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Conserved domains on  [gi|544825867|ref|WP_021241864|]
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MULTISPECIES: MurR/RpiR family transcriptional regulator [Enterobacter]

Protein Classification

MurR/RpiR family transcriptional regulator( domain architecture ID 11448252)

MurR/RpiR family transcriptional regulator similar to Escherichia coli MurR, which represses the expression of the murPQ operon involved in the uptake and degradation of N-acetylmuramic acid

CATH:  1.10.10.10
Gene Ontology:  GO:0006355|GO:0003700|GO:0003677
PubMed:  15808743|8576032
SCOP:  4000148

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 5-233 3.89e-51

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


:

Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 168.57  E-value: 3.89e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867   5 LATLLTRGASLTRAEYRVLAHLTEHPLLVGNITVRELAQATFVSTATIMRLCQKLGFSGFSEFIWHCKQLLSDTPHIAAQ 84
Cdd:COG1737    8 LERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSYER 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  85 AQSRPE-------LPVLFNQFIANYQHTFQWVTQDKRQQFSDLLRQKESFFLYGAGFSYLFAEYLTKKLQVMGKTA-FIS 156
Cdd:COG1737   88 LRRLSPddslediLAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVvLLD 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825867 157 GPGDSRNIFLSNAARYQVFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASANTLAEMADVHFALYDEAVHFAAEA 233
Cdd:COG1737  168 GDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRSSA 244
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 5-233 3.89e-51

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 168.57  E-value: 3.89e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867   5 LATLLTRGASLTRAEYRVLAHLTEHPLLVGNITVRELAQATFVSTATIMRLCQKLGFSGFSEFIWHCKQLLSDTPHIAAQ 84
Cdd:COG1737    8 LERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSYER 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  85 AQSRPE-------LPVLFNQFIANYQHTFQWVTQDKRQQFSDLLRQKESFFLYGAGFSYLFAEYLTKKLQVMGKTA-FIS 156
Cdd:COG1737   88 LRRLSPddslediLAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVvLLD 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825867 157 GPGDSRNIFLSNAARYQVFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASANTLAEMADVHFALYDEAVHFAAEA 233
Cdd:COG1737  168 GDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRSSA 244
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 115-225 7.16e-23

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: 90.75  E-value: 7.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867 115 QQFSDLLRQKESFFLYGAGFSYLFAEYLTKKLQVMGKTAFISGPGDSRNIFLSNAARYQVFIAVSRSGETEQVLDKARIA 194
Cdd:cd05013    4 EKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIA 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 544825867 195 KNVGMTIVAFTRASANTLAEMADVHFALYDE 225
Cdd:cd05013   84 KERGAKVIAITDSANSPLAKLADIVLLVSSE 114
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 120-241 6.36e-14

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: 66.55  E-value: 6.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  120 LLRQKESFFLYGAGFSYLFAEYLTKKLQVMGKTAFISGPGDS-RNIFLSNAARYQVFIAVSRSGETEQVLDKARIAKNVG 198
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASElRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 544825867  199 MTIVAFTRASANTLAEMADVHFAL-YDEAVHFAAEAAGVTSFES 241
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYInAGPETGVASTKSITAQLAA 124
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
1-218 1.42e-13

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 68.63  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867   1 MDNRLATLLTRGA-------SLTRAEYRVLAHLTEHPLLVGNITVRELAQATFVSTATIMRLCQKLGFSGFSEF---IWH 70
Cdd:PRK11337   5 FDSALPNGIGLGPyirmkqeGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLrsaLED 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  71 CKQL--LSDTPHIAAQAQSRPELPVLFNQFIANYQHTFQWVTQDKRQQFSDLLRQKESFFLYGAGFSYLFAEYLTKKLQV 148
Cdd:PRK11337  85 YFSQseQVLHSELSFDDAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLR 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825867 149 MGKTAfisGPGDSRNIFLSNAARYQ---VFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASANTLAEMADV 218
Cdd:PRK11337 165 IGVRC---QAYDDAHIMLMSAALLQegdVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADY 234
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 5-233 3.89e-51

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 168.57  E-value: 3.89e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867   5 LATLLTRGASLTRAEYRVLAHLTEHPLLVGNITVRELAQATFVSTATIMRLCQKLGFSGFSEFIWHCKQLLSDTPHIAAQ 84
Cdd:COG1737    8 LERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSYER 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  85 AQSRPE-------LPVLFNQFIANYQHTFQWVTQDKRQQFSDLLRQKESFFLYGAGFSYLFAEYLTKKLQVMGKTA-FIS 156
Cdd:COG1737   88 LRRLSPddslediLAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVvLLD 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825867 157 GPGDSRNIFLSNAARYQVFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASANTLAEMADVHFALYDEAVHFAAEA 233
Cdd:COG1737  168 GDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRSSA 244
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 115-225 7.16e-23

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: 90.75  E-value: 7.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867 115 QQFSDLLRQKESFFLYGAGFSYLFAEYLTKKLQVMGKTAFISGPGDSRNIFLSNAARYQVFIAVSRSGETEQVLDKARIA 194
Cdd:cd05013    4 EKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIA 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 544825867 195 KNVGMTIVAFTRASANTLAEMADVHFALYDE 225
Cdd:cd05013   84 KERGAKVIAITDSANSPLAKLADIVLLVSSE 114
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 120-241 6.36e-14

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: 66.55  E-value: 6.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  120 LLRQKESFFLYGAGFSYLFAEYLTKKLQVMGKTAFISGPGDS-RNIFLSNAARYQVFIAVSRSGETEQVLDKARIAKNVG 198
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASElRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 544825867  199 MTIVAFTRASANTLAEMADVHFAL-YDEAVHFAAEAAGVTSFES 241
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYInAGPETGVASTKSITAQLAA 124
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 99-218 9.56e-14

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: 67.22  E-value: 9.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  99 IANY-QHTFQWVTQDKRQQFSDLLRQKESFFLYGAGFSYLFAEYLTKKLQVMGKTAFISG--------PGDsrniflsna 169
Cdd:cd05005    7 ILEEiENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGetttpaigPGD--------- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 544825867 170 aryqVFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASANTLAEMADV 218
Cdd:cd05005   78 ----LLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADV 122
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
1-218 1.42e-13

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 68.63  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867   1 MDNRLATLLTRGA-------SLTRAEYRVLAHLTEHPLLVGNITVRELAQATFVSTATIMRLCQKLGFSGFSEF---IWH 70
Cdd:PRK11337   5 FDSALPNGIGLGPyirmkqeGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLrsaLED 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  71 CKQL--LSDTPHIAAQAQSRPELPVLFNQFIANYQHTFQWVTQDKRQQFSDLLRQKESFFLYGAGFSYLFAEYLTKKLQV 148
Cdd:PRK11337  85 YFSQseQVLHSELSFDDAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLR 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825867 149 MGKTAfisGPGDSRNIFLSNAARYQ---VFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASANTLAEMADV 218
Cdd:PRK11337 165 IGVRC---QAYDDAHIMLMSAALLQegdVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADY 234
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
 3-76 5.00e-11

Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best characterized member of this family is Swiss:P39266. RpiR is a regulator of the expression of rpiB gene.


Pssm-ID: 334531 [Multi-domain]  Cd Length: 77  Bit Score: 57.34  E-value: 5.00e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544825867    3 NRLATLLTRGASLTRAEYRVLAHLTEHPLLVGNITVRELAQATFVSTATIMRLCQKLGFSGFSEFIWHCKQLLS 76
Cdd:pfam01418   2 GLLEKIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELA 75
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
14-218 4.11e-10

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 59.54  E-value: 4.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  14 SLTRAEYRVLAHLTEHPLLVGNITVRELAQATFVSTATIMRLCQKLGFSGFSEFIWHCKQLLSDTP-------HIAAQAQ 86
Cdd:PRK14101 353 ALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTGTIpmshsqvHLGDTAT 432

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  87 SRPElPVLFNQFIA--------NYQHTFQWVtqdkrqqfsDLLRQKESFFLYGAGFSYLFAEYLTKK------------- 145
Cdd:PRK14101 433 DFGA-KVLDNTVSAilqlrehlNFEHVEQAI---------DILNNARRIEFYGLGNSNIVAQDAHYKffrfgiptiaygd 502

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544825867 146 LQVMGKTAFISGPGDsrniflsnaaryqVFIAVSRSGETEQVLDKARIAKNVGMTIVAFTraSANT-LAEMADV 218
Cdd:PRK14101 503 LYMQAASAALLGKGD-------------VIVAVSKSGRAPELLRVLDVAMQAGAKVIAIT--SSNTpLAKRATV 561
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
11-238 4.60e-09

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 55.54  E-value: 4.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  11 RGASLTRAEYRVLAHLTEHPLLVGNITVRELAQATFVSTATIMRLCQKLGFSGFSEFiwhcKQLLSDT-------PHIAA 83
Cdd:PRK11557   6 RYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPAL----KLALSEAlasqpepPSVPV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  84 QAQSRPELPV------LFNQFIANYQHTFQWVTQDKRQQFSDLLRQKESFFLYGAGFSYLFAEYLTKKLQVMGKTAFISG 157
Cdd:PRK11557  82 HNQIRGDDPLrlvgekLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAER 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867 158 PGDSRNIFLSNAARYQVFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASANTLAEMADvhFALYDEAVHFAAEAAGVT 237
Cdd:PRK11557 162 DMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRAS--HCLYTIAEEQATRSAAIS 239


                 .
gi 544825867 238 S 238
Cdd:PRK11557 240 S 240
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 174-225 5.43e-07

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: 49.59  E-value: 5.43e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 544825867 174 VFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASANTLAEMADVHFALYDE 225
Cdd:COG0794   94 VVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVE 145
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
5-217 7.88e-07

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 48.93  E-value: 7.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867   5 LATLLTRGASLTRAEYRVLAHLTEHPLLVGNITVRELAQATFVSTATIMRLCQKLGFSGFSEFIWH-------CKQLLSD 77
Cdd:PRK15482   4 LTKIRNAESEFTENEQKIADFLRANVSELKSVSSRKMAKQLGISQSSIVKFAQKLGAQGFTELRMAligeysaSREKTNA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  78 TP-HIAAQAQSRPELPVLFNQF----IANYQHTFQWVTQDKRQQFSDLLRQKESFFLYGAGFSYLFAEYLTKKLQVMGKT 152
Cdd:PRK15482  84 TAlHLHSSITSDDSLEVIARKLnrekELALEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKIGYR 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544825867 153 AFISGPGDSRNIFLSNAARYQVFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASANTLAEMAD 217
Cdd:PRK15482 164 VACEADTHVQATVSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAH 228
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 15-59 4.67e-06

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 42.96  E-value: 4.67e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 544825867   15 LTRAEYRVLAHLTEHPllvgNITVRELAQATFVSTATIMRLCQKL 59
Cdd:pfam12802   3 LTPAQFRVLLALARNP----GLTVAELARRLGISKQTVSRLVKRL 43
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 131-222 1.03e-05

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: 43.64  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867 131 GAGFSY---LFAEYLTKKLqvMGKTAFISGPGDSRNiFLSNAARYQVFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRA 207
Cdd:cd05008    6 GCGTSYhaaLVAKYLLERL--AGIPVEVEAASEFRY-RRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNV 82

                         90
                 ....*....|....*
gi 544825867 208 SANTLAEMADVHFAL 222
Cdd:cd05008   83 VGSTLAREADYVLYL 97
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 128-205 1.48e-05

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: 42.36  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867 128 FLYGAGFSYLFAEYLTKKLQVMGKTA--FISGPGDSRNIFLSNAARYQVFIAVSRSGETEQVLDKARIAKNVGMTIVAFT 205
Cdd:cd04795    2 FVIGIGGSGAIAAYFALELLELTGIEvvALIATELEHASLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAIT 81
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 131-225 3.66e-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: 42.14  E-value: 3.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867 131 GAGFSYLFAEYLTKKLQVMGKTAFISGPGDSRNIFLSNAARYQVFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASAN 210
Cdd:cd05014    7 GVGKSGHIARKIAATLSSTGTPAFFLHPTEALHGDLGMVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNS 86

                         90
                 ....*....|....*
gi 544825867 211 TLAEMADVHFALYDE 225
Cdd:cd05014   87 TLAKLSDVVLDLPVE 101
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
11-59 6.20e-05

DNA-binding transcriptional regulator, MarR family [Transcription];


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 41.88  E-value: 6.20e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 544825867  11 RGASLTRAEYRVLAHLTEHpllvGNITVRELAQATFVSTATIMRLCQKL 59
Cdd:COG1846   32 AELGLTPAQFRVLAALAEA----GGLTQSELAERLGLTKSTVSRLLDRL 76
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 111-222 7.24e-05

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: 43.35  E-value: 7.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867 111 QDKRQQFSDLLRQKESFFLY--GAGFSY---LFAEYLTKKLqvMGKTAFISGPGDsrniFLSNAA----RYQVFIAVSRS 181
Cdd:COG2222   19 AAAIAALLARLRAKPPRRVVlvGAGSSDhaaQAAAYLLERL--LGIPVAALAPSE----LVVYPAylklEGTLVVAISRS 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 544825867 182 GETEQVLDKARIAKNVGMTIVAFTRASANTLAEMADVHFAL 222
Cdd:COG2222   93 GNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPL 133
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 133-220 9.27e-05

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: 42.11  E-value: 9.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867 133 GFSYLFAEYLTKKLQvmgktafisgPGDsrniflsnaaryqVFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASANTL 212
Cdd:cd05006   86 GYEEVFSRQVEALGQ----------PGD-------------VLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKL 142


                 ....*...
gi 544825867 213 AEMADVHF 220
Cdd:cd05006  143 LELADIEI 150
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 175-219 2.25e-04

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 41.89  E-value: 2.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 544825867 175 FIAVSRSGETEQVLDKARIAKNVGMTIVAFTraSANTLAEMADVH 219
Cdd:PRK08674  82 VIAVSYSGNTEETLSAVEQALKRGAKIIAIT--SGGKLKEMAKEH 124
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 15-216 2.41e-04

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 41.52  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  15 LTRAEYRVLAHLTEHPLLVGNITVRELAQATFVSTATIMRLCQKLGFSGFSEFIWHCKQ-LLSDTPHI--AAQAQSRPE- 90
Cdd:PRK11302  14 LSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLAQsLANGTPYVnrNVEEDDSVEa 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825867  91 -LPVLFNQFIANYQHTFQWVTQDKRQQFSDLLRQ--KESFFLYGAGFSY----------------LFAEYLTKKLQVMGk 151
Cdd:PRK11302  94 yTGKIFESAMASLDHARQSLDPSAINRAVDLLTQakKISFFGLGASAAVahdaqnkffrfnvpvvYFDDIVMQRMSCMN- 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544825867 152 tafiSGPGDsrniflsnaaryqVFIAVSRSGETEQVLDKARIAKNVGMTIVAFTraSANT-LAEMA 216
Cdd:PRK11302 173 ----SSDGD-------------VVVLISHTGRTKSLVELAQLARENGATVIAIT--SAGSpLAREA 219
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 174-220 3.54e-04

A subgroup of the 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: 240214 [Multi-domain]  Cd Length: 120  Bit Score: 39.48  E-value: 3.54e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 544825867 174 VFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASANTLAEMADVHF 220
Cdd:cd05710   50 VVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVI 96
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 174-219 7.83e-04

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: 38.40  E-value: 7.83e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 544825867 174 VFIAVSRSGETEQVLDKARIAKNVGMTIVAFTraSANTLAEMADVH 219
Cdd:cd05017   46 LVIAVSYSGNTEETLSAVEQAKERGAKIVAIT--SGGKLLEMAREH 89
PRK13938 PRK13938
phosphoheptose isomerase; Provisional
 175-217 1.38e-03

phosphoheptose isomerase; Provisional


Pssm-ID: 139997 [Multi-domain]  Cd Length: 196  Bit Score: 38.95  E-value: 1.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 544825867 175 FIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASANTLAEMAD 217
Cdd:PRK13938 117 LFAISTSGNSMSVLRAAKTARELGVTVVAMTGESGGQLAEFAD 159
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
 174-218 2.14e-03

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 37.91  E-value: 2.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 544825867 174 VFIAVSRSGETEQVLDKARIAKNVGMTIVAFTRASANTLAEMADV 218
Cdd:PRK13937 109 VLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDH 153
 
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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