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Conserved domains on  [gi|544677870|ref|WP_021110161|]
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MurR/RpiR family transcriptional regulator [Glaesserella parasuis]

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 ...
 10-274 1.24e-75

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


:

Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 231.74  E-value: 1.24e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  10 FQNEVRKQYDSLSKRLKQVAQYILDNGDSVIFDTVSEIAEKAQVPPSTLIRFANAFGLSGFNDIKQLYRQNLMEGTTSYT 89
Cdd:COG1737    7 LLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSYE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  90 ERVQLfrqiepklnESKGDHTDVLRLFIQGNNQALAQLANQITEEQLEAVTKILDNANRIFIVGLKRSFSIASYLNYALS 169
Cdd:COG1737   87 RLRRL---------SPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 170 HLNYDVFLIDGLGGMFSEQLNRIREGDVVIAISFSPYATETISVLDATARTGVKHIAITDSQLSPLLTFSDVSFIIKEA- 248
Cdd:COG1737  158 RLGKNVVLLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEe 237

                        250       260
                 ....*....|....*....|....*....
gi 544677870 249 ---QISGFRSQCATMTLAQTIAVSLALRK 274
Cdd:COG1737  238 ptlRSSAFSSRVAQLALIDALAAAVAQRD 266
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 10-274 1.24e-75

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 231.74  E-value: 1.24e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  10 FQNEVRKQYDSLSKRLKQVAQYILDNGDSVIFDTVSEIAEKAQVPPSTLIRFANAFGLSGFNDIKQLYRQNLMEGTTSYT 89
Cdd:COG1737    7 LLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSYE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  90 ERVQLfrqiepklnESKGDHTDVLRLFIQGNNQALAQLANQITEEQLEAVTKILDNANRIFIVGLKRSFSIASYLNYALS 169
Cdd:COG1737   87 RLRRL---------SPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 170 HLNYDVFLIDGLGGMFSEQLNRIREGDVVIAISFSPYATETISVLDATARTGVKHIAITDSQLSPLLTFSDVSFIIKEA- 248
Cdd:COG1737  158 RLGKNVVLLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEe 237

                        250       260
                 ....*....|....*....|....*....
gi 544677870 249 ---QISGFRSQCATMTLAQTIAVSLALRK 274
Cdd:COG1737  238 ptlRSSAFSSRVAQLALIDALAAAVAQRD 266
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 134-269 6.86e-30

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: 109.63  E-value: 6.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 134 EQLEAVTKILDNANRIFIVGLKRSFSIASYLNYALSHLNYDVFLIDGLGGMFSEQLNrIREGDVVIAISFSPYATETISV 213
Cdd:cd05013    1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAAN-LTPGDVVIAISFSGETKETVEA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 214 LDATARTGVKHIAITDSQLSPLLTFSDVSFIIKEAQ----ISGFRSQCATMTLAQTIAVS 269
Cdd:cd05013   80 AEIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEgdfrSSAFSSRIAQLALIDALFLA 139
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 142-272 3.88e-20

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: 83.89  E-value: 3.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  142 ILDNANRIFIVGLKRSFSIASYLNYALSHLNYDVFLIDGLGGMFSEQLNRIREGDVVIAISFSPYATETISVLDATARTG 221
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 544677870  222 VKHIAITDSQLSPLLTFSDVSFIIKEAQISGFRSqcaTMTL-AQTIAVSLAL 272
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPETGVAS---TKSItAQLAALDALA 129
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
13-276 1.58e-18

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 84.97  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  13 EVRKQYDSLSKRLKQVAQYILDNGDSVIFDTVSEIAEKAQVPPSTLIRFANAFGLSGFNDIKqLYRQNLMEGTTSYTER- 91
Cdd:PRK14101 346 RIRQMRDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFK-LKLATGLTGTIPMSHSq 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  92 VQLfrqiepklneskGD-HTDVLRLFIQGNNQALAQLANQITEEQLEAVTKILDNANRIFIVGLKRSFSIASYLNYALSH 170
Cdd:PRK14101 425 VHL------------GDtATDFGAKVLDNTVSAILQLREHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFR 492

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 171 LNYDVFLIDGLgGMFSEQLNRIREGDVVIAISFSPYATETISVLDATARTGVKHIAITdSQLSPLLTFSDVSFI-----I 245
Cdd:PRK14101 493 FGIPTIAYGDL-YMQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAIT-SSNTPLAKRATVALEtdhieM 570

                        250       260       270
                 ....*....|....*....|....*....|.
gi 544677870 246 KEAQISgFRSQCATMTLAQTIAVSLALRKAS 276
Cdd:PRK14101 571 RESQLS-MISRILHLVMIDILAVGVAIRRAA 600
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 10-274 1.24e-75

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 231.74  E-value: 1.24e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  10 FQNEVRKQYDSLSKRLKQVAQYILDNGDSVIFDTVSEIAEKAQVPPSTLIRFANAFGLSGFNDIKQLYRQNLMEGTTSYT 89
Cdd:COG1737    7 LLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSSYE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  90 ERVQLfrqiepklnESKGDHTDVLRLFIQGNNQALAQLANQITEEQLEAVTKILDNANRIFIVGLKRSFSIASYLNYALS 169
Cdd:COG1737   87 RLRRL---------SPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 170 HLNYDVFLIDGLGGMFSEQLNRIREGDVVIAISFSPYATETISVLDATARTGVKHIAITDSQLSPLLTFSDVSFIIKEA- 248
Cdd:COG1737  158 RLGKNVVLLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEe 237

                        250       260
                 ....*....|....*....|....*....
gi 544677870 249 ---QISGFRSQCATMTLAQTIAVSLALRK 274
Cdd:COG1737  238 ptlRSSAFSSRVAQLALIDALAAAVAQRD 266
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 134-269 6.86e-30

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: 109.63  E-value: 6.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 134 EQLEAVTKILDNANRIFIVGLKRSFSIASYLNYALSHLNYDVFLIDGLGGMFSEQLNrIREGDVVIAISFSPYATETISV 213
Cdd:cd05013    1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAAN-LTPGDVVIAISFSGETKETVEA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 214 LDATARTGVKHIAITDSQLSPLLTFSDVSFIIKEAQ----ISGFRSQCATMTLAQTIAVS 269
Cdd:cd05013   80 AEIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEgdfrSSAFSSRIAQLALIDALFLA 139
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 142-272 3.88e-20

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: 83.89  E-value: 3.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  142 ILDNANRIFIVGLKRSFSIASYLNYALSHLNYDVFLIDGLGGMFSEQLNRIREGDVVIAISFSPYATETISVLDATARTG 221
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 544677870  222 VKHIAITDSQLSPLLTFSDVSFIIKEAQISGFRSqcaTMTL-AQTIAVSLAL 272
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPETGVAS---TKSItAQLAALDALA 129
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
13-276 1.58e-18

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 84.97  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  13 EVRKQYDSLSKRLKQVAQYILDNGDSVIFDTVSEIAEKAQVPPSTLIRFANAFGLSGFNDIKqLYRQNLMEGTTSYTER- 91
Cdd:PRK14101 346 RIRQMRDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFK-LKLATGLTGTIPMSHSq 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  92 VQLfrqiepklneskGD-HTDVLRLFIQGNNQALAQLANQITEEQLEAVTKILDNANRIFIVGLKRSFSIASYLNYALSH 170
Cdd:PRK14101 425 VHL------------GDtATDFGAKVLDNTVSAILQLREHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFR 492

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 171 LNYDVFLIDGLgGMFSEQLNRIREGDVVIAISFSPYATETISVLDATARTGVKHIAITdSQLSPLLTFSDVSFI-----I 245
Cdd:PRK14101 493 FGIPTIAYGDL-YMQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAIT-SSNTPLAKRATVALEtdhieM 570

                        250       260       270
                 ....*....|....*....|....*....|.
gi 544677870 246 KEAQISgFRSQCATMTLAQTIAVSLALRKAS 276
Cdd:PRK14101 571 RESQLS-MISRILHLVMIDILAVGVAIRRAA 600
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 124-249 1.33e-10

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: 59.13  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 124 LAQLANQITEEQLEAVTKILDNANRIFIVGLKRSFSIASYLNYALSHLNYDVFLIdglGGMFSEqlnRIREGDVVIAISF 203
Cdd:cd05005   11 IENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVV---GETTTP---AIGPGDLLIAISG 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 544677870 204 SpyaTETISVLDA--TAR-TGVKHIAITDSQLSPLLTFSDVSFIIKEAQ 249
Cdd:cd05005   85 S---GETSSVVNAaeKAKkAGAKVVLITSNPDSPLAKLADVVVVIPAAT 130
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
 12-74 7.47e-10

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: 54.26  E-value: 7.47e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544677870   12 NEVRKQYDSLSKRLKQVAQYILDNGDSVIFDTVSEIAEKAQVPPSTLIRFANAFGLSGFNDIK 74
Cdd:pfam01418   5 EKIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELK 67
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
14-228 1.89e-08

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 54.00  E-value: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  14 VRKQYDSLSKRLKQVAQYILDNGDSVIFDTVSEIAEKAQVPPSTLIRFANAFGLSGFNDIKQLYRQNLMEGTTSYTERVQ 93
Cdd:PRK11557   3 IRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALASQPEPPSVPVH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  94 lfrqiepklNESKGDhtDVLRL----FIQGNNQALAQLANQITEEQLEAVTKILDNANRIFIVGLKRSFSIASYLNYALS 169
Cdd:PRK11557  83 ---------NQIRGD--DPLRLvgekLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLM 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 544677870 170 HLNYDVFLIDGLGGMFSeQLNRIREGDVVIAISFSPYATETISVLDATARTGVKHIAIT 228
Cdd:PRK11557 152 KIGINAVAERDMHALLA-TVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAIT 209
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 122-270 3.18e-08

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: 53.44  E-value: 3.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 122 QALAQLANQITEEQLEAVTKILDNANRIFIVGLKRSFSIASYLNYAL---------------SHlnydvflidGLGGMfs 186
Cdd:COG0794   20 EALAALAERLDESFEKAVELILNCKGRVVVTGMGKSGHIARKIAATLastgtpafflhpaeaSH---------GDLGM-- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 187 eqlnrIREGDVVIAISFSPYATETISVLDATARTGVKHIAITDSQLSPLLTFSDVSFII---KEAqisgfrsqC------ 257
Cdd:COG0794   89 -----ITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLpveREA--------Cplnlap 155

                        170
                 ....*....|....*...
gi 544677870 258 ---ATMTLA--QTIAVSL 270
Cdd:COG0794  156 ttsTTATLAlgDALAVAL 173
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
13-243 4.02e-08

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 53.16  E-value: 4.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  13 EVRKQYDSLSKRLKQVAQYILDNGDSVIFDTVSEIAEKAQVPPSTLIRFANAFGLSGFNDIkqlyRQNLMEGTTSYTER- 91
Cdd:PRK15482   6 KIRNAESEFTENEQKIADFLRANVSELKSVSSRKMAKQLGISQSSIVKFAQKLGAQGFTEL----RMALIGEYSASREKt 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  92 ----VQLFRQIepklneSKGDHTDVL-RLFIQGNNQALAQLANQITEEQLEAVTKILDNANRIFIVGLKRSFSIASYLNY 166
Cdd:PRK15482  82 nataLHLHSSI------TSDDSLEVIaRKLNREKELALEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSF 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544677870 167 ALSHLNYDVFL-IDG-LGGMFSEQLnriREGDVVIAISFSPYATETISVLDATARTGVKHIAITDSQLSPLLTFSDVSF 243
Cdd:PRK15482 156 KLMKIGYRVACeADThVQATVSQAL---KKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTL 231
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
14-241 1.02e-07

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 52.07  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  14 VRKQYDSLSKRLKQVAQYILDNGDSVIFDTVSEIAEKAQVPPSTLIRFANAFGLSGFNDikqlYRQNLmegTTSYTERVQ 93
Cdd:PRK11337  19 IRMKQEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRN----LRSAL---EDYFSQSEQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  94 LFRQ-IEPklNESKgdhTDVLRLFIQGNNQALAQLANQITEEQLEAVTKILDNANRIFIVGLKRSFSIA-----SYLNYA 167
Cdd:PRK11337  92 VLHSeLSF--DDAP---QDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIArdvqhKFLRIG 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544677870 168 LSHLNYDvfliDGLGGMFSEQLnrIREGDVVIAISFSPYATETISVLDATARTGVKHIAITDSQLSPLLTFSDV 241
Cdd:PRK11337 167 VRCQAYD----DAHIMLMSAAL--LQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADY 234
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 149-229 1.24e-07

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: 48.52  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 149 IFIVGLKRSFSIASYLNYALSHLNY-DVFLIDGLGGMFSEQLNRIREGDVVIAISFSPYATETISVLDATARTGVKHIAI 227
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTGiEVVALIATELEHASLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                 ..
gi 544677870 228 TD 229
Cdd:cd04795   81 TD 82
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 148-269 2.38e-07

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: 48.69  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 148 RIFIVGLKRSFSIASYLNYALSHL-NYDVFL--IDGLGGmfseQLNRIREGDVVIAISFSPYATETISVLDATARTGVKH 224
Cdd:cd05014    2 KVVVTGVGKSGHIARKIAATLSSTgTPAFFLhpTEALHG----DLGMVTPGDVVIAISNSGETDELLNLLPHLKRRGAPI 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 544677870 225 IAITDSQLSPLLTFSDVSFII---KEAQISGFR---SQCATMTLAQTIAVS 269
Cdd:cd05014   78 IAITGNPNSTLAKLSDVVLDLpveEEACPLGLApttSTTAMLALGDALAVA 128
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 122-272 1.16e-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: 49.13  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 122 QALAQLANQITEEQLEAVTKILDNAN-RIFIVGLKRSFSIASYLNYAL-SHLNYDVFLIDGlggmfSE----QLNRIREG 195
Cdd:COG2222    9 EAWRRALAALAAAIAALLARLRAKPPrRVVLVGAGSSDHAAQAAAYLLeRLLGIPVAALAP-----SElvvyPAYLKLEG 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544677870 196 DVVIAISFSPYATETISVLDATARTGVKHIAITDSQLSPLLTFSDVSFIIKEAQISGFrsqCATMTLAQTIAVSLAL 272
Cdd:COG2222   84 TLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSV---AATKSFTTMLLALLAL 157
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 14-235 3.49e-06

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 47.30  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  14 VRKQYDSLSKRLKQVAQYILDNGDSVIFDTVSEIAEKAQVPPSTLIRFANAFGLSGFNDIKQLYRQNLMEGtTSYTErvq 93
Cdd:PRK11302   7 IQSRLEHLSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLAQSLANG-TPYVN--- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870  94 lfRQIEPklNESKGDHTDvlRLFiqgnNQALAQL---ANQITEEQLEAVTKILDNANRIFIVGLKRSFSIASYLNYALSH 170
Cdd:PRK11302  83 --RNVEE--DDSVEAYTG--KIF----ESAMASLdhaRQSLDPSAINRAVDLLTQAKKISFFGLGASAAVAHDAQNKFFR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 171 LN-----YDVFLIDGLGGMFSeqlnriREGDVVIAISFSPYATETISVLDATARTGVKHIAITdSQLSPL 235
Cdd:PRK11302 153 FNvpvvyFDDIVMQRMSCMNS------SDGDVVVLISHTGRTKSLVELAQLARENGATVIAIT-SAGSPL 215
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 148-263 2.27e-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: 37.09  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677870 148 RIFIVGLKRSFSIASYLNYAL-SHLNYDVFLIDGlggmfSEQLNR---IREGDVVIAISFSPYATETISVLDATARTGVK 223
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLeRLAGIPVEVEAA-----SEFRYRrplLDEDTLVIAISQSGETADTLAALRLAKEKGAK 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 544677870 224 HIAITDSQLSPLLTFSDVSFIIK-EAQIS-----GFRSQCATMTLA 263
Cdd:cd05008   76 TVAITNVVGSTLAREADYVLYLRaGPEISvaatkAFTSQLLALLLL 121
 
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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