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Conserved domains on  [gi|169646312|ref|NP_001010825|]
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protein adenylyltransferase FICD [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
198-423 3.33e-62

Fic family protein [Transcription];


:

Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 204.53  E-value: 3.33e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 198 IDSKVKKVMSIPKGSSALRR--VMEEtyyhhIYHTVAIEGNTLTLSEIRHILETRYaVPGKSLEEQNEVIGMHAAMKYIN 275
Cdd:COG3177   11 ADEALGRLDGLPEELRELLRklLIEE-----AYASSAIEGNTLTLDEVRSLLEGGL-TGGPPLRDEREVLNYVEALEYLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 276 TTLVSRigSVTMDDMLEIHRRVLGYV--DPVEAGRFRRTQVLVG-HHIPPHPRDVEKQMQEFTQWLNSEDamNLHPVEFA 352
Cdd:COG3177   85 ELLRGE--PLTEELILELHRILLKGLrgEDKEPGEYRTGQVGIGaVYVPPPPEEVPELMEELLDWLNEED--ELHPLIKA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169646312 353 ALAHYKLVYIHPFIDGNGRTSRLLMNLILMQAG------YPPITIRKEQRSEYYHVLEVANE-GDVRPFIRFIAKCTE 423
Cdd:COG3177  161 AIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGllsqplLPLSRIIEEDRDEYYDALEAVREtGDLTPWIEFFLEAIL 238
NlpI super family cl34822
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
105-184 1.00e-06

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG4785:

Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 49.53  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 105 EAKAALNQALEMKRQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTISPFHEKALVNRDRTL 184
Cdd:COG4785   72 LAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIAL 151
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
198-423 3.33e-62

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 204.53  E-value: 3.33e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 198 IDSKVKKVMSIPKGSSALRR--VMEEtyyhhIYHTVAIEGNTLTLSEIRHILETRYaVPGKSLEEQNEVIGMHAAMKYIN 275
Cdd:COG3177   11 ADEALGRLDGLPEELRELLRklLIEE-----AYASSAIEGNTLTLDEVRSLLEGGL-TGGPPLRDEREVLNYVEALEYLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 276 TTLVSRigSVTMDDMLEIHRRVLGYV--DPVEAGRFRRTQVLVG-HHIPPHPRDVEKQMQEFTQWLNSEDamNLHPVEFA 352
Cdd:COG3177   85 ELLRGE--PLTEELILELHRILLKGLrgEDKEPGEYRTGQVGIGaVYVPPPPEEVPELMEELLDWLNEED--ELHPLIKA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169646312 353 ALAHYKLVYIHPFIDGNGRTSRLLMNLILMQAG------YPPITIRKEQRSEYYHVLEVANE-GDVRPFIRFIAKCTE 423
Cdd:COG3177  161 AIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGllsqplLPLSRIIEEDRDEYYDALEAVREtGDLTPWIEFFLEAIL 238
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
 285-381 2.98e-23

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: 93.68  E-value: 2.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312  285 VTMDDMLEIHRRVLGYVDpvEAGRFRRTQVL-VGHHIPPHPRDVEKQMQEFTQWLNSEDAmnlHPVEFAALAHYKLVYIH 363
Cdd:pfam02661   2 LDLEDLLALHRLLIERHG--GAGGARDVNVSgLLESALARPEQIPFGLEELLLYPDLDRE---HPLEKAAALHFGFAKIH 76

                          90
                  ....*....|....*...
gi 169646312  364 PFIDGNGRTSRLLMNLIL 381
Cdd:pfam02661  77 PFRDGNGRTARLLANLFL 94
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
 285-418 9.39e-17

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: 77.95  E-value: 9.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312  285 VTMDDMLEIHRRVLGYVDPVeAGRFRRTQVLVGHHIPPHPRDVEKQMQEFTQWLNSEDAMnlhPVEFAALAHYKLVYIHP 364
Cdd:TIGR02613  49 LSETFLRRLHRRMFGDVWRW-AGDFRTTQKNIGVSPLQIPSELAILLDDVRYWLQNGTFS---PDEIAIRFHHRLVAIHP 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169646312  365 FIDGNGRTSRLLMNLILMQAGYPPIT-------IRKEQRSEYYHVLEVANEGDVRPFIRFI 418
Cdd:TIGR02613 125 FPNGNGRHARLATDLLLEQQGYSPFTwgsgslaLVGDLRKEYIAALKAADRHDYGPLLEFA 185
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
105-184 1.00e-06

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 49.53  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 105 EAKAALNQALEMKRQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTISPFHEKALVNRDRTL 184
Cdd:COG4785   72 LAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIAL 151
PRK10347 PRK10347
putative adenosine monophosphate-protein transferase Fic;
293-386 8.58e-05

putative adenosine monophosphate-protein transferase Fic;


Pssm-ID: 182396 [Multi-domain]  Cd Length: 200  Bit Score: 43.64  E-value: 8.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 293 IHRRVlgYVDPVE-AGRFRRTQVLVGHHIPPHPRDVEKQMQEFTQWLNSEDAMN-LHPVEFAA-LAHY--KLVYIHPFID 367
Cdd:PRK10347  62 IHRQL--YQDIFDwAGQLREVDIYQGDTPFCHFAYIEKEGNALMQDLEEEGYLVgLEKAKFVErLAHYycEINVLHPFRV 139

                         90
                 ....*....|....*....
gi 169646312 368 GNGRTSRLLMNLILMQAGY 386
Cdd:PRK10347 140 GSGLAQRIFFEQLAIHAGY 158
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 89-180 1.51e-04

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: 44.30  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312   89 AGLLTVKTTASPA-GKLE-AKAALNQALEMK---------------RQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSE 151
Cdd:TIGR02917 125 AELLALRGLAYLGlGQLElAQKSYEQALAIDprslyaklglaqlalAENRFDEARALIDEVLTADPGNVDALLLKGDLLL 204

                          90       100
                  ....*....|....*....|....*....
gi 169646312  152 EDKDIIQADYLYTRALTISPFHEKALVNR 180
Cdd:TIGR02917 205 SLGNIELALAAYRKAIALRPNNIAVLLAL 233
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
198-423 3.33e-62

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 204.53  E-value: 3.33e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 198 IDSKVKKVMSIPKGSSALRR--VMEEtyyhhIYHTVAIEGNTLTLSEIRHILETRYaVPGKSLEEQNEVIGMHAAMKYIN 275
Cdd:COG3177   11 ADEALGRLDGLPEELRELLRklLIEE-----AYASSAIEGNTLTLDEVRSLLEGGL-TGGPPLRDEREVLNYVEALEYLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 276 TTLVSRigSVTMDDMLEIHRRVLGYV--DPVEAGRFRRTQVLVG-HHIPPHPRDVEKQMQEFTQWLNSEDamNLHPVEFA 352
Cdd:COG3177   85 ELLRGE--PLTEELILELHRILLKGLrgEDKEPGEYRTGQVGIGaVYVPPPPEEVPELMEELLDWLNEED--ELHPLIKA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169646312 353 ALAHYKLVYIHPFIDGNGRTSRLLMNLILMQAG------YPPITIRKEQRSEYYHVLEVANE-GDVRPFIRFIAKCTE 423
Cdd:COG3177  161 AIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGllsqplLPLSRIIEEDRDEYYDALEAVREtGDLTPWIEFFLEAIL 238
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
 285-381 2.98e-23

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: 93.68  E-value: 2.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312  285 VTMDDMLEIHRRVLGYVDpvEAGRFRRTQVL-VGHHIPPHPRDVEKQMQEFTQWLNSEDAmnlHPVEFAALAHYKLVYIH 363
Cdd:pfam02661   2 LDLEDLLALHRLLIERHG--GAGGARDVNVSgLLESALARPEQIPFGLEELLLYPDLDRE---HPLEKAAALHFGFAKIH 76

                          90
                  ....*....|....*...
gi 169646312  364 PFIDGNGRTSRLLMNLIL 381
Cdd:pfam02661  77 PFRDGNGRTARLLANLFL 94
FIDO COG2184
Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];
282-422 3.91e-20

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


Pssm-ID: 441787 [Multi-domain]  Cd Length: 196  Bit Score: 88.06  E-value: 3.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 282 IGSVTMDDMLEIHRRVLGYVDPVeAGRFRRTQVLVGHHIPPHPRDVEKQMQEFTQWLNSEDAM-NLHPVEFA-ALAHYK- 358
Cdd:COG2184   48 PGVFDLAHLKAIHRRLFGDVYDW-AGQIRTVNISKGGTRFAPPSFIERELEALFDDLREENYLrGLDREEFAeRLARFHg 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169646312 359 -LVYIHPFIDGNGRTSRLLMNLILMQAGYpPITIRKEQRSEYYHVLEVANEGDVRPFIRFIAKCT 422
Cdd:COG2184  127 eLNVIHPFREGNGRTQRLFFDQLARQAGY-PLDWSRVDKEEYLEALIAADNGDYSPLKALFRDAL 190
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
 285-418 9.39e-17

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: 77.95  E-value: 9.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312  285 VTMDDMLEIHRRVLGYVDPVeAGRFRRTQVLVGHHIPPHPRDVEKQMQEFTQWLNSEDAMnlhPVEFAALAHYKLVYIHP 364
Cdd:TIGR02613  49 LSETFLRRLHRRMFGDVWRW-AGDFRTTQKNIGVSPLQIPSELAILLDDVRYWLQNGTFS---PDEIAIRFHHRLVAIHP 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169646312  365 FIDGNGRTSRLLMNLILMQAGYPPIT-------IRKEQRSEYYHVLEVANEGDVRPFIRFI 418
Cdd:TIGR02613 125 FPNGNGRHARLATDLLLEQQGYSPFTwgsgslaLVGDLRKEYIAALKAADRHDYGPLLEFA 185
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
105-184 1.00e-06

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 49.53  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 105 EAKAALNQALEMKRQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTISPFHEKALVNRDRTL 184
Cdd:COG4785   72 LAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIAL 151
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
105-180 2.17e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.85  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 105 EAKAALNQALEMK---------------RQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTI 169
Cdd:COG0457   26 EAIEDYEKALELDpddaealynlglaylRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALEL 105

                         90
                 ....*....|.
gi 169646312 170 SPFHEKALVNR 180
Cdd:COG0457  106 DPDDAEALYNL 116
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
105-192 7.06e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 47.31  E-value: 7.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 105 EAKAALNQALEMK---------------RQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTI 169
Cdd:COG0457   60 EALADYEQALELDpddaealnnlglalqALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL 139

                         90       100
                 ....*....|....*....|...
gi 169646312 170 SPFHEKALVNRDRTLPLVEEIDQ 192
Cdd:COG0457  140 DPDDADALYNLGIALEKLGRYEE 162
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
118-192 2.02e-05

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 43.24  E-value: 2.02e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169646312 118 RQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQAdYLYTRALTISPFHEKALVNRDRTLPLVEEIDQ 192
Cdd:COG3063    4 KLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEA-IALEKALKLDPNNAEALLNLAELLLELGDYDE 77
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
105-180 6.23e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 44.23  E-value: 6.23e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169646312 105 EAKAALNQALEMKRQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTISPFHEKALVNR 180
Cdd:COG0457    7 DAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNL 82
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 105-171 6.99e-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: 42.30  E-value: 6.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 105 EAKAALNQALEMK---------------RQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTI 169
Cdd:COG4235   35 EALAAYEKALRLDpdnadalldlaeallAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLAL 114


                 ..
gi 169646312 170 SP 171
Cdd:COG4235  115 LP 116
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 118-192 7.08e-05

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: 43.03  E-value: 7.08e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169646312 118 RQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTISPFHEKALVNRDRTLPLVEEIDQ 192
Cdd:COG5010   66 KLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDE 140
PRK10347 PRK10347
putative adenosine monophosphate-protein transferase Fic;
293-386 8.58e-05

putative adenosine monophosphate-protein transferase Fic;


Pssm-ID: 182396 [Multi-domain]  Cd Length: 200  Bit Score: 43.64  E-value: 8.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 293 IHRRVlgYVDPVE-AGRFRRTQVLVGHHIPPHPRDVEKQMQEFTQWLNSEDAMN-LHPVEFAA-LAHY--KLVYIHPFID 367
Cdd:PRK10347  62 IHRQL--YQDIFDwAGQLREVDIYQGDTPFCHFAYIEKEGNALMQDLEEEGYLVgLEKAKFVErLAHYycEINVLHPFRV 139

                         90
                 ....*....|....*....
gi 169646312 368 GNGRTSRLLMNLILMQAGY 386
Cdd:PRK10347 140 GSGLAQRIFFEQLAIHAGY 158
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 105-180 8.72e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 44.98  E-value: 8.72e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169646312 105 EAKAALNQALEMKRQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTISPFHEKALVNR 180
Cdd:COG3914  111 NAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNL 186
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 105-192 1.20e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 44.60  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 105 EAKAALNQALEMK---------------RQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTI 169
Cdd:COG3914  130 EALAALRRALALNpdfaeaylnlgealrRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALEL 209

                         90       100
                 ....*....|....*....|...
gi 169646312 170 SPFHEKALVNRDRTLPLVEEIDQ 192
Cdd:COG3914  210 DPDNADAHSNLLFALRQACDWEV 232
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 89-180 1.51e-04

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: 44.30  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312   89 AGLLTVKTTASPA-GKLE-AKAALNQALEMK---------------RQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSE 151
Cdd:TIGR02917 125 AELLALRGLAYLGlGQLElAQKSYEQALAIDprslyaklglaqlalAENRFDEARALIDEVLTADPGNVDALLLKGDLLL 204

                          90       100
                  ....*....|....*....|....*....
gi 169646312  152 EDKDIIQADYLYTRALTISPFHEKALVNR 180
Cdd:TIGR02917 205 SLGNIELALAAYRKAIALRPNNIAVLLAL 233
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
105-171 7.86e-04

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 38.61  E-value: 7.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 105 EAKAALNQALEMK---------------RQGKRGKAHKlFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTI 169
Cdd:COG3063   10 EAEEYYEKALELDpdnadalnnlgllllEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALEL 88


                 ..
gi 169646312 170 SP 171
Cdd:COG3063   89 DP 90
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 105-171 2.01e-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: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169646312 105 EAKAALNQALEMK---------------RQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTI 169
Cdd:COG5010   72 ESLALLEQALQLDpnnpelyynlallysRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151


                 ..
gi 169646312 170 SP 171
Cdd:COG5010  152 SP 153
DOC_P1 TIGR01550
death-on-curing family protein; The characterized member of this family is the death-on-curing ...
 350-386 2.13e-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: 37.83  E-value: 2.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 169646312  350 EFAALAHYKLVYIHPFIDGNGRTSRLLMNLILMQAGY 386
Cdd:TIGR01550  52 EVSAVLLYALIRSHPFNNANKRTALNALLLFLELNGY 88
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
105-167 3.08e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.22  E-value: 3.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169646312 105 EAKAALNQALEMK---------------RQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRAL 167
Cdd:COG0457   94 EALEDYDKALELDpddaealynlglallELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLE 171
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 105-171 3.57e-03

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: 37.86  E-value: 3.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169646312 105 EAKAALNQALEMKRQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTISP 171
Cdd:COG4783   71 EPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDP 137
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 106-180 5.18e-03

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: 37.09  E-value: 5.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169646312 106 AKAALNQALEMKRQGKRGKAHKLFLHALKMDPGFVDALNEFGIFSEEDKDIIQADYLYTRALTISPFHEKALVNR 180
Cdd:COG4783    4 AEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNL 78
Doc COG3654
Prophage maintenance system killer protein [Mobilome: prophages, transposons];
352-423 7.70e-03

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


Pssm-ID: 442871  Cd Length: 130  Bit Score: 36.38  E-value: 7.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169646312 352 AALAHYkLVYIHPFIDGNGRTSRLLMNLILMQAGYppiTIRKEQRSEYYHVLEVAN-EGDVRPFIRFIAKCTE 423
Cdd:COG3654   58 AALLYG-IAKNHPFVDGNKRTAFAAALVFLDLNGY---ELDADDDEAVDLVLAVAAgELDEEELAAWLRKHLE 126
 
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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