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Conserved domains on  [gi|2152187294|ref|WP_229095208|]
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MULTISPECIES: Fic family protein [Bacteroides]

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];
2-253 5.29e-65

Fic family protein [Transcription];


:

Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 205.69  E-value: 5.29e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294   2 NEDLKLLLDKADTLKGELSALrplpEDALQKIQDALDIEYTYESNRIEGNTLTLQETALVVNEGVTiSGKSMREHLEAIN 81
Cdd:COG3177     1 TPELLKLLAEADEALGRLDGL----PEELRELLRKLLIEEAYASSAIEGNTLTLDEVRSLLEGGLT-GGPPLRDEREVLN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294  82 HSEAIDYIKDIAKkDIEISERTIKEIHALILHGI--DRENAGKYRTVPVMIsGSTHMPPQPYLIQKQMEDFMIKYRqmEE 159
Cdd:COG3177    76 YVEALEYLLELLR-GEPLTEELILELHRILLKGLrgEDKEPGEYRTGQVGI-GAVYVPPPPEEVPELMEELLDWLN--EE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294 160 EKVHPVLIAAYLHDELVRIHPFIDGNGRTSRLLMNLYLLRNGYTLVTL----KGSNEDKISYYKALEESHTENKPEAFQK 235
Cdd:COG3177   152 DELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGLLSQPLlplsRIIEEDRDEYYDALEAVRETGDLTPWIE 231
                         250
                  ....*....|....*...
gi 2152187294 236 LVVEAEIASLQRYLSIME 253
Cdd:COG3177   232 FFLEAILEAAEEALALLE 249
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
2-253 5.29e-65

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 205.69  E-value: 5.29e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294   2 NEDLKLLLDKADTLKGELSALrplpEDALQKIQDALDIEYTYESNRIEGNTLTLQETALVVNEGVTiSGKSMREHLEAIN 81
Cdd:COG3177     1 TPELLKLLAEADEALGRLDGL----PEELRELLRKLLIEEAYASSAIEGNTLTLDEVRSLLEGGLT-GGPPLRDEREVLN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294  82 HSEAIDYIKDIAKkDIEISERTIKEIHALILHGI--DRENAGKYRTVPVMIsGSTHMPPQPYLIQKQMEDFMIKYRqmEE 159
Cdd:COG3177    76 YVEALEYLLELLR-GEPLTEELILELHRILLKGLrgEDKEPGEYRTGQVGI-GAVYVPPPPEEVPELMEELLDWLN--EE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294 160 EKVHPVLIAAYLHDELVRIHPFIDGNGRTSRLLMNLYLLRNGYTLVTL----KGSNEDKISYYKALEESHTENKPEAFQK 235
Cdd:COG3177   152 DELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGLLSQPLlplsRIIEEDRDEYYDALEAVRETGDLTPWIE 231
                         250
                  ....*....|....*...
gi 2152187294 236 LVVEAEIASLQRYLSIME 253
Cdd:COG3177   232 FFLEAILEAAEEALALLE 249
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
99-197 8.51e-24

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: 92.14  E-value: 8.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294  99 ISERTIKEIHALILHGIdrENAGKYRTVPVmISGSTHMPPQPYLIQKQMEDFMikyRQMEEEKVHPVLIAAYLHDELVRI 178
Cdd:pfam02661   2 LDLEDLLALHRLLIERH--GGAGGARDVNV-SGLLESALARPEQIPFGLEELL---LYPDLDREHPLEKAAALHFGFAKI 75
                          90
                  ....*....|....*....
gi 2152187294 179 HPFIDGNGRTSRLLMNLYL 197
Cdd:pfam02661  76 HPFRDGNGRTARLLANLFL 94
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
77-222 6.85e-07

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: 48.68  E-value: 6.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294  77 LEAINHSEAIDYIKDIAKKDIEI-SERTIKEIHALILHGIDREnAGKYRTVpvmisgSTHMPPQPYLIQKQMEDFM--IK 153
Cdd:TIGR02613  26 FEQANIAEGILWAEGRRRKKKDIlSETFLRRLHRRMFGDVWRW-AGDFRTT------QKNIGVSPLQIPSELAILLddVR 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2152187294 154 YrQMEEEKVHPVLIAAYLHDELVRIHPFIDGNGRTSRLLMNLYLLRNGYTLVT-----LKGSNEDKISYYKALE 222
Cdd:TIGR02613  99 Y-WLQNGTFSPDEIAIRFHHRLVAIHPFPNGNGRHARLATDLLLEQQGYSPFTwgsgsLALVGDLRKEYIAALK 171
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
2-253 5.29e-65

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 205.69  E-value: 5.29e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294   2 NEDLKLLLDKADTLKGELSALrplpEDALQKIQDALDIEYTYESNRIEGNTLTLQETALVVNEGVTiSGKSMREHLEAIN 81
Cdd:COG3177     1 TPELLKLLAEADEALGRLDGL----PEELRELLRKLLIEEAYASSAIEGNTLTLDEVRSLLEGGLT-GGPPLRDEREVLN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294  82 HSEAIDYIKDIAKkDIEISERTIKEIHALILHGI--DRENAGKYRTVPVMIsGSTHMPPQPYLIQKQMEDFMIKYRqmEE 159
Cdd:COG3177    76 YVEALEYLLELLR-GEPLTEELILELHRILLKGLrgEDKEPGEYRTGQVGI-GAVYVPPPPEEVPELMEELLDWLN--EE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294 160 EKVHPVLIAAYLHDELVRIHPFIDGNGRTSRLLMNLYLLRNGYTLVTL----KGSNEDKISYYKALEESHTENKPEAFQK 235
Cdd:COG3177   152 DELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGLLSQPLlplsRIIEEDRDEYYDALEAVRETGDLTPWIE 231
                         250
                  ....*....|....*...
gi 2152187294 236 LVVEAEIASLQRYLSIME 253
Cdd:COG3177   232 FFLEAILEAAEEALALLE 249
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
99-197 8.51e-24

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: 92.14  E-value: 8.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294  99 ISERTIKEIHALILHGIdrENAGKYRTVPVmISGSTHMPPQPYLIQKQMEDFMikyRQMEEEKVHPVLIAAYLHDELVRI 178
Cdd:pfam02661   2 LDLEDLLALHRLLIERH--GGAGGARDVNV-SGLLESALARPEQIPFGLEELL---LYPDLDREHPLEKAAALHFGFAKI 75
                          90
                  ....*....|....*....
gi 2152187294 179 HPFIDGNGRTSRLLMNLYL 197
Cdd:pfam02661  76 HPFRDGNGRTARLLANLFL 94
FIDO COG2184
Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];
75-204 8.55e-20

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


Pssm-ID: 441787 [Multi-domain]  Cd Length: 196  Bit Score: 84.59  E-value: 8.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294  75 EHLEAINHSEAIDYIKDIAKKDIeISERTIKEIHALILHGIDrENAGKYRTVPVMISGSTHMPPQpyLIQKQMEDFMIKY 154
Cdd:COG2184    28 DEAEAELTALRAAELFERPPPGV-FDLAHLKAIHRRLFGDVY-DWAGQIRTVNISKGGTRFAPPS--FIERELEALFDDL 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2152187294 155 RQ-------MEEEKVHpvlIAAYLHDELVRIHPFIDGNGRTSRLLMNLYLLRNGYTL 204
Cdd:COG2184   104 REenylrglDREEFAE---RLARFHGELNVIHPFREGNGRTQRLFFDQLARQAGYPL 157
Doc COG3654
Prophage maintenance system killer protein [Mobilome: prophages, transposons];
166-205 1.12e-07

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


Pssm-ID: 442871  Cd Length: 130  Bit Score: 49.47  E-value: 1.12e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2152187294 166 LIAAYLHdELVRIHPFIDGNGRTSRLLMNLYLLRNGYTLV 205
Cdd:COG3654    56 KAAALLY-GIAKNHPFVDGNKRTAFAAALVFLDLNGYELD 94
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
77-222 6.85e-07

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: 48.68  E-value: 6.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2152187294  77 LEAINHSEAIDYIKDIAKKDIEI-SERTIKEIHALILHGIDREnAGKYRTVpvmisgSTHMPPQPYLIQKQMEDFM--IK 153
Cdd:TIGR02613  26 FEQANIAEGILWAEGRRRKKKDIlSETFLRRLHRRMFGDVWRW-AGDFRTT------QKNIGVSPLQIPSELAILLddVR 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2152187294 154 YrQMEEEKVHPVLIAAYLHDELVRIHPFIDGNGRTSRLLMNLYLLRNGYTLVT-----LKGSNEDKISYYKALE 222
Cdd:TIGR02613  99 Y-WLQNGTFSPDEIAIRFHHRLVAIHPFPNGNGRHARLATDLLLEQQGYSPFTwgsgsLALVGDLRKEYIAALK 171
DOC_P1 TIGR01550
death-on-curing family protein; The characterized member of this family is the death-on-curing ...
168-202 3.09e-03

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: 36.68  E-value: 3.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2152187294 168 AAYLHDELVRIHPFIDGNGRTSRLLMNLYLLRNGY 202
Cdd:TIGR01550  54 SAVLLYALIRSHPFNNANKRTALNALLLFLELNGY 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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