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Conserved domains on  [gi|1610765755|ref|WP_135385256|]
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MULTISPECIES: Fic family protein [unclassified Escherichia]

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];
85-417 3.23e-67

Fic family protein [Transcription];


:

Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 216.86  E-value: 3.23e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755  85 TPVIAEACELVDKHATAL-ALKDQTERLRgagaelSQLRLEEPITSSQLEGANTTTLVARKMLETGR--APRTEDEHMIA 161
Cdd:COG3177     1 TPELLKLLAEADEALGRLdGLPEELRELL------RKLLIEEAYASSAIEGNTLTLDEVRSLLEGGLtgGPPLRDEREVL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755 162 GNARLMAEIPQLLTEQ-LTPALIRQLHAIGMGGINDAKYRPGEFReTDDVviadyDGNIVHQPPAAALLPERLEKVCQWL 240
Cdd:COG3177    75 NYVEALEYLLELLRGEpLTEELILELHRILLKGLRGEDKEPGEYR-TGQV-----GIGAVYVPPPPEEVPELMEELLDWL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755 241 NShEGYIHPLVRACILHFMLAHEHPFRDGNGRTSRALFYWYMLKSGYDVFKYISISRLLHVVPVKYAASYQYTESDGmDL 320
Cdd:COG3177   149 NE-EDELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGLLSQPLLPLSRIIEEDRDEYYDALEAVRETG-DL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755 321 TYFLEYQAGVIKRAVQNWQQHIDEIMQRSAKldrllfssgvlrRLNPRQVTLLNVMLANPgkEYTVSETSASLGVSDNTA 400
Cdd:COG3177   227 TPWIEFFLEAILEAAEEALALLERLLELARG------------RLNERQRKLLELLFENP--VLTASELAELLGVSRRTA 292
                         330
                  ....*....|....*..
gi 1610765755 401 RTDLRTIVKEGFAQEKK 417
Cdd:COG3177   293 RRDLKDLVELGILEKVG 309
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
85-417 3.23e-67

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 216.86  E-value: 3.23e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755  85 TPVIAEACELVDKHATAL-ALKDQTERLRgagaelSQLRLEEPITSSQLEGANTTTLVARKMLETGR--APRTEDEHMIA 161
Cdd:COG3177     1 TPELLKLLAEADEALGRLdGLPEELRELL------RKLLIEEAYASSAIEGNTLTLDEVRSLLEGGLtgGPPLRDEREVL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755 162 GNARLMAEIPQLLTEQ-LTPALIRQLHAIGMGGINDAKYRPGEFReTDDVviadyDGNIVHQPPAAALLPERLEKVCQWL 240
Cdd:COG3177    75 NYVEALEYLLELLRGEpLTEELILELHRILLKGLRGEDKEPGEYR-TGQV-----GIGAVYVPPPPEEVPELMEELLDWL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755 241 NShEGYIHPLVRACILHFMLAHEHPFRDGNGRTSRALFYWYMLKSGYDVFKYISISRLLHVVPVKYAASYQYTESDGmDL 320
Cdd:COG3177   149 NE-EDELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGLLSQPLLPLSRIIEEDRDEYYDALEAVRETG-DL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755 321 TYFLEYQAGVIKRAVQNWQQHIDEIMQRSAKldrllfssgvlrRLNPRQVTLLNVMLANPgkEYTVSETSASLGVSDNTA 400
Cdd:COG3177   227 TPWIEFFLEAILEAAEEALALLERLLELARG------------RLNERQRKLLELLFENP--VLTASELAELLGVSRRTA 292
                         330
                  ....*....|....*..
gi 1610765755 401 RTDLRTIVKEGFAQEKK 417
Cdd:COG3177   293 RRDLKDLVELGILEKVG 309
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
178-282 1.37e-17

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: 77.50  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755 178 LTPALIRQLHAIgmggINDAKYRPGEFRETDdvviadYDGNIVHQPPAAALLPERLEKVCQWLNSHEgyIHPLVRACILH 257
Cdd:pfam02661   2 LDLEDLLALHRL----LIERHGGAGGARDVN------VSGLLESALARPEQIPFGLEELLLYPDLDR--EHPLEKAAALH 69
                          90       100
                  ....*....|....*....|....*
gi 1610765755 258 FMLAHEHPFRDGNGRTSRALFYWYM 282
Cdd:pfam02661  70 FGFAKIHPFRDGNGRTARLLANLFL 94
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
85-417 3.23e-67

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 216.86  E-value: 3.23e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755  85 TPVIAEACELVDKHATAL-ALKDQTERLRgagaelSQLRLEEPITSSQLEGANTTTLVARKMLETGR--APRTEDEHMIA 161
Cdd:COG3177     1 TPELLKLLAEADEALGRLdGLPEELRELL------RKLLIEEAYASSAIEGNTLTLDEVRSLLEGGLtgGPPLRDEREVL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755 162 GNARLMAEIPQLLTEQ-LTPALIRQLHAIGMGGINDAKYRPGEFReTDDVviadyDGNIVHQPPAAALLPERLEKVCQWL 240
Cdd:COG3177    75 NYVEALEYLLELLRGEpLTEELILELHRILLKGLRGEDKEPGEYR-TGQV-----GIGAVYVPPPPEEVPELMEELLDWL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755 241 NShEGYIHPLVRACILHFMLAHEHPFRDGNGRTSRALFYWYMLKSGYDVFKYISISRLLHVVPVKYAASYQYTESDGmDL 320
Cdd:COG3177   149 NE-EDELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGLLSQPLLPLSRIIEEDRDEYYDALEAVRETG-DL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755 321 TYFLEYQAGVIKRAVQNWQQHIDEIMQRSAKldrllfssgvlrRLNPRQVTLLNVMLANPgkEYTVSETSASLGVSDNTA 400
Cdd:COG3177   227 TPWIEFFLEAILEAAEEALALLERLLELARG------------RLNERQRKLLELLFENP--VLTASELAELLGVSRRTA 292
                         330
                  ....*....|....*..
gi 1610765755 401 RTDLRTIVKEGFAQEKK 417
Cdd:COG3177   293 RRDLKDLVELGILEKVG 309
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
178-282 1.37e-17

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: 77.50  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755 178 LTPALIRQLHAIgmggINDAKYRPGEFRETDdvviadYDGNIVHQPPAAALLPERLEKVCQWLNSHEgyIHPLVRACILH 257
Cdd:pfam02661   2 LDLEDLLALHRL----LIERHGGAGGARDVN------VSGLLESALARPEQIPFGLEELLLYPDLDR--EHPLEKAAALH 69
                          90       100
                  ....*....|....*....|....*
gi 1610765755 258 FMLAHEHPFRDGNGRTSRALFYWYM 282
Cdd:pfam02661  70 FGFAKIHPFRDGNGRTARLLANLFL 94
FIDO COG2184
Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];
164-289 3.51e-06

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


Pssm-ID: 441787 [Multi-domain]  Cd Length: 196  Bit Score: 47.23  E-value: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610765755 164 ARLMAEI-PQLLTEQLTPALIRQLHAIGMGGIND-AkyrpGEFRETDdvvIadYDGNIVHQPPAaaLLPERLEKVCQWLN 241
Cdd:COG2184    36 ALRAAELfERPPPGVFDLAHLKAIHRRLFGDVYDwA----GQIRTVN---I--SKGGTRFAPPS--FIERELEALFDDLR 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1610765755 242 --------SHEGYIHplvRACILHFMLAHEHPFRDGNGRTSRALFYWYMLKSGYDV 289
Cdd:COG2184   105 eenylrglDREEFAE---RLARFHGELNVIHPFREGNGRTQRLFFDQLARQAGYPL 157
 
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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