEIHEFLFSDIYDFAGKIRSVNIAKGNFRF 77
Cdd:PRK10347  19 VMRNRLNIHQAQRLEQAAYEMTALRAAT---------IELGPLVrglpHLCAIHRQLYQDIFDWAGQLREVDIYQGDTPF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393  78 APVMYLEHS----LQHIDQ------MPQTSF-EEIIKKYVEMNIAHPFREGNGRSTRIWLDLiLKEELQKVVDWNLIDKA 146
Cdd:PRK10347  90 CHFAYIEKEgnalMQDLEEegylvgLEKAKFvERLAHYYCEINVLHPFRVGSGLAQRIFFEQ-LAIHAGYQLSWQGIEKE 168

                        170
                 ....*....|....
gi 446522393 147 DYLSAMERSPINDL 160
Cdd:PRK10347 169 AWNQANQSGAMGDL 182
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
 49-130 1.86e-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: 55.55  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393   49 EIHEFLFSDiYDFAGKIRSVNIA-KGNFRFAPVMYLEHSLQHIDQMPQTSFEEIIKK----YVEMNIAHPFREGNGRSTR 123
Cdd:pfam02661   9 ALHRLLIER-HGGAGGARDVNVSgLLESALARPEQIPFGLEELLLYPDLDREHPLEKaaalHFGFAKIHPFRDGNGRTAR 87


                  ....*..
gi 446522393  124 IWLDLIL 130
Cdd:pfam02661  88 LLANLFL 94
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
 46-175 7.19e-05

mobile mystery protein B; Members of this protein family, which we designate mobile mystery protein B, are found in mobization-related contexts more often than not, including within a CRISPR-associated gene region in Geobacter sulfurreducens PCA, and on plasmids in Agrobacterium tumefaciens and Coxiella burnetii, always together with mobile mystery protein A (TIGR02612), a member of the family of helix-turn-helix DNA binding proteins (pfam01381). This protein is encoded by the downstream member of the gene pair and belongs to the Fic protein family (pfam02661), where Fic (filamentation induced by cAMP) is a regulator of cell division. The characteristics of having a two-gene operon in a varied context and often on plasmids, with one member affecting cell division and the other able to bind DNA, suggests similarity to addiction modules.


Pssm-ID: 131662  Cd Length: 186  Bit Score: 41.74  E-value: 7.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446522393   46 GLSEIHEFLFSDIYDFAGKIRSV--NIAKGNFRFAPVMY-----LEHSLQHIDQMPqtsfEEI-IKKYVEMNIAHPFREG 117
Cdd:TIGR02613  53 FLRRLHRRMFGDVWRWAGDFRTTqkNIGVSPLQIPSELAillddVRYWLQNGTFSP----DEIaIRFHHRLVAIHPFPNG 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446522393  118 NGRSTRIWLDLILKEELQKVVDWNLIDKADylsamerspINDLEIRYLISNALTDKID 175
Cdd:TIGR02613 129 NGRHARLATDLLLEQQGYSPFTWGSGSLAL---------VGDLRKEYIAALKAADRHD 177
COG3177 COG3177
Fic family protein [Transcription];
112-155 1.07e-03

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 38.90  E-value: 1.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446522393 112 HPFREGNGRSTRIWLDLIL-KEELQKVVDWNLI-----DKADYLSAMERS 155
Cdd:COG3177  171 HPFADGNGRTGRLLMNLLLlRAGLLSQPLLPLSriieeDRDEYYDALEAV 220
 
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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