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Protein adenylyltransferase fic-1 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
232-500 3.08e-56

Fic family protein [Transcription];


:

Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 190.28  E-value: 3.08e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 232 DRKMLRSVHDLRDEFNHLQHSTALRRMMRETYFL-YVYHTVAIEGNTLSLGQTRAILESGmVIPGKSIREHNEVIGMDAA 310
Cdd:COG3177   1 TPELLKLLAEADEALGRLDGLPEELRELLRKLLIeEAYASSAIEGNTLTLDEVRSLLEGG-LTGGPPLRDEREVLNYVEA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 311 LRFLncsLLSKEHDEISIDDILEMHRRVLGN--ADPVEAGRIRTTQVYVG-RFTPVSPEYVMEQLKDIVDWLNDESTltI 387
Cdd:COG3177  80 LEYL---LELLRGEPLTEELILELHRILLKGlrGEDKEPGEYRTGQVGIGaVYVPPPPEEVPELMEELLDWLNEEDE--L 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 388 DPIERAAIAHYKLVLVHPFTDGNGRTARLLLNLIMMRSG------FPPVILPVETRAEYYASL-HVANLGDLRPFVRYVA 460
Cdd:COG3177 155 HPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGllsqplLPLSRIIEEDRDEYYDALeAVRETGDLTPWIEFFL 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17544594 461 KHSEASIQRYIGAMktssDNILNSGDSKLTPEESEVSEKI 500
Cdd:COG3177 235 EAILEAAEEALALL----ERLLELARGRLNERQRKLLELL 270
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
161-223 1.61e-09

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 55.78  E-value: 1.61e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17544594 161 GNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRAR 223
Cdd:COG4235  31 GRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGL 93
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
232-500 3.08e-56

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 190.28  E-value: 3.08e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 232 DRKMLRSVHDLRDEFNHLQHSTALRRMMRETYFL-YVYHTVAIEGNTLSLGQTRAILESGmVIPGKSIREHNEVIGMDAA 310
Cdd:COG3177   1 TPELLKLLAEADEALGRLDGLPEELRELLRKLLIeEAYASSAIEGNTLTLDEVRSLLEGG-LTGGPPLRDEREVLNYVEA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 311 LRFLncsLLSKEHDEISIDDILEMHRRVLGN--ADPVEAGRIRTTQVYVG-RFTPVSPEYVMEQLKDIVDWLNDESTltI 387
Cdd:COG3177  80 LEYL---LELLRGEPLTEELILELHRILLKGlrGEDKEPGEYRTGQVGIGaVYVPPPPEEVPELMEELLDWLNEEDE--L 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 388 DPIERAAIAHYKLVLVHPFTDGNGRTARLLLNLIMMRSG------FPPVILPVETRAEYYASL-HVANLGDLRPFVRYVA 460
Cdd:COG3177 155 HPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGllsqplLPLSRIIEEDRDEYYDALeAVRETGDLTPWIEFFL 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17544594 461 KHSEASIQRYIGAMktssDNILNSGDSKLTPEESEVSEKI 500
Cdd:COG3177 235 EAILEAAEEALALL----ERLLELARGRLNERQRKLLELL 270
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
326-422 2.11e-21

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: 88.68  E-value: 2.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594   326 ISIDDILEMHRRVLgnADPVEAGRIRTTQVY-VGRFTPVSPEYVMEQLKDIVDWLNDEstlTIDPIERAAIAHYKLVLVH 404
Cdd:pfam02661   2 LDLEDLLALHRLLI--ERHGGAGGARDVNVSgLLESALARPEQIPFGLEELLLYPDLD---REHPLEKAAALHFGFAKIH 76
                          90
                  ....*....|....*...
gi 17544594   405 PFTDGNGRTARLLLNLIM 422
Cdd:pfam02661  77 PFRDGNGRTARLLANLFL 94
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
320-459 2.73e-15

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: 74.10  E-value: 2.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594   320 SKEHDEISIDDILEMHRRVLGNADPVeAGRIRTTQVYVGrftpVSPEYVMEQLK----DIVDWLNDEstlTIDPIERAAI 395
Cdd:TIGR02613  43 RKKKDILSETFLRRLHRRMFGDVWRW-AGDFRTTQKNIG----VSPLQIPSELAilldDVRYWLQNG---TFSPDEIAIR 114
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17544594   396 AHYKLVLVHPFTDGNGRTARLLLNLIMMRSGFPP-------VILPVETRAEYYASLHVANLGDLRPFVRYV 459
Cdd:TIGR02613 115 FHHRLVAIHPFPNGNGRHARLATDLLLEQQGYSPftwgsgsLALVGDLRKEYIAALKAADRHDYGPLLEFA 185
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
161-223 1.61e-09

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 55.78  E-value: 1.61e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17544594 161 GNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRAR 223
Cdd:COG4235  31 GRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGL 93
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
142-222 2.39e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 40.84  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594   142 AKVKEAILAAKAAGRS-RKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVL 220
Cdd:TIGR02917 561 ELNPQEIEPALALAQYyLGKGQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLL 640

                  ..
gi 17544594   221 RA 222
Cdd:TIGR02917 641 LA 642
PRK10347 PRK10347
putative adenosine monophosphate-protein transferase Fic;
347-465 6.13e-03

putative adenosine monophosphate-protein transferase Fic;


Pssm-ID: 182396 [Multi-domain]  Cd Length: 200  Bit Score: 38.25  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594  347 AGRIRTTQVYVGRFTPVSPEYVMEQLKDIVDWLNDESTLTIDPIER--AAIAHY--KLVLVHPFTDGNGRTARLLLNLIM 422
Cdd:PRK10347  74 AGQLREVDIYQGDTPFCHFAYIEKEGNALMQDLEEEGYLVGLEKAKfvERLAHYycEINVLHPFRVGSGLAQRIFFEQLA 153
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 17544594  423 MRSGFPPVILPVETrAEYYASLHVANLGDLRPFVRYVAKH-SEA 465
Cdd:PRK10347 154 IHAGYQLSWQGIEK-EAWNQANQSGAMGDLTALQMIFSKVvSEA 196
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
232-500 3.08e-56

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 190.28  E-value: 3.08e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 232 DRKMLRSVHDLRDEFNHLQHSTALRRMMRETYFL-YVYHTVAIEGNTLSLGQTRAILESGmVIPGKSIREHNEVIGMDAA 310
Cdd:COG3177   1 TPELLKLLAEADEALGRLDGLPEELRELLRKLLIeEAYASSAIEGNTLTLDEVRSLLEGG-LTGGPPLRDEREVLNYVEA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 311 LRFLncsLLSKEHDEISIDDILEMHRRVLGN--ADPVEAGRIRTTQVYVG-RFTPVSPEYVMEQLKDIVDWLNDESTltI 387
Cdd:COG3177  80 LEYL---LELLRGEPLTEELILELHRILLKGlrGEDKEPGEYRTGQVGIGaVYVPPPPEEVPELMEELLDWLNEEDE--L 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 388 DPIERAAIAHYKLVLVHPFTDGNGRTARLLLNLIMMRSG------FPPVILPVETRAEYYASL-HVANLGDLRPFVRYVA 460
Cdd:COG3177 155 HPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGllsqplLPLSRIIEEDRDEYYDALeAVRETGDLTPWIEFFL 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17544594 461 KHSEASIQRYIGAMktssDNILNSGDSKLTPEESEVSEKI 500
Cdd:COG3177 235 EAILEAAEEALALL----ERLLELARGRLNERQRKLLELL 270
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
326-422 2.11e-21

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: 88.68  E-value: 2.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594   326 ISIDDILEMHRRVLgnADPVEAGRIRTTQVY-VGRFTPVSPEYVMEQLKDIVDWLNDEstlTIDPIERAAIAHYKLVLVH 404
Cdd:pfam02661   2 LDLEDLLALHRLLI--ERHGGAGGARDVNVSgLLESALARPEQIPFGLEELLLYPDLD---REHPLEKAAALHFGFAKIH 76
                          90
                  ....*....|....*...
gi 17544594   405 PFTDGNGRTARLLLNLIM 422
Cdd:pfam02661  77 PFRDGNGRTARLLANLFL 94
FIDO COG2184
Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];
327-461 5.15e-19

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


Pssm-ID: 441787 [Multi-domain]  Cd Length: 196  Bit Score: 84.98  E-value: 5.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 327 SIDDILEMHRRVLGNADPVeAGRIRTTQVYVGRFTPVSPEYVMEQLKDIVDWLNDESTLTIDP----IERAAIAHYKLVL 402
Cdd:COG2184  52 DLAHLKAIHRRLFGDVYDW-AGQIRTVNISKGGTRFAPPSFIERELEALFDDLREENYLRGLDreefAERLARFHGELNV 130
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17544594 403 VHPFTDGNGRTARLLLNLIMMRSGFPPVILPVEtRAEYYASLHVANLGDLRPFVRYVAK 461
Cdd:COG2184 131 IHPFREGNGRTQRLFFDQLARQAGYPLDWSRVD-KEEYLEALIAADNGDYSPLKALFRD 188
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
320-459 2.73e-15

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: 74.10  E-value: 2.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594   320 SKEHDEISIDDILEMHRRVLGNADPVeAGRIRTTQVYVGrftpVSPEYVMEQLK----DIVDWLNDEstlTIDPIERAAI 395
Cdd:TIGR02613  43 RKKKDILSETFLRRLHRRMFGDVWRW-AGDFRTTQKNIG----VSPLQIPSELAilldDVRYWLQNG---TFSPDEIAIR 114
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17544594   396 AHYKLVLVHPFTDGNGRTARLLLNLIMMRSGFPP-------VILPVETRAEYYASLHVANLGDLRPFVRYV 459
Cdd:TIGR02613 115 FHHRLVAIHPFPNGNGRHARLATDLLLEQQGYSPftwgsgsLALVGDLRKEYIAALKAADRHDYGPLLEFA 185
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
161-223 1.61e-09

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 55.78  E-value: 1.61e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17544594 161 GNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRAR 223
Cdd:COG4235  31 GRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGL 93
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
142-224 1.26e-07

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 50.58  E-value: 1.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 142 AKVKEAILAAKAAGRSrkdGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLR 221
Cdd:COG4783   2 ACAEALYALAQALLLA---GDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNL 78

                ...
gi 17544594 222 ART 224
Cdd:COG4783  79 GLA 81
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
161-223 3.28e-07

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 49.23  E-value: 3.28e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17544594 161 GNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRAR 223
Cdd:COG4235  65 GDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARLLEAS 127
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
161-256 3.52e-07

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 52.69  E-value: 3.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 161 GNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRARttplvsaidrkMLRSVH 240
Cdd:COG3914 126 GRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGN-----------ALQDLG 194
                        90
                ....*....|....*.
gi 17544594 241 DLRDEFNHLQHSTALR 256
Cdd:COG3914 195 RLEEAIAAYRRALELD 210
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
158-223 5.00e-07

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 49.57  E-value: 5.00e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17544594 158 RKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRAR 223
Cdd:COG5010  65 NKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAA 130
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
158-223 5.58e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 51.27  E-value: 5.58e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17544594 158 RKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRAR 223
Cdd:COG2956 121 EQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAE 186
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
158-223 5.89e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 50.88  E-value: 5.89e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17544594 158 RKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRAR 223
Cdd:COG2956  53 RRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAE 118
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
161-223 9.58e-07

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 48.26  E-value: 9.58e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17544594 161 GNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRAR 223
Cdd:COG4783  52 GDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLAR 114
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
158-223 9.78e-07

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 47.09  E-value: 9.78e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17544594 158 RKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQcYVKALAYDPGNSEALVLRAR 223
Cdd:COG3063   3 LKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAE 67
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
146-224 1.14e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 51.15  E-value: 1.14e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17544594 146 EAILAAKAAGRSRKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRART 224
Cdd:COG3914  77 LAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEA 155
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
161-224 1.82e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 49.23  E-value: 1.82e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17544594 161 GNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRART 224
Cdd:COG0457  56 GRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLA 119
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
158-214 2.30e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 47.11  E-value: 2.30e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17544594 158 RKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGN 214
Cdd:COG4783  83 LKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
161-224 5.51e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 47.69  E-value: 5.51e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17544594 161 GNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRART 224
Cdd:COG0457  90 GRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIA 153
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
158-224 9.10e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 47.31  E-value: 9.10e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17544594 158 RKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRART 224
Cdd:COG0457  19 RRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLA 85
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
165-224 2.44e-05

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 43.84  E-value: 2.44e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 165 RAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRART 224
Cdd:COG4235   1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEA 60
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
158-223 3.43e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 45.49  E-value: 3.43e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17544594 158 RKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRAR 223
Cdd:COG2956  87 LKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAE 152
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
158-223 3.51e-05

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 46.52  E-value: 3.51e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17544594 158 RKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEA--LVLRAR 223
Cdd:COG3914 157 RRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAhsNLLFAL 224
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
145-223 7.49e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 44.72  E-value: 7.49e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17544594 145 KEAILAAKAAGRSRKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRAR 223
Cdd:COG2956 142 ENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAE 220
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
161-212 1.96e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.46  E-value: 1.96e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 17544594 161 GNLERAMTImEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDP 212
Cdd:COG3063  40 GRYDEAIAL-EKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDP 90
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
140-220 2.07e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.10  E-value: 2.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 140 DPAKVKEAILAAKAAgrsRKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALV 219
Cdd:COG2956 174 DPDCARALLLLAELY---LEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLA 250

                .
gi 17544594 220 L 220
Cdd:COG2956 251 L 251
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
161-212 2.29e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 38.79  E-value: 2.29e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 17544594 161 GNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDP 212
Cdd:COG5010 102 GDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
142-222 2.39e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 40.84  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594   142 AKVKEAILAAKAAGRS-RKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVL 220
Cdd:TIGR02917 561 ELNPQEIEPALALAQYyLGKGQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLL 640

                  ..
gi 17544594   221 RA 222
Cdd:TIGR02917 641 LA 642
PRK10347 PRK10347
putative adenosine monophosphate-protein transferase Fic;
347-465 6.13e-03

putative adenosine monophosphate-protein transferase Fic;


Pssm-ID: 182396 [Multi-domain]  Cd Length: 200  Bit Score: 38.25  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594  347 AGRIRTTQVYVGRFTPVSPEYVMEQLKDIVDWLNDESTLTIDPIER--AAIAHY--KLVLVHPFTDGNGRTARLLLNLIM 422
Cdd:PRK10347  74 AGQLREVDIYQGDTPFCHFAYIEKEGNALMQDLEEEGYLVGLEKAKfvERLAHYycEINVLHPFRVGSGLAQRIFFEQLA 153
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 17544594  423 MRSGFPPVILPVETrAEYYASLHVANLGDLRPFVRYVAKH-SEA 465
Cdd:PRK10347 154 IHAGYQLSWQGIEK-EAWNQANQSGAMGDLTALQMIFSKVvSEA 196
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
147-223 8.00e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 38.17  E-value: 8.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17544594 147 AILAAKAAGRSRK------DGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVL 220
Cdd:COG2956   2 LLPVAAALGWYFKglnyllNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE 81

                ...
gi 17544594 221 RAR 223
Cdd:COG2956  82 LAQ 84
 
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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