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Conserved domains on  [gi|446355820|ref|WP_000433675|]
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MULTISPECIES: MurR/RpiR family transcriptional regulator [Salmonella]

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 ...
 9-293 2.70e-82

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


:

Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 249.46  E-value: 2.70e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820   9 KPGKILDTLGAMQKSLTRASQRIVQYILAFPRQVTQSSIADLSRDTQAGEATVIRFCRTLGYKGFQDFKMDLAIELATTE 88
Cdd:COG1737    3 SAMSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  89 SddsSPLLDAEVSESDDAHAIGLKLQNTISNVLSETLNLLDMQQVLGVVDALRHCHSVYIFGVGSSGITALDMKHKLMRI 168
Cdd:COG1737   83 S---SYERLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 169 GLRGDAVSNN-HFMYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFCLINGNRQGM 247
Cdd:COG1737  160 GKNVVLLDGDgHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPT 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446355820 248 LQGDSIGTKAAQLFVFDLLYTLLVQSSPEQARESKLRTMNALDMTK 293
Cdd:COG1737  240 LRSSAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSELR 285
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 9-293 2.70e-82

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 249.46  E-value: 2.70e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820   9 KPGKILDTLGAMQKSLTRASQRIVQYILAFPRQVTQSSIADLSRDTQAGEATVIRFCRTLGYKGFQDFKMDLAIELATTE 88
Cdd:COG1737    3 SAMSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  89 SddsSPLLDAEVSESDDAHAIGLKLQNTISNVLSETLNLLDMQQVLGVVDALRHCHSVYIFGVGSSGITALDMKHKLMRI 168
Cdd:COG1737   83 S---SYERLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 169 GLRGDAVSNN-HFMYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFCLINGNRQGM 247
Cdd:COG1737  160 GKNVVLLDGDgHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPT 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446355820 248 LQGDSIGTKAAQLFVFDLLYTLLVQSSPEQARESKLRTMNALDMTK 293
Cdd:COG1737  240 LRSSAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSELR 285
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
20-290 1.49e-45

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 155.30  E-value: 1.49e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  20 MQKSLTRASQRIVQYILAFPRQVTQSSIADLSRDTQAGEATVIRFCRTLGYKGFQDFKMDLAIELATTESddsspLLDAE 99
Cdd:PRK11337  22 KQEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALEDYFSQSEQ-----VLHSE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 100 VSESDDAHAIGLKLQNTISNVLSETLNLLDMQQVLGVVDALRHCHSVYIFGVGSSGITALDMKHKLMRIGLRGDAVSNNH 179
Cdd:PRK11337  97 LSFDDAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAH 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 180 FMYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFcLINGNRQGM-LQGDSIGTKAA 258
Cdd:PRK11337 177 IMLMSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADY-VICSTAQGSpLLGENAAARIA 255

                        250       260       270
                 ....*....|....*....|....*....|..
gi 446355820 259 QLFVFDLLYTLLVQSSPEQARESKLRTMNALD 290
Cdd:PRK11337 256 QLNILDAFFVSVAQLNIEQAEINLQKTGAAVD 287
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 136-269 1.32e-38

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: 132.74  E-value: 1.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 136 VVDALRHCHSVYIFGVGSSGITALDMKHKLMRIGLRGDAVSNNHFMYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQ 215
Cdd:cd05013    6 AVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKE 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446355820 216 AGATTVAITHNLGSPLCEEADFCLINGNRQGMLQGDSIGTKAAQLFVFDLLYTL 269
Cdd:cd05013   86 RGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 140-269 9.44e-21

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: 85.81  E-value: 9.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  140 LRHCHSVYIFGVGSSGITALDMKHKLMRIGLRGDAVSNNH-FMYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGA 218
Cdd:pfam01380   2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASeLRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446355820  219 TTVAITHNLGSPLCEEADFCL-INGNRQgMLQGdSIGTKAAQLFVFDLLYTL 269
Cdd:pfam01380  82 KIIAITDSPGSPLAREADHVLyINAGPE-TGVA-STKSITAQLAALDALAVA 131
 
Name Accession Description Interval E-value
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 9-293 2.70e-82

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 249.46  E-value: 2.70e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820   9 KPGKILDTLGAMQKSLTRASQRIVQYILAFPRQVTQSSIADLSRDTQAGEATVIRFCRTLGYKGFQDFKMDLAIELATTE 88
Cdd:COG1737    3 SAMSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  89 SddsSPLLDAEVSESDDAHAIGLKLQNTISNVLSETLNLLDMQQVLGVVDALRHCHSVYIFGVGSSGITALDMKHKLMRI 168
Cdd:COG1737   83 S---SYERLRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 169 GLRGDAVSNN-HFMYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFCLINGNRQGM 247
Cdd:COG1737  160 GKNVVLLDGDgHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPT 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446355820 248 LQGDSIGTKAAQLFVFDLLYTLLVQSSPEQARESKLRTMNALDMTK 293
Cdd:COG1737  240 LRSSAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSELR 285
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
20-290 1.49e-45

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 155.30  E-value: 1.49e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  20 MQKSLTRASQRIVQYILAFPRQVTQSSIADLSRDTQAGEATVIRFCRTLGYKGFQDFKMDLAIELATTESddsspLLDAE 99
Cdd:PRK11337  22 KQEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSALEDYFSQSEQ-----VLHSE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 100 VSESDDAHAIGLKLQNTISNVLSETLNLLDMQQVLGVVDALRHCHSVYIFGVGSSGITALDMKHKLMRIGLRGDAVSNNH 179
Cdd:PRK11337  97 LSFDDAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYDDAH 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 180 FMYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFcLINGNRQGM-LQGDSIGTKAA 258
Cdd:PRK11337 177 IMLMSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADY-VICSTAQGSpLLGENAAARIA 255

                        250       260       270
                 ....*....|....*....|....*....|..
gi 446355820 259 QLFVFDLLYTLLVQSSPEQARESKLRTMNALD 290
Cdd:PRK11337 256 QLNILDAFFVSVAQLNIEQAEINLQKTGAAVD 287
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 136-269 1.32e-38

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: 132.74  E-value: 1.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 136 VVDALRHCHSVYIFGVGSSGITALDMKHKLMRIGLRGDAVSNNHFMYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQ 215
Cdd:cd05013    6 AVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKE 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446355820 216 AGATTVAITHNLGSPLCEEADFCLINGNRQGMLQGDSIGTKAAQLFVFDLLYTL 269
Cdd:cd05013   86 RGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 15-239 8.91e-36

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 129.73  E-value: 8.91e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  15 DTLGAMQKSL---TRASQRIVQYILAFPRQVTQSSIADLSRDTQAGEATVIRFCRTLGYKGFQDFKMDLAIELATtesdd 91
Cdd:PRK11302   2 NMLEKIQSRLehlSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLAQSLAN----- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  92 SSPLLDAEVSESDDAHAIGLKL-QNTISNvLSETLNLLDMQQVLGVVDALRHCHSVYIFGVGSSGITALDMKHKLMRIGL 170
Cdd:PRK11302  77 GTPYVNRNVEEDDSVEAYTGKIfESAMAS-LDHARQSLDPSAINRAVDLLTQAKKISFFGLGASAAVAHDAQNKFFRFNV 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446355820 171 RGDAVSNNHFMYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAIThNLGSPLCEEADFCL 239
Cdd:PRK11302 156 PVVYFDDIVMQRMSCMNSSDGDVVVLISHTGRTKSLVELAQLARENGATVIAIT-SAGSPLAREATLAL 223
PRK15482 PRK15482
HTH-type transcriptional regulator MurR;
21-272 3.10e-34

HTH-type transcriptional regulator MurR;


Pssm-ID: 185379 [Multi-domain]  Cd Length: 285  Bit Score: 125.58  E-value: 3.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  21 QKSLTRASQRIVQYILAFPRQVTQSSIADLSRDTQAGEATVIRFCRTLGYKGFQDFKMDLAIELATT--ESDDSSPLLDA 98
Cdd:PRK15482  11 ESEFTENEQKIADFLRANVSELKSVSSRKMAKQLGISQSSIVKFAQKLGAQGFTELRMALIGEYSASreKTNATALHLHS 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  99 EVSESDDAHAIGLKLQNTISNVLSETLNLLDMQQVLGVVDALRHCHSVYIFGVGSSGITALDMKHKLMRIGLRGDAVSNN 178
Cdd:PRK15482  91 SITSDDSLEVIARKLNREKELALEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKIGYRVACEADT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 179 HFMYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFCLINGNRQGMLQGDSIGTKAA 258
Cdd:PRK15482 171 HVQATVSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSGETEWRSSSMSTRTA 250

                        250
                 ....*....|....
gi 446355820 259 QLFVFDLLYTLLVQ 272
Cdd:PRK15482 251 QNSVTDLLFVGLVQ 264
PRK14101 PRK14101
bifunctional transcriptional regulator/glucokinase;
13-271 4.49e-34

bifunctional transcriptional regulator/glucokinase;


Pssm-ID: 184507 [Multi-domain]  Cd Length: 638  Bit Score: 130.81  E-value: 4.49e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  13 ILDTLGAMQKSLTRASQRIVQYILAFPRQVTQSSIADLSRDTQAGEATVIRFCRTLGYKGFQDFKMDLAIELATTesdds 92
Cdd:PRK14101 343 VFERIRQMRDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTGT----- 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  93 SPLLDAEVSESDDAHAIGLK-LQNTISNVLsETLNLLDMQQVLGVVDALRHCHSVYIFGVGSSGITALDMKHKLMRIGLR 171
Cdd:PRK14101 418 IPMSHSQVHLGDTATDFGAKvLDNTVSAIL-QLREHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIP 496

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 172 GDAVSNNHFMYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNlGSPLCEEADFclingnrqgMLQGD 251
Cdd:PRK14101 497 TIAYGDLYMQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITSS-NTPLAKRATV---------ALETD 566

                        250       260
                 ....*....|....*....|.
gi 446355820 252 SIGTKAAQL-FVFDLLYTLLV 271
Cdd:PRK14101 567 HIEMRESQLsMISRILHLVMI 587
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
23-280 2.81e-30

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 114.86  E-value: 2.81e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  23 SLTRASQRIVQYILAFPRQVTQSSIADLSRDTQAGEATVIRFCRTLGYKGFQDFKMDLAIELATTESDDSSPLLDaEVSE 102
Cdd:PRK11557   9 GLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALASQPEPPSVPVHN-QIRG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 103 SDDAHAIGLKLQNTISNVLSETLNLLDMQQVLGVVDALRHCHSVYIFGVGSSGITALDMKHKLMRIGLRGDAVSNNHFMY 182
Cdd:PRK11557  88 DDPLRLVGEKLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAERDMHALL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 183 MQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFCLINGNRQGMLQGDSIGTKAAQLFV 262
Cdd:PRK11557 168 ATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAEEQATRSAAISSTHAQGML 247

                        250
                 ....*....|....*...
gi 446355820 263 FDLLYTLLVQSSPEQARE 280
Cdd:PRK11557 248 TDLLFMALIQQDLERAPE 265
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 140-269 9.44e-21

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: 85.81  E-value: 9.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  140 LRHCHSVYIFGVGSSGITALDMKHKLMRIGLRGDAVSNNH-FMYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGA 218
Cdd:pfam01380   2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASeLRHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446355820  219 TTVAITHNLGSPLCEEADFCL-INGNRQgMLQGdSIGTKAAQLFVFDLLYTL 269
Cdd:pfam01380  82 KIIAITDSPGSPLAREADHVLyINAGPE-TGVA-STKSITAQLAALDALAVA 131
HTH_6 pfam01418
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ...
 13-86 6.36e-19

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: 79.30  E-value: 6.36e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446355820   13 ILDTLGAMQKSLTRASQRIVQYILAFPRQVTQSSIADLSRDTQAGEATVIRFCRTLGYKGFQDFKMDLAIELAT 86
Cdd:pfam01418   3 LLEKIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGELAN 76
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 146-239 6.12e-14

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: 71.08  E-value: 6.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 146 VYIFGVGSSGITALDMKHKLMR-IGLRGDAVSNNHFMYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAIT 224
Cdd:COG2222   37 VVLVGAGSSDHAAQAAAYLLERlLGIPVAALAPSELVVYPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAIT 116

                         90
                 ....*....|....*
gi 446355820 225 HNLGSPLCEEADFCL 239
Cdd:COG2222  117 NNPDSPLAEAADRVL 131
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 111-240 7.10e-14

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


Pssm-ID: 240138 [Multi-domain]  Cd Length: 179  Bit Score: 68.37  E-value: 7.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 111 LKLQNTISNVLSETLNLLDMQQVLGVVDALRHCHSVYIFGVGSSGIT--ALDMKhkLMRIGLR----GDAVSNNhfmymq 184
Cdd:cd05005    1 MEYLSLILEEIENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVakAFAMR--LMHLGLNvyvvGETTTPA------ 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446355820 185 atlLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFCLI 240
Cdd:cd05005   73 ---IGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVV 125
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 146-266 9.53e-14

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: 66.75  E-value: 9.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 146 VYIFGVGSSGITALDMKHKLMRI-GLRGDAVSNNHFMYMQATLLKaGDVAMGVSHSGTSPETVHSLRLARQAGATTVAIT 224
Cdd:cd05008    2 ILIVGCGTSYHAALVAKYLLERLaGIPVEVEAASEFRYRRPLLDE-DTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446355820 225 HNLGSPLCEEADFCLingnrqGMLQGDSIG---TKA--AQLFVFDLL 266
Cdd:cd05008   81 NVVGSTLAREADYVL------YLRAGPEISvaaTKAftSQLLALLLL 121
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 198-242 1.66e-11

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: 60.28  E-value: 1.66e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446355820 198 SHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFCLING 242
Cdd:cd05710   55 SHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVIVYG 99
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 146-225 1.93e-09

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: 53.53  E-value: 1.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 146 VYIFGVGSSGITALDMKHKLMRI-GLRGDAVSNNHFMYM-QATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAI 223
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELtGIEVVALIATELEHAsLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                 ..
gi 446355820 224 TH 225
Cdd:cd04795   81 TD 82
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 116-240 5.99e-09

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: 54.44  E-value: 5.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 116 TISNVLSETLNLLDMQQVLGVVDALRHC----HSVYIFGVGSSGITAL----DMKHKLMR-------IGLRGD-----AV 175
Cdd:cd05006    2 QESIQLKEALLELLAEAIEQAAQLLAEAllngGKILICGNGGSAADAQhfaaELVKRFEKerpglpaIALTTDtsiltAI 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 176 SN-NHFMYMQA----TLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFCLI 240
Cdd:cd05006   82 ANdYGYEEVFSrqveALGQPGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIH 151
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 183-238 2.09e-08

N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.


Pssm-ID: 240140 [Multi-domain]  Cd Length: 257  Bit Score: 54.07  E-value: 2.09e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446355820 183 MQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFC 238
Cdd:cd05007  111 LQAINLTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIA 166
murQ PRK05441
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 188-236 5.91e-08

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 235467 [Multi-domain]  Cd Length: 299  Bit Score: 52.86  E-value: 5.91e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446355820 188 LKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEAD 236
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEAD 177
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 150-266 7.04e-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: 47.54  E-value: 7.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 150 GVGSSGITALDMKHKLMRIGLRGdavsnnhfMYMQAT--------LLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTV 221
Cdd:cd05014    7 GVGKSGHIARKIAATLSSTGTPA--------FFLHPTealhgdlgMVTPGDVVIAISNSGETDELLNLLPHLKRRGAPII 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446355820 222 AITHNLGSPLCEEADFCLINGNRQGmlqGDSIGTKA-----AQLFVFDLL 266
Cdd:cd05014   79 AITGNPNSTLAKLSDVVLDLPVEEE---ACPLGLAPttsttAMLALGDAL 125
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 136-224 4.10e-06

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


Pssm-ID: 433326 [Multi-domain]  Cd Length: 138  Bit Score: 45.28  E-value: 4.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820  136 VVDALRHCHSVYIFGVGSSGITALDMKH------KLMRIGLRGDA----VSNNHFMY-----------MQATLLKAGDVA 194
Cdd:pfam13580  28 IAASLANGGKVYAFGTGHSAAPAEELFAragglaGFEPILLPALAlhtdASATISTAlerdegyarqiLALYPGRPGDVL 107

                          90       100       110
                  ....*....|....*....|....*....|
gi 446355820  195 MGVSHSGTSPETVHSLRLARQAGATTVAIT 224
Cdd:pfam13580 108 IVISNSGINAVPVEAALEAKERGMKVIALT 137
PRK13937 PRK13937
phosphoheptose isomerase; Provisional
 136-240 4.76e-06

phosphoheptose isomerase; Provisional


Pssm-ID: 184408 [Multi-domain]  Cd Length: 188  Bit Score: 46.00  E-value: 4.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 136 VVDALRHCHSVYIFGVGSSgitALDMKH---------KLMR-----IGLRGD-----AVSNN---HFMY---MQAtLLKA 190
Cdd:PRK13937  31 LIEALANGGKILLCGNGGS---AADAQHiaaelvgrfKKERpalpaIALTTDtsaltAIGNDygfERVFsrqVEA-LGRP 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446355820 191 GDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFCLI 240
Cdd:PRK13937 107 GDVLIGISTSGNSPNVLAALEKARELGMKTIGLTGRDGGKMKELCDHLLI 156
PRK12570 PRK12570
N-acetylmuramic acid-6-phosphate etherase; Reviewed
 183-236 1.30e-05

N-acetylmuramic acid-6-phosphate etherase; Reviewed


Pssm-ID: 237142 [Multi-domain]  Cd Length: 296  Bit Score: 45.84  E-value: 1.30e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446355820 183 MQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEAD 236
Cdd:PRK12570 120 LKAIGLTADDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIAD 173
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 188-240 1.49e-05

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: 45.74  E-value: 1.49e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446355820 188 LKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFCLI 240
Cdd:COG0794   89 ITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLD 141
PRK02947 PRK02947
sugar isomerase domain-containing protein;
136-242 3.52e-05

sugar isomerase domain-containing protein;


Pssm-ID: 179510 [Multi-domain]  Cd Length: 246  Bit Score: 44.09  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 136 VVDALRHCHSVYIFGVGSSGITALDM---------KHKLM--RIGLRGDAVSNNHF--------MYMQATLLKAGDVAMG 196
Cdd:PRK02947  33 IADSIRNGGLIYVFGTGHSHILAEEVfyragglapVNPILepSLMLHEGAVASSYLervegyakAILDRYDIRPGDVLIV 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446355820 197 VSHSGTSPETVHSLRLARQAGATTVAIT-----------HNLGSPLCEEADFCLING 242
Cdd:PRK02947 113 VSNSGRNPVPIEMALEAKERGAKVIAVTslaysasvasrHSSGKRLAEVADVVLDNG 169
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 187-266 6.24e-05

Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440218 [Multi-domain]  Cd Length: 610  Bit Score: 44.23  E-value: 6.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 187 LLKAGDVAMGVSHSGtspET---VHSLRLARQAGATTVAITHNLGSPLCEEADFCLIngnrqgMLQGDSIG---TKA--A 258
Cdd:COG0449  338 VVDPGTLVIAISQSG---ETadtLAALREAKEKGAKVLAICNVVGSTIARESDAVLY------THAGPEIGvasTKAftT 408


                 ....*...
gi 446355820 259 QLFVFDLL 266
Cdd:COG0449  409 QLAALYLL 416
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
187-280 1.08e-04

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 43.49  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 187 LLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFCLIngnrqgMLQGDSIG---TKA--AQLF 261
Cdd:PRK00331 333 VLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLY------THAGPEIGvasTKAftAQLA 406

                         90       100
                 ....*....|....*....|...
gi 446355820 262 VFDLLYTLLVQS----SPEQARE 280
Cdd:PRK00331 407 VLYLLALALAKArgtlSAEEEAD 429
PRK08674 PRK08674
bifunctional phosphoglucose/phosphomannose isomerase; Validated
 146-224 1.64e-04

bifunctional phosphoglucose/phosphomannose isomerase; Validated


Pssm-ID: 181536 [Multi-domain]  Cd Length: 337  Bit Score: 42.66  E-value: 1.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446355820 146 VYIFGVGSSGITAlDMKHKLMRIGLRGDAVSNNHfmYMQATLLKAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAIT 224
Cdd:PRK08674  37 IVISGMGGSGIGG-DLLRILLFDELKVPVFVNRD--YTLPAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKIIAIT 112
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 146-224 1.74e-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: 40.33  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 146 VYIFGVGSSGITAlDMKHKLMRIGLRG-DAVSNNHFMYMQA---TLLKAgdvamgVSHSGTSPETVHSLRLARQAGATTV 221
Cdd:cd05017    2 IVILGMGGSGIGG-DLLESLLLDEAKIpVYVVKDYTLPAFVdrkTLVIA------VSYSGNTEETLSAVEQAKERGAKIV 74


                 ...
gi 446355820 222 AIT 224
Cdd:cd05017   75 AIT 77
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 192-283 1.44e-03

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 39.86  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 192 DVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFCLIngnrqgMLQGDSIG---TKA--AQLFVFDLL 266
Cdd:PTZ00394 403 DVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIH------LNAGVEVGvasTKAytSQVVVLTLV 476

                         90
                 ....*....|....*...
gi 446355820 267 YTLLVQSS-PEQARESKL 283
Cdd:PTZ00394 477 ALLLSSDSvRLQERRNEI 494
PRK13938 PRK13938
phosphoheptose isomerase; Provisional
 189-241 1.53e-03

phosphoheptose isomerase; Provisional


Pssm-ID: 139997 [Multi-domain]  Cd Length: 196  Bit Score: 38.95  E-value: 1.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446355820 189 KAGDVAMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFcLIN 241
Cdd:PRK13938 112 RPGDTLFAISTSGNSMSVLRAAKTARELGVTVVAMTGESGGQLAEFADF-LIN 163
frlB PRK11382
fructoselysine 6-phosphate deglycase;
119-239 1.56e-03

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 39.60  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446355820 119 NVLSETLNLL--DMQQVLGVVDAL--RHCHSVYIFGVGSSGITALDMKHKLMRIG-LRGDAVSNNHFMYMQATLLKAGDV 193
Cdd:PRK11382  16 NMVQEVEKVLshDVPLVHAIVEEMvkRDIDRIYFVACGSPLNAAQTAKHLADRFSdLQVYAISGWEFCDNTPYRLDDRCA 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446355820 194 AMGVSHSGTSPETVHSLRLARQAGATTVAITHNLGSPLCEEADFCL 239
Cdd:PRK11382  96 VIGVSDYGKTEEVIKALELGRACGALTAAFTKRADSPITSAAEFSI 141
 
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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