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Conserved domains on  [gi|488313839|ref|WP_002383224|]
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MULTISPECIES: MurR/RpiR family transcriptional regulator [Enterococcus]

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 ...
 1-288 2.51e-73

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


:

Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 226.73  E-value: 2.51e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839   1 MKNHYLDQRIRIKKPNLSLTEKKISDYFVHSESLLTQMTLESLANEIGVSQSSVYQFVKKIGYSGFQEFKIDIARNSNyq 80
Cdd:COG1737    2 MSAMSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELA-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839  81 ptfQNVNSVNGADDISPDDDSITIAKKVLQANIYSLSNATQFLTKELLDNVLALMYSAKTLHFFGQGGSSIVAFDSFHKF 160
Cdd:COG1737   80 ---EGLSSYERLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 161 IRTNYRCNYI-FDYHMQLSFVTKLTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAIIVVTE 239
Cdd:COG1737  157 LRLGKNVVLLdGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSE 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 488313839 240 EGLFRAESLASRISYLTVMDILYTNTMYHNFDQNADSLKKIRDNISTTK 288
Cdd:COG1737  237 EPTLRSSAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSELR 285
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 1-288 2.51e-73

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 226.73  E-value: 2.51e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839   1 MKNHYLDQRIRIKKPNLSLTEKKISDYFVHSESLLTQMTLESLANEIGVSQSSVYQFVKKIGYSGFQEFKIDIARNSNyq 80
Cdd:COG1737    2 MSAMSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELA-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839  81 ptfQNVNSVNGADDISPDDDSITIAKKVLQANIYSLSNATQFLTKELLDNVLALMYSAKTLHFFGQGGSSIVAFDSFHKF 160
Cdd:COG1737   80 ---EGLSSYERLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 161 IRTNYRCNYI-FDYHMQLSFVTKLTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAIIVVTE 239
Cdd:COG1737  157 LRLGKNVVLLdGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSE 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 488313839 240 EGLFRAESLASRISYLTVMDILYTNTMYHNFDQNADSLKKIRDNISTTK 288
Cdd:COG1737  237 EPTLRSSAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSELR 285
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 126-263 5.67e-40

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: 136.20  E-value: 5.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 126 ELLDNVLALMYSAKTLHFFGQGGSSIVAFDSFHKFIRTNYRCNYIFDYHMQLSFVTKLTSEDCVFIFSHSGKTKESINLA 205
Cdd:cd05013    1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488313839 206 RQVKKTNAKMITLTGNSGSELAGLSDEAIIVVTEEGLFRAESLASRISYLTVMDILYT 263
Cdd:cd05013   81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFL 138
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
9-281 3.40e-37

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 133.73  E-value: 3.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839   9 RIRIKKPNLSLTEKKISDYFVHSESLLTQMTLESLANEIGVSQSSVYQFVKKIGYSGFQEFKIDIArNSNYQPTfQNVNS 88
Cdd:PRK11337  18 YIRMKQEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALE-DYFSQSE-QVLHS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839  89 vngadDISPDDDSITIAKKVLQANIYSLSNATQFLTKELLDNVLALMYSAKTLHFFGQGGSSIVAFDSFHKFIRTNYRCN 168
Cdd:PRK11337  96 -----ELSFDDAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQ 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 169 YIFDYHMQLSFVTKLTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAIIVVTEEGLFRAESL 248
Cdd:PRK11337 171 AYDDAHIMLMSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTAQGSPLLGENA 250

                        250       260       270
                 ....*....|....*....|....*....|...
gi 488313839 249 ASRISYLTVMDILYTNTMYHNFDQNADSLKKIR 281
Cdd:PRK11337 251 AARIAQLNILDAFFVSVAQLNIEQAEINLQKTG 283
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 134-240 8.15e-17

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: 75.03  E-value: 8.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839  134 LMYSAKTLHFFGQGGSSIVAFDSFHKFIRTNYRCNYIFD----YHMQLSFVTKltsEDCVFIFSHSGKTKESINLARQVK 209
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELaselRHGVLALVDE---DDLVIAISYSGETKDLLAAAELAK 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 488313839  210 KTNAKMITLTGNSGSELAGLSDEAIIVVTEE 240
Cdd:pfam01380  78 ARGAKIIAITDSPGSPLAREADHVLYINAGP 108
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 1-288 2.51e-73

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 226.73  E-value: 2.51e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839   1 MKNHYLDQRIRIKKPNLSLTEKKISDYFVHSESLLTQMTLESLANEIGVSQSSVYQFVKKIGYSGFQEFKIDIARNSNyq 80
Cdd:COG1737    2 MSAMSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELA-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839  81 ptfQNVNSVNGADDISPDDDSITIAKKVLQANIYSLSNATQFLTKELLDNVLALMYSAKTLHFFGQGGSSIVAFDSFHKF 160
Cdd:COG1737   80 ---EGLSSYERLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 161 IRTNYRCNYI-FDYHMQLSFVTKLTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAIIVVTE 239
Cdd:COG1737  157 LRLGKNVVLLdGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSE 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 488313839 240 EGLFRAESLASRISYLTVMDILYTNTMYHNFDQNADSLKKIRDNISTTK 288
Cdd:COG1737  237 EPTLRSSAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSELR 285
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 126-263 5.67e-40

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: 136.20  E-value: 5.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 126 ELLDNVLALMYSAKTLHFFGQGGSSIVAFDSFHKFIRTNYRCNYIFDYHMQLSFVTKLTSEDCVFIFSHSGKTKESINLA 205
Cdd:cd05013    1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488313839 206 RQVKKTNAKMITLTGNSGSELAGLSDEAIIVVTEEGLFRAESLASRISYLTVMDILYT 263
Cdd:cd05013   81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFL 138
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
9-281 3.40e-37

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 133.73  E-value: 3.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839   9 RIRIKKPNLSLTEKKISDYFVHSESLLTQMTLESLANEIGVSQSSVYQFVKKIGYSGFQEFKIDIArNSNYQPTfQNVNS 88
Cdd:PRK11337  18 YIRMKQEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALE-DYFSQSE-QVLHS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839  89 vngadDISPDDDSITIAKKVLQANIYSLSNATQFLTKELLDNVLALMYSAKTLHFFGQGGSSIVAFDSFHKFIRTNYRCN 168
Cdd:PRK11337  96 -----ELSFDDAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQ 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 169 YIFDYHMQLSFVTKLTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAIIVVTEEGLFRAESL 248
Cdd:PRK11337 171 AYDDAHIMLMSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTAQGSPLLGENA 250

                        250       260       270
                 ....*....|....*....|....*....|...
gi 488313839 249 ASRISYLTVMDILYTNTMYHNFDQNADSLKKIR 281
Cdd:PRK11337 251 AARIAQLNILDAFFVSVAQLNIEQAEINLQKTG 283
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 8-290 1.13e-30

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 116.25  E-value: 1.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839   8 QRIRIKKPNLSLTEKKISDYFVHSESLLTQMTLESLANEIGVSQSSVYQFVKKIGYSGFQEFKIDIARN-SNYQPTF-QN 85
Cdd:PRK11302   5 EKIQSRLEHLSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLAQSlANGTPYVnRN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839  86 VNSVNGADdispdddsiTIAKKVLQANIYSLSNATQFLTKELLDNVLALMYSAKTLHFFGQGGSSIVAFDSFHKFIRTNY 165
Cdd:PRK11302  85 VEEDDSVE---------AYTGKIFESAMASLDHARQSLDPSAINRAVDLLTQAKKISFFGLGASAAVAHDAQNKFFRFNV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 166 RCNYIFDYHMQLSFVTKLTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTgNSGSELAGLSDEAIIVVTEEGLFRA 245
Cdd:PRK11302 156 PVVYFDDIVMQRMSCMNSSDGDVVVLISHTGRTKSLVELAQLARENGATVIAIT-SAGSPLAREATLALTLDVPEDTDIY 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 488313839 246 ESLASRISYLTVMDILYTNTMYHNFDQNADSLKKIRDNISTTKTD 290
Cdd:PRK11302 235 MPMVSRIAQLTVIDVLATGFTLRRGAKFRDNLKRVKEALKESRFD 279
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
9-281 1.55e-28

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 110.56  E-value: 1.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839   9 RIRIKKPNLSLTEKKISDYFVHSESLLTQMTLESLANEIGVSQSSVYQFVKKIGYSGFQEFKIDIARNSNYQPTFQNVNS 88
Cdd:PRK15482   6 KIRNAESEFTENEQKIADFLRANVSELKSVSSRKMAKQLGISQSSIVKFAQKLGAQGFTELRMALIGEYSASREKTNATA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839  89 VNGADDISPDDDSITIAKKVLQANIYSLSNATQFLTKELLDNVLALMYSAKTLHFFGQGGSSIVAFDSFHKFIRTNYRCN 168
Cdd:PRK15482  86 LHLHSSITSDDSLEVIARKLNREKELALEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKIGYRVA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 169 YIFDYHMQLSFVTKLTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAIIVVTEEGLFRAESL 248
Cdd:PRK15482 166 CEADTHVQATVSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSGETEWRSSSM 245

                        250       260       270
                 ....*....|....*....|....*....|...
gi 488313839 249 ASRISYLTVMDILYTNTMYHNfdqNADSLKKIR 281
Cdd:PRK15482 246 STRTAQNSVTDLLFVGLVQLN---DVESLKMIQ 275
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
9-278 2.56e-28

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 109.85  E-value: 2.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839   9 RIRIKKPNLSLTEKKISDYFVHSESLLTQMTLESLANEIGVSQSSVYQFVKKIGYSGFQEFKIDIARNSNYQPTFQNVNS 88
Cdd:PRK11557   2 RIRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALASQPEPPSVPV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839  89 VNGaddISPDDDSITIAKKVLQANIYSLSNATQFLTKELLDNVLALMYSAKTLHFFGQGGSSIVAFDSFHKFIRTNYRCN 168
Cdd:PRK11557  82 HNQ---IRGDDPLRLVGEKLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 169 YIFDYHMQLSFVTKLTSEDCVFIFSHSGKTKEsINLARQ-VKKTNAKMITLTGNSGSELAGLSDEAIIVVTEEGLFRAES 247
Cdd:PRK11557 159 AERDMHALLATVQALSPDDLLLAISYSGERRE-LNLAADeALRVGAKVLAITGFTPNALQQRASHCLYTIAEEQATRSAA 237

                        250       260       270
                 ....*....|....*....|....*....|.
gi 488313839 248 LASRISYLTVMDILYTNTMYHNFDQNADSLK 278
Cdd:PRK11557 238 ISSTHAQGMLTDLLFMALIQQDLERAPERIR 268
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
8-275 1.82e-17

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 82.27  E-value: 1.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839   8 QRIRIKKPNLSLTEKKISDYFVHSESLLTQMTLESLANEIGVSQSSVYQFVKKIGYSGFQEFKIDIARN-------SNYQ 80
Cdd:PRK14101 345 ERIRQMRDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGltgtipmSHSQ 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839  81 PTFQNVNSVNGAddispdddsitiakKVLQANIYSLSNATQFLTKELLDNVLALMYSAKTLHFFGQGGSSIVAFDSFHKF 160
Cdd:PRK14101 425 VHLGDTATDFGA--------------KVLDNTVSAILQLREHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKF 490

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 161 IRTNYRCNYIFDYHMQLSFVTKLTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTgNSGSELAGLSDEAIIVVTEE 240
Cdd:PRK14101 491 FRFGIPTIAYGDLYMQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAIT-SSNTPLAKRATVALETDHIE 569

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 488313839 241 GLFRAESLASRISYLTVMDILYTNTMYHNFDQNAD 275
Cdd:PRK14101 570 MRESQLSMISRILHLVMIDILAVGVAIRRAAPNAE 604
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 134-240 8.15e-17

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: 75.03  E-value: 8.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839  134 LMYSAKTLHFFGQGGSSIVAFDSFHKFIRTNYRCNYIFD----YHMQLSFVTKltsEDCVFIFSHSGKTKESINLARQVK 209
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELaselRHGVLALVDE---DDLVIAISYSGETKDLLAAAELAK 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 488313839  210 KTNAKMITLTGNSGSELAGLSDEAIIVVTEE 240
Cdd:pfam01380  78 ARGAKIIAITDSPGSPLAREADHVLYINAGP 108
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
 9-74 3.12e-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: 58.11  E-value: 3.12e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488313839    9 RIRIKKPNLSLTEKKISDYFVHSESLLTQMTLESLANEIGVSQSSVYQFVKKIGYSGFQEFKIDIA 74
Cdd:pfam01418   6 KIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALA 71
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 183-241 4.20e-11

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: 59.48  E-value: 4.20e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 183 LTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAIIV-VTEEG 241
Cdd:cd05014   45 VTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLpVEEEA 104
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 183-241 2.48e-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: 54.21  E-value: 2.48e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 183 LTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAIIV-VTEEG 241
Cdd:COG0794   89 ITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLpVEREA 148
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 183-236 1.03e-07

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: 51.04  E-value: 1.03e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488313839 183 LTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAIIV 236
Cdd:cd05005   73 IGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVI 126
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 189-234 7.19e-07

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: 49.90  E-value: 7.19e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488313839 189 VFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAI 234
Cdd:COG2222   86 VVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVL 131
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 189-234 4.37e-06

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: 44.87  E-value: 4.37e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488313839 189 VFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAI 234
Cdd:cd05710   51 VILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVI 96
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 171-234 9.43e-06

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: 44.03  E-value: 9.43e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488313839 171 FDYHMQLsfvtkLTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAI 234
Cdd:cd05008   37 FRYRRPL-----LDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAITNVVGSTLAREADYVL 95
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 183-236 8.47e-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: 42.50  E-value: 8.47e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488313839 183 LTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAIIV 236
Cdd:cd05006   99 GQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIHV 152
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 143-232 2.83e-04

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 41.89  E-value: 2.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 143 FFGQGGSSIVAfDSFHKFIRTNYRCNYIF--DYHMqLSFVTKLTSedcVFIFSHSGKTKESINLARQVKKTNAKMITLTg 220
Cdd:PRK08674  39 ISGMGGSGIGG-DLLRILLFDELKVPVFVnrDYTL-PAFVDEKTL---VIAVSYSGNTEETLSAVEQALKRGAKIIAIT- 112

                         90
                 ....*....|..
gi 488313839 221 nSGSELAGLSDE 232
Cdd:PRK08674 113 -SGGKLKEMAKE 123
gmhA PRK00414
D-sedoheptulose 7-phosphate isomerase;
187-236 5.33e-04

D-sedoheptulose 7-phosphate isomerase;


Pssm-ID: 179012 [Multi-domain]  Cd Length: 192  Bit Score: 40.10  E-value: 5.33e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 488313839 187 DCVFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAIIV 236
Cdd:PRK00414 113 DVLLGISTSGNSGNIIKAIEAARAKGMKVITLTGKDGGKMAGLADIEIRV 162
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 143-227 8.99e-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: 8.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 143 FFGQGGSSIV-----AFDSFHKFIRTnYRCNyifDYHMQlsfvTKLTSEDCVFIFSHSGKTKESINLARQVKKTNAKMIT 217
Cdd:cd05017    4 ILGMGGSGIGgdlleSLLLDEAKIPV-YVVK---DYTLP----AFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVA 75

                         90
                 ....*....|
gi 488313839 218 LTgnSGSELA 227
Cdd:cd05017   76 IT--SGGKLL 83
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 182-269 2.63e-03

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 38.90  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488313839 182 KLTSEDCVFIFSHSGKTKESINLARQVKKTNAKMITLTGNSGSELAGLSDEAI-IVVTEEGLFRAESLASRISYLTVMDI 260
Cdd:PRK12570 124 GLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAIsPVVGPEVLTGSTRLKSGTAQKMVLNM 203

                         90
                 ....*....|....*
gi 488313839 261 LYTNTM------YHN 269
Cdd:PRK12570 204 LSTASMirlgksYQN 218
 
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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