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Conserved domains on  [gi|1995764531|gb|QSH11261|]
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DnaA initiator-associating protein DiaA [Enterobacter hormaechei]

Protein Classification

DnaA initiator-associating protein DiaA( domain architecture ID 10793492)

DnaA initiator-associating protein DiaA is required for the timely initiation of chromosomal replication via direct interactions with the DnaA initiator protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10886 PRK10886
DnaA initiator-associating protein DiaA; Provisional
 1-196 4.08e-150

DnaA initiator-associating protein DiaA; Provisional


:

Pssm-ID: 182811  Cd Length: 196  Bit Score: 413.94  E-value: 4.08e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531   1 MLERIKVCFTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALN 80
Cdd:PRK10886    1 MLERIKVCFTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  81 TDNVVLTAIANDRLHDEIYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLLGPQDVE 160
Cdd:PRK10886   81 TDNVVLTAIANDRLHDEVYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLLGPQDVE 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1995764531 161 IRIPSHRSARIQEMHMLTVNCLCDLIDNTLFPHQDD 196
Cdd:PRK10886  161 IRIPSHRSARIQEMHMLTVNCLCDLIDNTLFPHQDD 196
 
Name Accession Description Interval E-value
PRK10886 PRK10886
DnaA initiator-associating protein DiaA; Provisional
 1-196 4.08e-150

DnaA initiator-associating protein DiaA; Provisional


Pssm-ID: 182811  Cd Length: 196  Bit Score: 413.94  E-value: 4.08e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531   1 MLERIKVCFTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALN 80
Cdd:PRK10886    1 MLERIKVCFTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  81 TDNVVLTAIANDRLHDEIYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLLGPQDVE 160
Cdd:PRK10886   81 TDNVVLTAIANDRLHDEVYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLLGPQDVE 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1995764531 161 IRIPSHRSARIQEMHMLTVNCLCDLIDNTLFPHQDD 196
Cdd:PRK10886  161 IRIPSHRSARIQEMHMLTVNCLCDLIDNTLFPHQDD 196
GmhA COG0279
Phosphoheptose isomerase [Carbohydrate transport and metabolism];
1-192 4.46e-104

Phosphoheptose isomerase [Carbohydrate transport and metabolism];


Pssm-ID: 440048 [Multi-domain]  Cd Length: 189  Bit Score: 297.03  E-value: 4.46e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531   1 MLERIKVCFTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALN 80
Cdd:COG0279     1 MLDRIKQYFEESIEALQALAEALAEAIEAAAELLAEALLNGGKILVCGNGGSAADAQHFAAELVGRFERERPGLPAIALT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  81 TDNVVLTAIANDRLHDEIYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLlgpQDVE 160
Cdd:COG0279    81 TDTSVLTAIANDYGYDEVFARQVEALGRPGDVLLAISTSGNSPNVLRALEAARERGMTTIALTGRDGGKLAGL---ADIE 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1995764531 161 IRIPSHRSARIQEMHMLTVNCLCDLIDNTLFP 192
Cdd:COG0279   158 IRVPSDSTARIQEVHLLIIHILCELIEAALFG 189
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 9-188 1.06e-85

Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).


Pssm-ID: 240139 [Multi-domain]  Cd Length: 177  Bit Score: 250.12  E-value: 1.06e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531   9 FTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALNTDNVVLTA 88
Cdd:cd05006     1 FQESIQLKEALLELLAEAIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEKERPGLPAIALTTDTSILTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  89 IANDRLHDEIYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLlgpQDVEIRIPSHRS 168
Cdd:cd05006    81 IANDYGYEEVFSRQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLEL---ADIEIHVPSDDT 157

                         170       180
                  ....*....|....*....|
gi 1995764531 169 ARIQEMHMLTVNCLCDLIDN 188
Cdd:cd05006   158 PRIQEVHLLIGHILCELVEE 177
gmhA TIGR00441
phosphoheptose isomerase; This model describes phosphoheptose isomerase. Because a closely ...
 31-187 1.84e-58

phosphoheptose isomerase; This model describes phosphoheptose isomerase. Because a closely related paralo in Escherichia coli differs in function (DnaA initiator-associating protein diaA), this model has been rebuilt with a high stringency, and is likely to miss many true examples for phosphoheptose isomerase. Involved in lipopolysaccharide biosynthesis it may have a role in virulence in Haemophilus ducreyi. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 129533  Cd Length: 154  Bit Score: 180.45  E-value: 1.84e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  31 AMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALNTDNVVLTAIANDRLHDEIYAKQVRALGHAG 110
Cdd:TIGR00441   1 VVLLADSFKAGGKVLICGNGGSACDAQHFAAELTGRYRENRPGLPAIALSADVSHLTCVSNDYGYEDVFSRQVEALGQKG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1995764531 111 DVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLlgpQDVEIRIPSHRSARIQEMHMLTVNCLCDLID 187
Cdd:TIGR00441  81 DVLLGISTSGNSKNVLKAIEAAKDKGMKTITLAGKDGGKMAGL---ADIELRVPHFYTPRIQEIHIKVIHILCQLIE 154
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 13-144 3.44e-30

SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.


Pssm-ID: 433326 [Multi-domain]  Cd Length: 138  Bit Score: 107.68  E-value: 3.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  13 IQTQIAAAEAlpDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALNTDNVVLTAIAND 92
Cdd:pfam13580   9 LLERVVETQA--DAIEKAADLIAASLANGGKVYAFGTGHSAAPAEELFARAGGLAGFEPILLPALALHTDASATISTALE 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1995764531  93 RlhDEIYAKQVRAL--GHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTG 144
Cdd:pfam13580  87 R--DEGYARQILALypGRPGDVLIVISNSGINAVPVEAALEAKERGMKVIALTS 138
 
Name Accession Description Interval E-value
PRK10886 PRK10886
DnaA initiator-associating protein DiaA; Provisional
 1-196 4.08e-150

DnaA initiator-associating protein DiaA; Provisional


Pssm-ID: 182811  Cd Length: 196  Bit Score: 413.94  E-value: 4.08e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531   1 MLERIKVCFTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALN 80
Cdd:PRK10886    1 MLERIKVCFTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  81 TDNVVLTAIANDRLHDEIYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLLGPQDVE 160
Cdd:PRK10886   81 TDNVVLTAIANDRLHDEVYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLLGPQDVE 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1995764531 161 IRIPSHRSARIQEMHMLTVNCLCDLIDNTLFPHQDD 196
Cdd:PRK10886  161 IRIPSHRSARIQEMHMLTVNCLCDLIDNTLFPHQDD 196
GmhA COG0279
Phosphoheptose isomerase [Carbohydrate transport and metabolism];
1-192 4.46e-104

Phosphoheptose isomerase [Carbohydrate transport and metabolism];


Pssm-ID: 440048 [Multi-domain]  Cd Length: 189  Bit Score: 297.03  E-value: 4.46e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531   1 MLERIKVCFTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALN 80
Cdd:COG0279     1 MLDRIKQYFEESIEALQALAEALAEAIEAAAELLAEALLNGGKILVCGNGGSAADAQHFAAELVGRFERERPGLPAIALT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  81 TDNVVLTAIANDRLHDEIYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLlgpQDVE 160
Cdd:COG0279    81 TDTSVLTAIANDYGYDEVFARQVEALGRPGDVLLAISTSGNSPNVLRALEAARERGMTTIALTGRDGGKLAGL---ADIE 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1995764531 161 IRIPSHRSARIQEMHMLTVNCLCDLIDNTLFP 192
Cdd:COG0279   158 IRVPSDSTARIQEVHLLIIHILCELIEAALFG 189
PRK13936 PRK13936
phosphoheptose isomerase; Provisional
 1-195 2.89e-98

phosphoheptose isomerase; Provisional


Pssm-ID: 237567  Cd Length: 197  Bit Score: 282.70  E-value: 2.89e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531   1 MLERIKVCFTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALN 80
Cdd:PRK13936    3 LQSRIRQHFEDSIDTKQQAMEVLAPPIAQAVELMVQALLNEGKILACGNGGSAADAQHFSAELLNRFERERPSLPAIALT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  81 TDNVVLTAIANDRLHDEIYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLLGPQDVE 160
Cdd:PRK13936   83 TDTSTLTAIANDYSYNEVFSKQVRALGQPGDVLLAISTSGNSANVIQAIQAAHEREMHVVALTGRDGGKMASLLLPEDVE 162

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1995764531 161 IRIPSHRSARIQEMHMLTVNCLCDLIDNTLFPHQD 195
Cdd:PRK13936  163 IRVPAERTARIQEVHLLAIHCLCDLIDSQLLGSEE 197
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 9-188 1.06e-85

Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).


Pssm-ID: 240139 [Multi-domain]  Cd Length: 177  Bit Score: 250.12  E-value: 1.06e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531   9 FTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALNTDNVVLTA 88
Cdd:cd05006     1 FQESIQLKEALLELLAEAIEQAAQLLAEALLNGGKILICGNGGSAADAQHFAAELVKRFEKERPGLPAIALTTDTSILTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  89 IANDRLHDEIYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLlgpQDVEIRIPSHRS 168
Cdd:cd05006    81 IANDYGYEEVFSRQVEALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLEL---ADIEIHVPSDDT 157

                         170       180
                  ....*....|....*....|
gi 1995764531 169 ARIQEMHMLTVNCLCDLIDN 188
Cdd:cd05006   158 PRIQEVHLLIGHILCELVEE 177
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
 5-192 4.19e-73

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 218.57  E-value: 4.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531   5 IKVCFTESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALNTDNV 84
Cdd:PRK13937    2 ITKHFRESQAVMEAFLESLLEAIAKVAEALIEALANGGKILLCGNGGSAADAQHIAAELVGRFKKERPALPAIALTTDTS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  85 VLTAIANDRLHDEIYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLLgpqDVEIRIP 164
Cdd:PRK13937   82 ALTAIGNDYGFERVFSRQVEALGRPGDVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELC---DHLLIVP 158

                         170       180
                  ....*....|....*....|....*...
gi 1995764531 165 SHRSARIQEMHMLTVNCLCDLIDNTLFP 192
Cdd:PRK13937  159 SDDTPRIQEMHITIGHILCDLVERALFE 186
gmhA TIGR00441
phosphoheptose isomerase; This model describes phosphoheptose isomerase. Because a closely ...
 31-187 1.84e-58

phosphoheptose isomerase; This model describes phosphoheptose isomerase. Because a closely related paralo in Escherichia coli differs in function (DnaA initiator-associating protein diaA), this model has been rebuilt with a high stringency, and is likely to miss many true examples for phosphoheptose isomerase. Involved in lipopolysaccharide biosynthesis it may have a role in virulence in Haemophilus ducreyi. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 129533  Cd Length: 154  Bit Score: 180.45  E-value: 1.84e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  31 AMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALNTDNVVLTAIANDRLHDEIYAKQVRALGHAG 110
Cdd:TIGR00441   1 VVLLADSFKAGGKVLICGNGGSACDAQHFAAELTGRYRENRPGLPAIALSADVSHLTCVSNDYGYEDVFSRQVEALGQKG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1995764531 111 DVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLlgpQDVEIRIPSHRSARIQEMHMLTVNCLCDLID 187
Cdd:TIGR00441  81 DVLLGISTSGNSKNVLKAIEAAKDKGMKTITLAGKDGGKMAGL---ADIELRVPHFYTPRIQEIHIKVIHILCQLIE 154
gmhA PRK00414
D-sedoheptulose 7-phosphate isomerase;
2-187 1.17e-51

D-sedoheptulose 7-phosphate isomerase;


Pssm-ID: 179012 [Multi-domain]  Cd Length: 192  Bit Score: 164.52  E-value: 1.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531   2 LERIKVCFTESIQT--QIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIAL 79
Cdd:PRK00414    3 QDLIRNELNEAAETlaNFLKDDANIHAIQRAAVLIADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  80 nTDNVVLTAIANDRLHDEIYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLlgpQDV 159
Cdd:PRK00414   83 -SDVSHLSCVSNDFGYDYVFSRYVEAVGREGDVLLGISTSGNSGNIIKAIEAARAKGMKVITLTGKDGGKMAGL---ADI 158

                         170       180
                  ....*....|....*....|....*....
gi 1995764531 160 EIRIPSHRSA-RIQEMHMLTVNCLCDLID 187
Cdd:PRK00414  159 EIRVPHFGYAdRIQEIHIKVIHILIQLIE 187
PRK13938 PRK13938
phosphoheptose isomerase; Provisional
 10-194 2.59e-35

phosphoheptose isomerase; Provisional


Pssm-ID: 139997 [Multi-domain]  Cd Length: 196  Bit Score: 122.92  E-value: 2.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  10 TESIQTQIAAAEALPDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALNTDNVVLTAI 89
Cdd:PRK13938   14 TIAVKTRILNDRVLLEAARAIGDRLIAGYRAGARVFMCGNGGSAADAQHFAAELTGHLIFDRPPLGAEALHANSSHLTAV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  90 ANDRLHDEIYAKQVRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLlgpQDVEIRIPSHRSA 169
Cdd:PRK13938   94 ANDYDYDTVFARALEGSARPGDTLFAISTSGNSMSVLRAAKTARELGVTVVAMTGESGGQLAEF---ADFLINVPSRDTG 170

                         170       180
                  ....*....|....*....|....*.
gi 1995764531 170 RIQEMHMLTVNCLCDLIDNTLF-PHQ 194
Cdd:PRK13938  171 RIQESHIVFIHAISEHVEHALFaPRQ 196
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 13-144 3.44e-30

SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.


Pssm-ID: 433326 [Multi-domain]  Cd Length: 138  Bit Score: 107.68  E-value: 3.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  13 IQTQIAAAEAlpDAISRAAMTLVQSLLNGNKILCCGNGTSAANAQHFAASMINRFETERPSLPAIALNTDNVVLTAIAND 92
Cdd:pfam13580   9 LLERVVETQA--DAIEKAADLIAASLANGGKVYAFGTGHSAAPAEELFARAGGLAGFEPILLPALALHTDASATISTALE 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1995764531  93 RlhDEIYAKQVRAL--GHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTG 144
Cdd:pfam13580  87 R--DEGYARQILALypGRPGDVLIVISNSGINAVPVEAALEAKERGMKVIALTS 138
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 9-151 7.36e-10

DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 56.86  E-value: 7.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531   9 FTESIQTQIAAAEALPDAISRAAMT-LVQSLLNGNKILCCGNGTSAANAQHFAA--SMINRfeterpslPAIALNTDNvv 85
Cdd:COG1737   101 LAKVLEAEIANLEETLELLDEEALErAVDLLAKARRIYIFGVGASAPVAEDLAYklLRLGK--------NVVLLDGDG-- 170

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1995764531  86 ltaiandrlhdEIYAKQVRALGhAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELA 151
Cdd:COG1737   171 -----------HLQAESAALLG-PGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLA 224
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 35-151 2.86e-07

RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.


Pssm-ID: 240144 [Multi-domain]  Cd Length: 139  Bit Score: 47.61  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  35 VQSLLNGNKILCCGNGTSAANAQHFA--ASMINrfeterpsLPAIALNTDNVVLTAIANDRlhdeiyakqvralghAGDV 112
Cdd:cd05013     7 VDLLAKARRIYIFGVGSSGLVAEYLAykLLRLG--------KPVVLLSDPHLQLMSAANLT---------------PGDV 63

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1995764531 113 LLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELA 151
Cdd:cd05013    64 VIAISFSGETKETVEAAEIAKERGAKVIAITDSANSPLA 102
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 13-153 1.24e-06

Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441824 [Multi-domain]  Cd Length: 336  Bit Score: 47.59  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  13 IQTQIAAAEALPDAISRAAMTLVQSLLNGN--KILCCGNGTSAANAQHFAasminrfeterpslPAIALNTDNVVLTAIA 90
Cdd:COG2222     4 IAQQPEAWRRALAALAAAIAALLARLRAKPprRVVLVGAGSSDHAAQAAA--------------YLLERLLGIPVAALAP 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1995764531  91 NDRLHDEIYakqvraLGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGL 153
Cdd:COG2222    70 SELVVYPAY------LKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEA 126
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 43-169 4.47e-05

KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.


Pssm-ID: 240145 [Multi-domain]  Cd Length: 128  Bit Score: 41.37  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  43 KILCCGNGTSAANAQHFAASMInrfeterpSL--PAIALNtdnvvltaiANDRLH-DeiyakqvraLGH--AGDVLLAIS 117
Cdd:cd05014     2 KVVVTGVGKSGHIARKIAATLS--------STgtPAFFLH---------PTEALHgD---------LGMvtPGDVVIAIS 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1995764531 118 TRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLlgpQDVEIRIPSHRSA 169
Cdd:cd05014    56 NSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKL---SDVVLDLPVEEEA 104
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 16-151 1.03e-04

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 41.89  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  16 QIAAAEALPDAISraamtLVQSLLNGNKILCCGNGTSAAnaqhfAASMINRFETERPSLPAIALNTDNVvltaiandrlh 95
Cdd:PRK08674   14 QFEEALEIAISLD-----LEEDLEKIDNIVISGMGGSGI-----GGDLLRILLFDELKVPVFVNRDYTL----------- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1995764531  96 deiyakqvRALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGydGGELA 151
Cdd:PRK08674   73 --------PAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKIIAITS--GGKLK 118
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 11-144 1.43e-04

D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440557 [Multi-domain]  Cd Length: 317  Bit Score: 41.50  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  11 ESIQTQIAAAEALPDAISRAAMTLVQSLLN-GNKILCCGNGTSAANAQHFAASMINrfeTERPSL---PAIALNTDnvvl 86
Cdd:COG0794    13 EVLEIEAEALAALAERLDESFEKAVELILNcKGRVVVTGMGKSGHIARKIAATLAS---TGTPAFflhPAEASHGD---- 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  87 taiandrlhdeiyakqvraLG--HAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTG 144
Cdd:COG0794    86 -------------------LGmiTPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITG 126
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 108-164 3.98e-04

Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.


Pssm-ID: 240138 [Multi-domain]  Cd Length: 179  Bit Score: 39.48  E-value: 3.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1995764531 108 HAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLLgpqDVEIRIP 164
Cdd:cd05005    74 GPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLA---DVVVVIP 127
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
105-177 5.29e-04

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 39.74  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531 105 ALGHAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELAGLlgpQDVEIRIPSHRS--------ARIQEMHM 176
Cdd:PRK11337  183 ALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKL---ADYVICSTAQGSpllgenaaARIAQLNI 259


                  .
gi 1995764531 177 L 177
Cdd:PRK11337  260 L 260
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 43-178 1.05e-03

The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.


Pssm-ID: 240148 [Multi-domain]  Cd Length: 119  Bit Score: 37.24  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  43 KILCCGNGTSAAnaqhfAASMINRFETERPSLPAIALNTDNVVLTAiandrlhdeiyakqvralgHAGDVLLAISTRGNS 122
Cdd:cd05017     1 NIVILGMGGSGI-----GGDLLESLLLDEAKIPVYVVKDYTLPAFV-------------------DRKTLVIAVSYSGNT 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1995764531 123 RDIVKAVEAAVTRDMTIVALTgyDGGELAGLLGPQDVE-IRIPSHRSARIQEMHMLT 178
Cdd:cd05017    57 EETLSAVEQAKERGAKIVAIT--SGGKLLEMAREHGVPvIIIPKGLQPRAAFPYLFT 111
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 43-151 3.18e-03

SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.


Pssm-ID: 240141 [Multi-domain]  Cd Length: 126  Bit Score: 36.32  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  43 KILCCGNGTSAaNAQHFAASMINRFeterpslpaialnTDNVVLTAIANDRLHDeiyakqvRALGHAGDVLLAISTRGNS 122
Cdd:cd05008     1 RILIVGCGTSY-HAALVAKYLLERL-------------AGIPVEVEAASEFRYR-------RPLLDEDTLVIAISQSGET 59

                          90       100
                  ....*....|....*....|....*....
gi 1995764531 123 RDIVKAVEAAVTRDMTIVALTGYDGGELA 151
Cdd:cd05008    60 ADTLAALRLAKEKGAKTVAITNVVGSTLA 88
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 44-143 3.51e-03

SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.


Pssm-ID: 240112 [Multi-domain]  Cd Length: 87  Bit Score: 35.43  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  44 ILCCGNGTSAANAQHFAASMINRFeterpSLPAIALNTDNvvltaiandrlhdEIYAKQVRALGhAGDVLLAISTRGNSR 123
Cdd:cd04795     1 IFVIGIGGSGAIAAYFALELLELT-----GIEVVALIATE-------------LEHASLLSLLR-KGDVVIALSYSGRTE 61

                          90       100
                  ....*....|....*....|
gi 1995764531 124 DIVKAVEAAVTRDMTIVALT 143
Cdd:cd04795    62 ELLAALEIAKELGIPVIAIT 81
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 110-151 3.70e-03

SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 36.12  E-value: 3.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1995764531 110 GDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGYDGGELA 151
Cdd:pfam01380  54 DDLVIAISYSGETKDLLAAAELAKARGAKIIAITDSPGSPLA 95
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
13-145 4.02e-03

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 37.05  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764531  13 IQTQIAAAEALPDAISRAAMT-LVQSLLNGNKILCCGNGTSAANAQHFAASMINrfeterpslpaIALNtdnvvltAIAN 91
Cdd:PRK11557   99 IKENTAAMRATLDVNSEEKLHeCVTMLRSARRIILTGIGASGLVAQNFAWKLMK-----------IGIN-------AVAE 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1995764531  92 DRLHDEIYAkqVRALGhAGDVLLAISTRGNSRDIVKAVEAAVTRDMTIVALTGY 145
Cdd:PRK11557  161 RDMHALLAT--VQALS-PDDLLLAISYSGERRELNLAADEALRVGAKVLAITGF 211
 
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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