NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490261964|ref|WP_004159182|]
View 

MurR/RpiR family transcriptional regulator [Erwinia amylovora]

Protein Classification

MurR/RpiR family transcriptional regulator( domain architecture ID 11485394)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
5-279 3.45e-176

MurR/RpiR family transcriptional regulator;


:

Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 486.58  E-value: 3.45e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964   5 LRIRQLYPSLAMNERRLADYLLSQPEHALHLSSQKLADESGVSQSSVVKFAQKLGYKGFPALKLALSESLAGK---DATT 81
Cdd:PRK11557   1 LRIRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALASQpepPSVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964  82 VHNHILSDDALKVVGEKLLSEKTSAIRATLDINSEEMLLATLRLLKQARRIVLIGIGASGLVAKDFSWKLMKIGISAVAE 161
Cdd:PRK11557  81 VHNQIRGDDPLRLVGEKLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 162 QDMHALLASVQALSVGDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANHCLYTVAEEQSTRSAALSS 241
Cdd:PRK11557 161 RDMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAEEQATRSAAISS 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490261964 242 TTAQLTLTDLLFMALIQHDQERASSHIRHSEALVKKLV 279
Cdd:PRK11557 241 THAQGMLTDLLFMALIQQDLERAPERIRHSEALVKKLV 278
 
Name Accession Description Interval E-value
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
5-279 3.45e-176

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 486.58  E-value: 3.45e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964   5 LRIRQLYPSLAMNERRLADYLLSQPEHALHLSSQKLADESGVSQSSVVKFAQKLGYKGFPALKLALSESLAGK---DATT 81
Cdd:PRK11557   1 LRIRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALASQpepPSVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964  82 VHNHILSDDALKVVGEKLLSEKTSAIRATLDINSEEMLLATLRLLKQARRIVLIGIGASGLVAKDFSWKLMKIGISAVAE 161
Cdd:PRK11557  81 VHNQIRGDDPLRLVGEKLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 162 QDMHALLASVQALSVGDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANHCLYTVAEEQSTRSAALSS 241
Cdd:PRK11557 161 RDMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAEEQATRSAAISS 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490261964 242 TTAQLTLTDLLFMALIQHDQERASSHIRHSEALVKKLV 279
Cdd:PRK11557 241 THAQGMLTDLLFMALIQQDLERAPERIRHSEALVKKLV 278
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 1-278 3.62e-80

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 243.68  E-value: 3.62e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964   1 MSSLLRIRQLYPSLAMNERRLADYLLSQPEHALHLSSQKLADESGVSQSSVVKFAQKLGYKGFPALKLALSESLA-GKDA 79
Cdd:COG1737    5 MSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAeGLSS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964  80 TTVHNHILSDDALKVVGEKLLSEKTSAIRATLDINSEEMLLATLRLLKQARRIVLIGIGASGLVAKDFSWKLMKIGISAV 159
Cdd:COG1737   85 YERLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 160 A-EQDMHALLASVQALSVGDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANHCLYTVAEEQSTRSAA 238
Cdd:COG1737  165 LlDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRSSA 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 490261964 239 LSSTTAQLTLTDLLFMALIQHDQERASSHIRHSEALVKKL 278
Cdd:COG1737  245 FSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSEL 284
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 117-255 3.72e-36

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: 125.80  E-value: 3.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 117 EMLLATLRLLKQARRIVLIGIGASGLVAKDFSWKLMKIGISAVAEQDMHALLASVQALSVGDVLLAISYTGERREINLAA 196
Cdd:cd05013    1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490261964 197 QEARRIGATVLAFTGFTPNTLQQSANHCLYTVAEEQSTRSAALSSTTAQLTLTDLLFMA 255
Cdd:cd05013   81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 125-255 3.77e-24

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: 94.29  E-value: 3.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964  125 LLKQARRIVLIGIGASGLVAKDFSWKLMKIGISAVAEQDMHALLASVQAL-SVGDVLLAISYTGERREINLAAQEARRIG 203
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALvDEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 490261964  204 ATVLAFTGFTPNTLQQSANHCLYTVAEEQsTRSAALSSTTAQLTLTDLLFMA 255
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPE-TGVASTKSITAQLAALDALAVA 131
 
Name Accession Description Interval E-value
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
5-279 3.45e-176

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 486.58  E-value: 3.45e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964   5 LRIRQLYPSLAMNERRLADYLLSQPEHALHLSSQKLADESGVSQSSVVKFAQKLGYKGFPALKLALSESLAGK---DATT 81
Cdd:PRK11557   1 LRIRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALASQpepPSVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964  82 VHNHILSDDALKVVGEKLLSEKTSAIRATLDINSEEMLLATLRLLKQARRIVLIGIGASGLVAKDFSWKLMKIGISAVAE 161
Cdd:PRK11557  81 VHNQIRGDDPLRLVGEKLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 162 QDMHALLASVQALSVGDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANHCLYTVAEEQSTRSAALSS 241
Cdd:PRK11557 161 RDMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAEEQATRSAAISS 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490261964 242 TTAQLTLTDLLFMALIQHDQERASSHIRHSEALVKKLV 279
Cdd:PRK11557 241 THAQGMLTDLLFMALIQQDLERAPERIRHSEALVKKLV 278
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 1-278 3.62e-80

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 243.68  E-value: 3.62e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964   1 MSSLLRIRQLYPSLAMNERRLADYLLSQPEHALHLSSQKLADESGVSQSSVVKFAQKLGYKGFPALKLALSESLA-GKDA 79
Cdd:COG1737    5 MSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAeGLSS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964  80 TTVHNHILSDDALKVVGEKLLSEKTSAIRATLDINSEEMLLATLRLLKQARRIVLIGIGASGLVAKDFSWKLMKIGISAV 159
Cdd:COG1737   85 YERLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKNVV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 160 A-EQDMHALLASVQALSVGDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANHCLYTVAEEQSTRSAA 238
Cdd:COG1737  165 LlDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRSSA 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 490261964 239 LSSTTAQLTLTDLLFMALIQHDQERASSHIRHSEALVKKL 278
Cdd:COG1737  245 FSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSEL 284
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
1-278 2.54e-63

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 200.69  E-value: 2.54e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964   1 MSSLLRIRQLYPSLAMNERRLADYLLSQPEHALHLSSQKLADESGVSQSSVVKFAQKLGYKGFPALKLAL----SESLAG 76
Cdd:PRK15482   1 MLYLTKIRNAESEFTENEQKIADFLRANVSELKSVSSRKMAKQLGISQSSIVKFAQKLGAQGFTELRMALigeySASREK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964  77 KDATTVHNH--ILSDDALKVVGEKLLSEKTSAIRATLDINSEEMLLATLRLLKQARRIVLIGIGASGLVAKDFSWKLMKI 154
Cdd:PRK15482  81 TNATALHLHssITSDDSLEVIARKLNREKELALEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 155 GISAVAEQDMHALLASVQALSVGDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANHCLYTVAEEQST 234
Cdd:PRK15482 161 GYRVACEADTHVQATVSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSGETEW 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 490261964 235 RSAALSSTTAQLTLTDLLFMALIQHDQERASSHIRHSEALVKKL 278
Cdd:PRK15482 241 RSSSMSTRTAQNSVTDLLFVGLVQLNDVESLKMIQRSSELTQRL 284
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
6-276 7.05e-40

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 140.28  E-value: 7.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964   6 RIRQLYPSLAMNERRLADYLLSQPEHALHLSSQKLADESGVSQSSVVKFAQKLGYKGFPALKLALSESLAgKDATTVHNH 85
Cdd:PRK11337  18 YIRMKQEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALEDYFS-QSEQVLHSE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964  86 ILSDDALKVVGEKLLSEKTSAIRATLDI-NSEEMLLATlRLLKQARRIVLIGIGASGLVAKDFSWKLMKIGISAVAEQDM 164
Cdd:PRK11337  97 LSFDDAPQDVVNKVFNTSLQAIEETQSIlDVDEFHRAA-RFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 165 HALLASVQALSVGDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANHCLYTVAEEQSTRSAALSSTTA 244
Cdd:PRK11337 176 HIMLMSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTAQGSPLLGENAAARIA 255

                        250       260       270
                 ....*....|....*....|....*....|..
gi 490261964 245 QLTLTDLLFMALIQHDQERASSHIRHSEALVK 276
Cdd:PRK11337 256 QLNILDAFFVSVAQLNIEQAEINLQKTGAAVD 287
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 117-255 3.72e-36

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: 125.80  E-value: 3.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 117 EMLLATLRLLKQARRIVLIGIGASGLVAKDFSWKLMKIGISAVAEQDMHALLASVQALSVGDVLLAISYTGERREINLAA 196
Cdd:cd05013    1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490261964 197 QEARRIGATVLAFTGFTPNTLQQSANHCLYTVAEEQSTRSAALSSTTAQLTLTDLLFMA 255
Cdd:cd05013   81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 1-252 8.13e-32

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 118.94  E-value: 8.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964   1 MSSLLRIRQLYPSLAMNERRLADYLLSQPEHALHLSSQKLADESGVSQSSVVKFAQKLGYKGFPALKLALSESLAgKDAT 80
Cdd:PRK11302   1 MNMLEKIQSRLEHLSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLAQSLA-NGTP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964  81 TVHNHILSDDALKVVGEKLLSektSAIrATLDINSEEMLLATLR----LLKQARRIVLIGIGASGLVAKDFSWKLMKIGI 156
Cdd:PRK11302  80 YVNRNVEEDDSVEAYTGKIFE---SAM-ASLDHARQSLDPSAINravdLLTQAKKISFFGLGASAAVAHDAQNKFFRFNV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 157 SAVAEQD--MHALLASVQalSVGDVLLAISYTGERREINLAAQEARRIGATVLAFTgfTPNT-LQQSANHCLYTVAEEQS 233
Cdd:PRK11302 156 PVVYFDDivMQRMSCMNS--SDGDVVVLISHTGRTKSLVELAQLARENGATVIAIT--SAGSpLAREATLALTLDVPEDT 231

                        250
                 ....*....|....*....
gi 490261964 234 TRSAALSSTTAQLTLTDLL 252
Cdd:PRK11302 232 DIYMPMVSRIAQLTVIDVL 250
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
6-276 3.19e-30

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 119.25  E-value: 3.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964   6 RIRQLYPSLAMNERRLADYLLSQPEHALHLSSQKLADESGVSQSSVVKFAQKLGYKGFPALKLALSESLAGKDATTvHNH 85
Cdd:PRK14101 346 RIRQMRDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTGTIPMS-HSQ 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964  86 ILSDDALKVVGEKLLSEKTSAIRATLDINSEEMLLATLRLLKQARRIVLIGIGASGLVAKDFSWKLMKIGISAVAEQDMH 165
Cdd:PRK14101 425 VHLGDTATDFGAKVLDNTVSAILQLREHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIAYGDLY 504

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 166 ALLASVQALSVGDVLLAISYTGERREINLAAQEARRIGATVLAFTgfTPNT-LQQSANHCLYTVAEEQSTRSAALSSTTA 244
Cdd:PRK14101 505 MQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAIT--SSNTpLAKRATVALETDHIEMRESQLSMISRIL 582

                        250       260       270
                 ....*....|....*....|....*....|..
gi 490261964 245 QLTLTDLLFMALIqhdQERASSHIRHSEALVK 276
Cdd:PRK14101 583 HLVMIDILAVGVA---IRRAAPNAELAEAVAR 611
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 125-255 3.77e-24

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: 94.29  E-value: 3.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964  125 LLKQARRIVLIGIGASGLVAKDFSWKLMKIGISAVAEQDMHALLASVQAL-SVGDVLLAISYTGERREINLAAQEARRIG 203
Cdd:pfam01380   1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALvDEDDLVIAISYSGETKDLLAAAELAKARG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 490261964  204 ATVLAFTGFTPNTLQQSANHCLYTVAEEQsTRSAALSSTTAQLTLTDLLFMA 255
Cdd:pfam01380  81 AKIIAITDSPGSPLAREADHVLYINAGPE-TGVASTKSITAQLAALDALAVA 131
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
 1-77 8.39e-23

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: 89.31  E-value: 8.39e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490261964    1 MSSLLRIRQLYPSLAMNERRLADYLLSQPEHALHLSSQKLADESGVSQSSVVKFAQKLGYKGFPALKLALSESLAGK 77
Cdd:pfam01418   1 MGLLEKIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELANS 77
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 130-255 4.57e-15

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: 69.88  E-value: 4.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 130 RRIVLIGIGASGLVAKDFSWKLMKIGISAV---AEQDMHALLASVQAlsvGDVLLAISYTGERREINLAAQEARRIGATV 206
Cdd:cd05014    1 GKVVVTGVGKSGHIARKIAATLSSTGTPAFflhPTEALHGDLGMVTP---GDVVIAISNSGETDELLNLLPHLKRRGAPI 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490261964 207 LAFTGFTPNTLQQSANHCL-YTVAEEQSTRS-AALSSTTAQLTLTDLLFMA 255
Cdd:cd05014   78 IAITGNPNSTLAKLSDVVLdLPVEEEACPLGlAPTTSTTAMLALGDALAVA 128
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 101-265 2.21e-13

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: 66.83  E-value: 2.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 101 SEKTSAIRATLDINSEEMLLATL----RLLKQARRIVLIGIGASGLVAKDFSWKLMKIGISA--VAEqdmhallASVQAL 174
Cdd:cd05005    1 MEYLSLILEEIENVADKIDEEELdkliSAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVyvVGE-------TTTPAI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 175 SVGDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANHCLYTVAEEQSTRSAALSST--------TAQL 246
Cdd:cd05005   74 GPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGEHKSIqplgtlfeQSAL 153

                        170
                 ....*....|....*....
gi 490261964 247 TLTDLLFMALIQHDQERAS 265
Cdd:cd05005  154 VFLDAVIAKLMEELGVSEE 172
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 105-259 1.33e-11

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: 63.84  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 105 SAIRATLDINSEEML----------LATLRLLKQAR-RIVLIGIGASGLVAKDFSWKLMKIGISAV----AEQdMHALLA 169
Cdd:COG0794    9 ESAREVLEIEAEALAalaerldesfEKAVELILNCKgRVVVTGMGKSGHIARKIAATLASTGTPAFflhpAEA-SHGDLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 170 SVQAlsvGDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANHCLYT-VAEEQ-STRSAALSSTTAQLT 247
Cdd:COG0794   88 MITP---GDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLpVEREAcPLNLAPTTSTTATLA 164

                        170
                 ....*....|..
gi 490261964 248 LTDLLFMALIQH 259
Cdd:COG0794  165 LGDALAVALLEA 176
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 132-210 8.74e-10

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: 54.30  E-value: 8.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 132 IVLIGIGASGLVAKDFSWKLMKI-GISAVAEQDMHALLAS-VQALSVGDVLLAISYTGERREINLAAQEARRIGATVLAF 209
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELtGIEVVALIATELEHASlLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                 .
gi 490261964 210 T 210
Cdd:cd04795   81 T 81
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 105-264 3.03e-08

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: 53.75  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 105 SAIRATLDINSEEM--LLATLRLLKQaRRIVLIGIGAS---GLVAKDFSWKLMKIGISAVAeqdmhALLASVQALSV--- 176
Cdd:COG2222    9 EAWRRALAALAAAIaaLLARLRAKPP-RRVVLVGAGSSdhaAQAAAYLLERLLGIPVAALA-----PSELVVYPAYLkle 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 177 GDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANHCLYT-VAEEQSTrsAALSSTTAQLTLTDLLFMA 255
Cdd:COG2222   83 GTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLpAGPEKSV--AATKSFTTMLLALLALLAA 160


                 ....*....
gi 490261964 256 LIQHDQERA 264
Cdd:COG2222  161 WGGDDALLA 169
GmhA COG0279
Phosphoheptose isomerase [Carbohydrate transport and metabolism];
97-225 3.68e-08

Phosphoheptose isomerase [Carbohydrate transport and metabolism];


Pssm-ID: 440048 [Multi-domain]  Cd Length: 189  Bit Score: 52.04  E-value: 3.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964  97 EKLLSEKTSAIRATLDINSEEMLLATLRL---LKQARRIVLIGIGASGLVAKDFSWKLMKI------GISAVAEQDMHAL 167
Cdd:COG0279    6 KQYFEESIEALQALAEALAEAIEAAAELLaeaLLNGGKILVCGNGGSAADAQHFAAELVGRfererpGLPAIALTTDTSV 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490261964 168 LAS--------------VQALSV-GDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANHCL 225
Cdd:COG0279   86 LTAiandygydevfarqVEALGRpGDVLLAISTSGNSPNVLRALEAARERGMTTIALTGRDGGKLAGLADIEI 158
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
87-267 5.86e-08

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 52.85  E-value: 5.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964  87 LSDDALKVVGEKLLSEKTSAIRaTLDINSEEMLLATLRLLKQARRIVLIGIGASGLVAKDFSWKLMKIGISAVAEQDMHA 166
Cdd:PRK11543   1 MSEALLNAGRQTLMLELQEASR-LPERLGDDFVRAANIILHCEGKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 167 LLASVQALSVGDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANhCLYTVAEEQST---RSAALSSTT 243
Cdd:PRK11543  80 LHGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAK-AVLDISVEREAcpmHLAPTSSTV 158

                        170       180
                 ....*....|....*....|....*...
gi 490261964 244 AQLTLTDLLFMALIQH----DQERASSH 267
Cdd:PRK11543 159 NTLMMGDALAMAVMQArgfnEEDFARSH 186
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 100-226 2.34e-06

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: 46.73  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 100 LSEKTSAIRATLDINSEEM-----LLAtlRLLKQARRIVLIGIGASGLVAKDFSWKLMKI------GISAVA-EQDMHAL 167
Cdd:cd05006    1 FQESIQLKEALLELLAEAIeqaaqLLA--EALLNGGKILICGNGGSAADAQHFAAELVKRfekerpGLPAIAlTTDTSIL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490261964 168 LA-------------SVQALSV-GDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANHCLY 226
Cdd:cd05006   79 TAiandygyeevfsrQVEALGQpGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIH 151
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 131-256 4.12e-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: 45.18  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 131 RIVLIGIGAS---GLVAKDFSWKLMKIGISAVAEqdmHALLASVQALSVGDVLLAISYTGERREINLAAQEARRIGATVL 207
Cdd:cd05008    1 RILIVGCGTSyhaALVAKYLLERLAGIPVEVEAA---SEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 490261964 208 AFTGFTPNTLQQSANHCLYTVA-EEQStrSAALSSTTAQLTLtdLLFMAL 256
Cdd:cd05008   78 AITNVVGSTLAREADYVLYLRAgPEIS--VAATKAFTSQLLA--LLLLAL 123
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
 171-225 2.37e-04

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 41.00  E-value: 2.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490261964 171 VQALSV-GDVLLAISYTGERREINLAAQEARRIGATVLAFTGFTPNTLQQSANHCL 225
Cdd:PRK13937 100 VEALGRpGDVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLL 155
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 131-210 2.24e-03

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


Pssm-ID: 240148 [Multi-domain]  Cd Length: 119  Bit Score: 37.24  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 131 RIVLIGIGASGL---VAKDFSWKLMKIGISAVAEqdmHALLASVQAlsvGDVLLAISYTGERREINLAAQEARRIGATVL 207
Cdd:cd05017    1 NIVILGMGGSGIggdLLESLLLDEAKIPVYVVKD---YTLPAFVDR---KTLVIAVSYSGNTEETLSAVEQAKERGAKIV 74


                 ...
gi 490261964 208 AFT 210
Cdd:cd05017   75 AIT 77
PRK10892 PRK10892
arabinose-5-phosphate isomerase KdsD;
131-258 2.79e-03

arabinose-5-phosphate isomerase KdsD;


Pssm-ID: 182814 [Multi-domain]  Cd Length: 326  Bit Score: 38.55  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261964 131 RIVLIGIGASGLVAKDFSWKLMKIGISAVAEQDMHALLASVQALSVGDVLLAISYTGERREINLAAQEARRIGATVLAFT 210
Cdd:PRK10892  49 KVVVMGMGKSGHIGRKMAATFASTGTPSFFVHPGEAAHGDLGMVTPQDVVIAISNSGESSEILALIPVLKRLHVPLICIT 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 490261964 211 GFTPNTLQQSAN-HCLYTVAEEQSTRS-AALSSTTAQLTLTDLLFMALIQ 258
Cdd:PRK10892 129 GRPESSMARAADiHLCVKVPKEACPLGlAPTSSTTATLVMGDALAVALLK 178
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH