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Conserved domains on  [gi|493674768|ref|WP_006625075|]
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MULTISPECIES: Fic family protein [Limnospira]

Protein Classification

Fic family protein( domain architecture ID 11459786)

Fic (Filamentation induced by cAMP) family protein similar to Shewanella oneidensis adenosine monophosphate-protein transferase SoFic, which mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins

Gene Ontology:  GO:0005524|GO:0000287|GO:0042803

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
29-317 8.88e-34

Fic family protein [Transcription];


:

Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 129.42  E-value: 8.88e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768  29 NEQADRLRQ-SGEFQTFSEKLRREIAIETGIIERlYTIDRGITRLLIEQGINEAliphgstdiPVKQVVSLIKDQEAAIE 107
Cdd:COG3177   12 DEALGRLDGlPEELRELLRKLLIEEAYASSAIEG-NTLTLDEVRSLLEGGLTGG---------PPLRDEREVLNYVEALE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768 108 GLFNFVGGQRnLSTSYIKELHQVLTQSQEStealnpqgkifrVPLIKGDWKRQPNNplrpDGTIHEYCPPEQVASEMDLL 187
Cdd:COG3177   82 YLLELLRGEP-LTEELILELHRILLKGLRG------------EDKEPGEYRTGQVG----IGAVYVPPPPEEVPELMEEL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768 188 ITLHHQhqEQKVPPEIEAAWLHHRFTQIHPFQDGNGRVARCLASLVCIQA------SWFPLVITRDDRSVYIAALEQAD- 260
Cdd:COG3177  145 LDWLNE--EDELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLLRAgllsqpLLPLSRIIEEDRDEYYDALEAVRe 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493674768 261 SGDLSSLINLFAKSQKQAFLRSLGLSEQVLSETRRTQVIVSA-IADKLKQNQLASVQD 317
Cdd:COG3177  223 TGDLTPWIEFFLEAILEAAEEALALLERLLELARGRLNERQRkLLELLFENPVLTASE 280
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
29-317 8.88e-34

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 129.42  E-value: 8.88e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768  29 NEQADRLRQ-SGEFQTFSEKLRREIAIETGIIERlYTIDRGITRLLIEQGINEAliphgstdiPVKQVVSLIKDQEAAIE 107
Cdd:COG3177   12 DEALGRLDGlPEELRELLRKLLIEEAYASSAIEG-NTLTLDEVRSLLEGGLTGG---------PPLRDEREVLNYVEALE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768 108 GLFNFVGGQRnLSTSYIKELHQVLTQSQEStealnpqgkifrVPLIKGDWKRQPNNplrpDGTIHEYCPPEQVASEMDLL 187
Cdd:COG3177   82 YLLELLRGEP-LTEELILELHRILLKGLRG------------EDKEPGEYRTGQVG----IGAVYVPPPPEEVPELMEEL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768 188 ITLHHQhqEQKVPPEIEAAWLHHRFTQIHPFQDGNGRVARCLASLVCIQA------SWFPLVITRDDRSVYIAALEQAD- 260
Cdd:COG3177  145 LDWLNE--EDELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLLRAgllsqpLLPLSRIIEEDRDEYYDALEAVRe 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493674768 261 SGDLSSLINLFAKSQKQAFLRSLGLSEQVLSETRRTQVIVSA-IADKLKQNQLASVQD 317
Cdd:COG3177  223 TGDLTPWIEFFLEAILEAAEEALALLERLLELARGRLNERQRkLLELLFENPVLTASE 280
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
 119-234 2.88e-15

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: 71.34  E-value: 2.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768  119 LSTSYIKELHQVLTQSQESTEALnpqgkifrvplikgdwkRQPNNPlrpDGTIHEYCPPEQVASEMDLLITLHHQHQEqk 198
Cdd:pfam02661   2 LDLEDLLALHRLLIERHGGAGGA-----------------RDVNVS---GLLESALARPEQIPFGLEELLLYPDLDRE-- 59

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 493674768  199 vPPEIEAAWLHHRFTQIHPFQDGNGRVARCLASLVC 234
Cdd:pfam02661  60 -HPLEKAAALHFGFAKIHPFRDGNGRTARLLANLFL 94
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
 177-273 9.02e-12

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: 63.70  E-value: 9.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768  177 PEQVASEMD-LLITLHHQHQEQKVPPEIEAAWLHHRFTQIHPFQDGNGRVARCLASLVCIQASWFP-------LVITRDD 248
Cdd:TIGR02613  83 PLQIPSELAiLLDDVRYWLQNGTFSPDEIAIRFHHRLVAIHPFPNGNGRHARLATDLLLEQQGYSPftwgsgsLALVGDL 162

                          90       100
                  ....*....|....*....|....*
gi 493674768  249 RSVYIAALEQADSGDLSSLINlFAK 273
Cdd:TIGR02613 163 RKEYIAALKAADRHDYGPLLE-FAR 186
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
29-317 8.88e-34

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 129.42  E-value: 8.88e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768  29 NEQADRLRQ-SGEFQTFSEKLRREIAIETGIIERlYTIDRGITRLLIEQGINEAliphgstdiPVKQVVSLIKDQEAAIE 107
Cdd:COG3177   12 DEALGRLDGlPEELRELLRKLLIEEAYASSAIEG-NTLTLDEVRSLLEGGLTGG---------PPLRDEREVLNYVEALE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768 108 GLFNFVGGQRnLSTSYIKELHQVLTQSQEStealnpqgkifrVPLIKGDWKRQPNNplrpDGTIHEYCPPEQVASEMDLL 187
Cdd:COG3177   82 YLLELLRGEP-LTEELILELHRILLKGLRG------------EDKEPGEYRTGQVG----IGAVYVPPPPEEVPELMEEL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768 188 ITLHHQhqEQKVPPEIEAAWLHHRFTQIHPFQDGNGRVARCLASLVCIQA------SWFPLVITRDDRSVYIAALEQAD- 260
Cdd:COG3177  145 LDWLNE--EDELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLLRAgllsqpLLPLSRIIEEDRDEYYDALEAVRe 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493674768 261 SGDLSSLINLFAKSQKQAFLRSLGLSEQVLSETRRTQVIVSA-IADKLKQNQLASVQD 317
Cdd:COG3177  223 TGDLTPWIEFFLEAILEAAEEALALLERLLELARGRLNERQRkLLELLFENPVLTASE 280
FIDO COG2184
Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];
174-278 5.85e-16

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


Pssm-ID: 441787 [Multi-domain]  Cd Length: 196  Bit Score: 76.12  E-value: 5.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768 174 YCPPEQVASEM-DLLITLHHQHQEQKVPPE--IE-AAWLHHRFTQIHPFQDGNGRVARCLASLVCIQASWfPLVITRDDR 249
Cdd:COG2184   86 FAPPSFIERELeALFDDLREENYLRGLDREefAErLARFHGELNVIHPFREGNGRTQRLFFDQLARQAGY-PLDWSRVDK 164

                         90       100
                 ....*....|....*....|....*....
gi 493674768 250 SVYIAALEQADSGDLSSLINLFAKSQKQA 278
Cdd:COG2184  165 EEYLEALIAADNGDYSPLKALFRDALTPA 193
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
 119-234 2.88e-15

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: 71.34  E-value: 2.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768  119 LSTSYIKELHQVLTQSQESTEALnpqgkifrvplikgdwkRQPNNPlrpDGTIHEYCPPEQVASEMDLLITLHHQHQEqk 198
Cdd:pfam02661   2 LDLEDLLALHRLLIERHGGAGGA-----------------RDVNVS---GLLESALARPEQIPFGLEELLLYPDLDRE-- 59

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 493674768  199 vPPEIEAAWLHHRFTQIHPFQDGNGRVARCLASLVC 234
Cdd:pfam02661  60 -HPLEKAAALHFGFAKIHPFRDGNGRTARLLANLFL 94
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
 177-273 9.02e-12

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: 63.70  E-value: 9.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493674768  177 PEQVASEMD-LLITLHHQHQEQKVPPEIEAAWLHHRFTQIHPFQDGNGRVARCLASLVCIQASWFP-------LVITRDD 248
Cdd:TIGR02613  83 PLQIPSELAiLLDDVRYWLQNGTFSPDEIAIRFHHRLVAIHPFPNGNGRHARLATDLLLEQQGYSPftwgsgsLALVGDL 162

                          90       100
                  ....*....|....*....|....*
gi 493674768  249 RSVYIAALEQADSGDLSSLINlFAK 273
Cdd:TIGR02613 163 RKEYIAALKAADRHDYGPLLE-FAR 186
 
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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