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Conserved domains on  [gi|636385639|gb|KDL62843|]
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hypothetical protein AD94_00067 [Klebsiella variicola]

Protein Classification

SIS domain-containing protein( domain architecture ID 11454870)

SIS (sugar isomerase) domain-containing protein such as Bacillus subtilis fructosamine deglycase FrlB, which catalyzes the conversion of a range of fructosamine 6-phosphates to glucose 6-phosphate and a free amino acid

CATH:  3.40.50.10490
EC:  3.5.-.-
Gene Ontology:  GO:0097367|GO:0005975|GO:0016787
PubMed:  10203754
SCOP:  4000802

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 9-336 1.17e-51

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: 174.32  E-value: 1.17e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639   9 IREEPACLAQILRGYRQKLAAIETFARQHPVRRILLLATGSSLNAALCARYFFEQRFGVLVDIKEPYNFTHYEA-IDPHT 87
Cdd:COG2222    4 IAQQPEAWRRALAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAyLKLEG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  88 DLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVLDINTGIESvGFV-TRGFSATVLNLLLIALIIA 166
Cdd:COG2222   84 TLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEK-SVAaTKSFTTMLLALLALLAAWG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 167 rqqgkvsevEEQHYLAEFQRLLAAIPDVIARTSRFIDRYSetLRSGERFVATGYGALVGVAKEFETKFTETVRVPSSGFE 246
Cdd:COG2222  163 ---------GDDALLAALDALPAALEAALAADWPAAALAA--LADAERVVFLGRGPLYGLAREAALKLKELSAGHAEAYS 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 247 LEAYMHGPY--LEANTRHVMLFIEDAPDARTRALRDYMAPSIARAFTLTlSDDEDAQTLALNCPCEHHLAPLLLIVPVQM 324
Cdd:COG2222  232 AAEFRHGPKslVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIG-AEDDAAITLPAIPDLHDALDPLLLLVVAQR 310

                        330
                 ....*....|..
gi 636385639 325 LAWHTAGLKGID 336
Cdd:COG2222  311 LALALALARGLD 322
 
Name Accession Description Interval E-value
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 9-336 1.17e-51

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: 174.32  E-value: 1.17e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639   9 IREEPACLAQILRGYRQKLAAIETFARQHPVRRILLLATGSSLNAALCARYFFEQRFGVLVDIKEPYNFTHYEA-IDPHT 87
Cdd:COG2222    4 IAQQPEAWRRALAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAyLKLEG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  88 DLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVLDINTGIESvGFV-TRGFSATVLNLLLIALIIA 166
Cdd:COG2222   84 TLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEK-SVAaTKSFTTMLLALLALLAAWG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 167 rqqgkvsevEEQHYLAEFQRLLAAIPDVIARTSRFIDRYSetLRSGERFVATGYGALVGVAKEFETKFTETVRVPSSGFE 246
Cdd:COG2222  163 ---------GDDALLAALDALPAALEAALAADWPAAALAA--LADAERVVFLGRGPLYGLAREAALKLKELSAGHAEAYS 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 247 LEAYMHGPY--LEANTRHVMLFIEDAPDARTRALRDYMAPSIARAFTLTlSDDEDAQTLALNCPCEHHLAPLLLIVPVQM 324
Cdd:COG2222  232 AAEFRHGPKslVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIG-AEDDAAITLPAIPDLHDALDPLLLLVVAQR 310

                        330
                 ....*....|..
gi 636385639 325 LAWHTAGLKGID 336
Cdd:COG2222  311 LALALALARGLD 322
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 41-155 1.00e-35

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: 126.46  E-value: 1.00e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  41 RILLLATGSSLNAALCARYFFEQRFGVLVDIKEPYNFTHYEAIDPHTDLVVAISQSGKSASTLEAMRKVQASGLPVFALT 120
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 636385639 121 SDPQSPIARACDGVLDINTGIESVGFVTRGFSATV 155
Cdd:cd05008   81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQL 115
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
9-339 1.22e-25

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 107.82  E-value: 1.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639   9 IREEPACLAQILRGYRQKLAAIETFARQ-HPVRRILLLATGSSLNAALCARYFFEQ--RFGVLVDI------KEPYnfth 79
Cdd:PRK00331 258 IYEQPEAIRDTLEGRLDELGEGELADEDlKKIDRIYIVACGTSYHAGLVAKYLIESlaGIPVEVEIasefryRDPV---- 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  80 yeaIDPHTdLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVLDINTGIEsVGfV--TRGFSATVLN 157
Cdd:PRK00331 334 ---LSPKT-LVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPE-IG-VasTKAFTAQLAV 407

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 158 LLLIALIIARQQGKVSEVEEQHYLAEFQRLLAAIPDVIARTSRfIDRYSETLRSGERFVATGYGALVGVAKEFETKFTET 237
Cdd:PRK00331 408 LYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLDLKEQ-IEELAEDFADARNALFLGRGVDYPVALEGALKLKEI 486

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 238 vrvpssgfeleAYM-----------HGP--YLEANTRHVMLfiedAPDARTRA-LRDYMAPSIAR-AFTLTLSDDEDA-- 300
Cdd:PRK00331 487 -----------SYIhaegyaagelkHGPiaLIDEGMPVVAI----APNDELYEkTKSNIQEVKARgARVIVIADEGDEva 551

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 636385639 301 ----QTLALNcPCEHHLAPLLLIVPVQMLAWHTAGLKGID------LAK 339
Cdd:PRK00331 552 eeadDVIEVP-EVHELLAPLLYVVPLQLLAYHVALARGTDvdkprnLAK 599
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 40-154 9.32e-13

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: 64.63  E-value: 9.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639   40 RRILLLATGSSLNAALCARYFFEQrfgvlvdIKEPYNFTHYEAIDPHT--------DLVVAISQSGKSASTLEAMRKVQA 111
Cdd:pfam01380   6 KRIFVIGRGTSYAIALELALKFEE-------IGYKVVEVELASELRHGvlalvdedDLVIAISYSGETKDLLAAAELAKA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 636385639  112 SGLPVFALTSDPQSPIARACDGVLDINTGIESVGFVTRGFSAT 154
Cdd:pfam01380  79 RGAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQ 121
 
Name Accession Description Interval E-value
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 9-336 1.17e-51

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: 174.32  E-value: 1.17e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639   9 IREEPACLAQILRGYRQKLAAIETFARQHPVRRILLLATGSSLNAALCARYFFEQRFGVLVDIKEPYNFTHYEA-IDPHT 87
Cdd:COG2222    4 IAQQPEAWRRALAALAAAIAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAyLKLEG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  88 DLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVLDINTGIESvGFV-TRGFSATVLNLLLIALIIA 166
Cdd:COG2222   84 TLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEK-SVAaTKSFTTMLLALLALLAAWG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 167 rqqgkvsevEEQHYLAEFQRLLAAIPDVIARTSRFIDRYSetLRSGERFVATGYGALVGVAKEFETKFTETVRVPSSGFE 246
Cdd:COG2222  163 ---------GDDALLAALDALPAALEAALAADWPAAALAA--LADAERVVFLGRGPLYGLAREAALKLKELSAGHAEAYS 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 247 LEAYMHGPY--LEANTRHVMLFIEDAPDARTRALRDYMAPSIARAFTLTlSDDEDAQTLALNCPCEHHLAPLLLIVPVQM 324
Cdd:COG2222  232 AAEFRHGPKslVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIG-AEDDAAITLPAIPDLHDALDPLLLLVVAQR 310

                        330
                 ....*....|..
gi 636385639 325 LAWHTAGLKGID 336
Cdd:COG2222  311 LALALALARGLD 322
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 41-155 1.00e-35

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: 126.46  E-value: 1.00e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  41 RILLLATGSSLNAALCARYFFEQRFGVLVDIKEPYNFTHYEAIDPHTDLVVAISQSGKSASTLEAMRKVQASGLPVFALT 120
Cdd:cd05008    1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 636385639 121 SDPQSPIARACDGVLDINTGIESVGFVTRGFSATV 155
Cdd:cd05008   81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQL 115
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 9-339 1.03e-29

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: 119.73  E-value: 1.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639   9 IREEPACLAQILRGY-----RQKLAAIETFARQ-HPVRRILLLATGSSLNAALCARYFFEQ--RFGVLVDI-KEpynFTH 79
Cdd:COG0449  258 IHEQPEAIRDTLRGRldedgRVVLDELNLAAEDlRNIDRIYIVACGTSYHAGLVGKYLIEElaRIPVEVEIaSE---FRY 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  80 YEAIDPHTDLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVLDINTGIEsVGfV--TRGFSATVLN 157
Cdd:COG0449  335 RDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPE-IG-VasTKAFTTQLAA 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 158 LLLIALIIARQQGKVSEVEEQHYLAEFQRLLAAIPDVIARTSRfIDRYSETLRSGERFV----ATGY-----GALvgvak 228
Cdd:COG0449  413 LYLLALYLARARGTLSAEEEAELLEELRKLPEKIEEVLDLEEQ-IEELAEKYADARNALflgrGINYpvaleGAL----- 486

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 229 efetKFTETVRVPSSGF---ELEaymHGP--YLEANTrhVMLFIedAPDartRALRDYMAPSI----AR-AFTLTLSDDE 298
Cdd:COG0449  487 ----KLKEISYIHAEGYaagELK---HGPiaLIDEGM--PVVAI--APQ---DELYEKTLSNIqevkARgGKVIAIADEG 552

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 636385639 299 DAQTLALNC------PCEHHLAPLLLIVPVQMLAWHTAGLKGID------LAK 339
Cdd:COG0449  553 DEEVEELADdvievpEVDELLAPILAVVPLQLLAYHVAVLRGTDvdqprnLAK 605
SIS_GlmS_GlmD_2 cd05009
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 202-346 1.83e-26

SIS (Sugar ISomerase) domain repeat 2 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: 240142 [Multi-domain]  Cd Length: 153  Bit Score: 102.73  E-value: 1.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 202 IDRYSETLRSGERFVATGYGALVGVAKEFETKFTETVRVPSSGFELEAYMHGPY--LEANTRHVMLFIEDAPDARTRALR 279
Cdd:cd05009    3 IKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIalVDEGTPVIFLAPEDRLEEKLESLI 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636385639 280 DYMApsiAR-AFTLTLSDDEDAQTLA----LNCPCEHHLAPLLLIVPVQMLAWHTAGLKGIDLAKRIFDDFD 346
Cdd:cd05009   83 KEVK---ARgAKVIVITDDGDAKDLAdvviRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKS 151
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
9-339 1.22e-25

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 107.82  E-value: 1.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639   9 IREEPACLAQILRGYRQKLAAIETFARQ-HPVRRILLLATGSSLNAALCARYFFEQ--RFGVLVDI------KEPYnfth 79
Cdd:PRK00331 258 IYEQPEAIRDTLEGRLDELGEGELADEDlKKIDRIYIVACGTSYHAGLVAKYLIESlaGIPVEVEIasefryRDPV---- 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  80 yeaIDPHTdLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVLDINTGIEsVGfV--TRGFSATVLN 157
Cdd:PRK00331 334 ---LSPKT-LVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPE-IG-VasTKAFTAQLAV 407

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 158 LLLIALIIARQQGKVSEVEEQHYLAEFQRLLAAIPDVIARTSRfIDRYSETLRSGERFVATGYGALVGVAKEFETKFTET 237
Cdd:PRK00331 408 LYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLDLKEQ-IEELAEDFADARNALFLGRGVDYPVALEGALKLKEI 486

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 238 vrvpssgfeleAYM-----------HGP--YLEANTRHVMLfiedAPDARTRA-LRDYMAPSIAR-AFTLTLSDDEDA-- 300
Cdd:PRK00331 487 -----------SYIhaegyaagelkHGPiaLIDEGMPVVAI----APNDELYEkTKSNIQEVKARgARVIVIADEGDEva 551

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 636385639 301 ----QTLALNcPCEHHLAPLLLIVPVQMLAWHTAGLKGID------LAK 339
Cdd:PRK00331 552 eeadDVIEVP-EVHELLAPLLYVVPLQLLAYHVALARGTDvdkprnLAK 599
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 9-339 3.84e-17

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 82.38  E-value: 3.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639   9 IREEPACLAQILrGYRQKLAAIETFAR-----QH-----PVRRILLLATGSSLNAALCARYFFeQRFGV--LVDIKEPYN 76
Cdd:PTZ00295 283 IFEQPIALSRAL-NNGGRLSGYNNRVKlggldQYleellNIKNLILVGCGTSYYAALFAASIM-QKLKCfnTVQVIDASE 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  77 FTHYEAIDPHTDlVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVLDINTGIESVGFVTRGFSATVL 156
Cdd:PTZ00295 361 LTLYRLPDEDAG-VIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVASTKAFTSQVT 439

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 157 NLLLIALIIArqQGKVSEVEEQHyLAEFQRLLAAIPDVIARTSRF----IDRYSETLRSGERFVATGYGALVGVAKEFET 232
Cdd:PTZ00295 440 VLSLIALWFA--QNKEYSCSNYK-CSSLINSLHRLPTYIGMTLKSceeqCKRIAEKLKNAKSMFILGKGLGYPIALEGAL 516

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 233 KFTETVRVPSSGFELEAYMHGPYL----EANTRhVMLFIEDapDARTRALRDYMAPSIAR-AFTLTLSDDED-----AQT 302
Cdd:PTZ00295 517 KIKEITYIHAEGFSGGALKHGPFAlidkEKNTP-VILIILD--DEHKELMINAAEQVKARgAYIIVITDDEDlvkdfADE 593

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 636385639 303 LALNCPCEhHLAPLLLIVPVQMLAWHTAGLKGID------LAK 339
Cdd:PTZ00295 594 IILIPSNG-PLTALLAVIPLQLLAYEIAILRGINpdkprgLAK 635
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 40-139 1.94e-14

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: 69.57  E-value: 1.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  40 RRILLLATGSSlnaALCARYFFeQRFGVLVDIKEPYNFTHYEAIDPHT----DLVVAISQSGKSASTLEAMRKVQASGLP 115
Cdd:cd05013   14 RRIYIFGVGSS---GLVAEYLA-YKLLRLGKPVVLLSDPHLQLMSAANltpgDVVIAISFSGETKETVEAAEIAKERGAK 89

                         90       100
                 ....*....|....*....|....
gi 636385639 116 VFALTSDPQSPIARACDGVLDINT 139
Cdd:cd05013   90 VIAITDSANSPLAKLADIVLLVSS 113
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 40-334 8.21e-14

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 72.60  E-value: 8.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  40 RRILLLATGSSLNAALCARYFFEQRFGVLVDIKEPYNFTHYEAIDPHTDLVVAISQSGKSASTLEAMRKVQASGLPVFAL 119
Cdd:PTZ00394 355 RRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGI 434

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 120 TSDPQSPIARACDGVLDINTGIESVGFVTRGFSATVLNLLLIALIIARQQGKVseveeQHYLAEFQRLLAAIPDVIARTS 199
Cdd:PTZ00394 435 TNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLLSSDSVRL-----QERRNEIIRGLAELPAAISECL 509

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639 200 RF----IDRYSETLRSGERFVATGYGALVGVAKEFETKFTETVRVPSSGFELEAYMHGP--YLEANTRHVMLFIEDAPDA 273
Cdd:PTZ00394 510 KIthdpVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGIHSGELKHGPlaLIDETSPVLAMCTHDKHFG 589

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636385639 274 RTRALRDYMAPSIARAFTLTLSDD---EDAQTLALNCP----CehhLAPLLLIVPVQMLAWHTAGLKG 334
Cdd:PTZ00394 590 LSKSAVQQVKARGGAVVVFATEVDaelKAAASEIVLVPktvdC---LQCVVNVIPFQLLAYYMALLRG 654
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 40-154 9.32e-13

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: 64.63  E-value: 9.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639   40 RRILLLATGSSLNAALCARYFFEQrfgvlvdIKEPYNFTHYEAIDPHT--------DLVVAISQSGKSASTLEAMRKVQA 111
Cdd:pfam01380   6 KRIFVIGRGTSYAIALELALKFEE-------IGYKVVEVELASELRHGvlalvdedDLVIAISYSGETKDLLAAAELAKA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 636385639  112 SGLPVFALTSDPQSPIARACDGVLDINTGIESVGFVTRGFSAT 154
Cdd:pfam01380  79 RGAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQ 121
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 40-135 4.33e-11

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


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 62.64  E-value: 4.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  40 RRILLLATGSSLNAALCARYFFeQRFGVLVdikepynftHYEAIDPHT-----------DLVVAISQSGKSASTLEAMRK 108
Cdd:COG1737  135 RRIYIFGVGASAPVAEDLAYKL-LRLGKNV---------VLLDGDGHLqaesaallgpgDVVIAISFSGYTRETLEAARL 204

                         90       100
                 ....*....|....*....|....*..
gi 636385639 109 VQASGLPVFALTSDPQSPIARACDGVL 135
Cdd:COG1737  205 AKERGAKVIAITDSPLSPLAKLADVVL 231
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 5-142 1.63e-09

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 59.38  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639   5 MMTYIREEPACLAQILRG----------YRQKLAAIETFARQ-HPVRRILLLATGSSLNAALCARYFFEQRFGVLVDIKE 73
Cdd:PLN02981 318 MQKEIHEQPESLTTTMRGrlirggsgkaKRVLLGGLKDHLKTiRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMEL 397

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636385639  74 PYNFTHYEAIDPHTDLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVLDINTGIE 142
Cdd:PLN02981 398 ASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAE 466
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 82-137 1.04e-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: 51.42  E-value: 1.04e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 636385639  82 AIDPHtDLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVLDI 137
Cdd:cd05005   72 AIGPG-DLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVI 126
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 88-137 1.56e-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: 49.46  E-value: 1.56e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 636385639  88 DLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVLDI 137
Cdd:cd05014   49 DVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDL 98
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 41-132 3.91e-07

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: 48.34  E-value: 3.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  41 RILLLATGSSLNAALCARYFFEQR--FGVLVDIKEPYNFTHYEAIDPHTdLVVAISQSGKSASTLEAMRKVQASGLPVFA 118
Cdd:cd05710    1 NVFFVGCGGSLADMYPAKYFLKKEskLPVFVYNAAEFLHTGPKRLTEKS-VVILASHSGNTKETVAAAKFAKEKGATVIG 79

                         90
                 ....*....|....
gi 636385639 119 LTSDPQSPIARACD 132
Cdd:cd05710   80 LTDDEDSPLAKLAD 93
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 88-137 6.29e-06

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: 47.28  E-value: 6.29e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 636385639  88 DLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVLDI 137
Cdd:COG0794   93 DVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDL 142
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
88-137 5.21e-05

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 44.37  E-value: 5.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 636385639  88 DLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVLDI 137
Cdd:PRK11543  91 DVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDI 140
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
87-135 1.22e-04

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 43.21  E-value: 1.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 636385639  87 TDLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVL 135
Cdd:PRK11337 188 GDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVI 236
PRK11302 PRK11302
DNA-binding transcriptional regulator HexR; Provisional
 40-137 3.88e-04

DNA-binding transcriptional regulator HexR; Provisional


Pssm-ID: 183082 [Multi-domain]  Cd Length: 284  Bit Score: 41.52  E-value: 3.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  40 RRILLLATGSSLNAALCARY-FFeqRFGVLVDIKEPYNFTHYEAIDPHT-DLVVAISQSGKSASTLEAMRKVQASGLPVF 117
Cdd:PRK11302 129 KKISFFGLGASAAVAHDAQNkFF--RFNVPVVYFDDIVMQRMSCMNSSDgDVVVLISHTGRTKSLVELAQLARENGATVI 206

                         90       100
                 ....*....|....*....|
gi 636385639 118 ALTSdPQSPIARACDGVLDI 137
Cdd:PRK11302 207 AITS-AGSPLAREATLALTL 225
SIS_Etherase cd05007
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ...
 88-149 4.67e-04

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: 41.35  E-value: 4.67e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636385639  88 DLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIARACDGVLDINTGIESVGFVTR 149
Cdd:cd05007  120 DVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTR 181
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 42-120 7.35e-04

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: 38.12  E-value: 7.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  42 ILLLATGSSLNAALCARYFFEQRFGVLVDIKEPYNFTHYE--AIDPHTDLVVAISQSGKSASTLEAMRKVQASGLPVFAL 119
Cdd:cd04795    1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASllSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                 .
gi 636385639 120 T 120
Cdd:cd04795   81 T 81
SIS_PGI_PMI_1 cd05017
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ...
 41-121 9.51e-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: 9.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  41 RILLLATGSSLNAALCARYFFEQRFGVLVDIKEPYNFTHYeaIDPHTdLVVAISQSGKSASTLEAMRKVQASGLPVFALT 120
Cdd:cd05017    1 NIVILGMGGSGIGGDLLESLLLDEAKIPVYVVKDYTLPAF--VDRKT-LVIAVSYSGNTEETLSAVEQAKERGAKIVAIT 77


                 .
gi 636385639 121 S 121
Cdd:cd05017   78 S 78
SIS_2 pfam13580
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 27-121 9.95e-04

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: 38.73  E-value: 9.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639   27 LAAIETFARQ---HPVRRILLLATGSSLNAALCARYFFEQRFGVLVDIKEPYNfthyeaIDPHtDLVVAISQSGKSASTL 103
Cdd:pfam13580  48 APAEELFARAgglAGFEPILLPALALHTDASATISTALERDEGYARQILALYP------GRPG-DVLIVISNSGINAVPV 120

                          90
                  ....*....|....*...
gi 636385639  104 EAMRKVQASGLPVFALTS 121
Cdd:pfam13580 121 EAALEAKERGMKVIALTS 138
frlB PRK11382
fructoselysine 6-phosphate deglycase;
36-136 1.22e-03

fructoselysine 6-phosphate deglycase;


Pssm-ID: 183111 [Multi-domain]  Cd Length: 340  Bit Score: 40.37  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385639  36 QHPVRRILLLATGSSLNAALCARYFFEqRFGVLvdikEPYNFTHYEAID--PH----TDLVVAISQSGKSASTLEAMRKV 109
Cdd:PRK11382  41 KRDIDRIYFVACGSPLNAAQTAKHLAD-RFSDL----QVYAISGWEFCDntPYrlddRCAVIGVSDYGKTEEVIKALELG 115

                         90       100
                 ....*....|....*....|....*..
gi 636385639 110 QASGLPVFALTSDPQSPIARACDGVLD 136
Cdd:PRK11382 116 RACGALTAAFTKRADSPITSAAEFSID 142
gmhA PRK00414
D-sedoheptulose 7-phosphate isomerase;
75-149 3.26e-03

D-sedoheptulose 7-phosphate isomerase;


Pssm-ID: 179012 [Multi-domain]  Cd Length: 192  Bit Score: 38.18  E-value: 3.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636385639  75 YNFTHY-EAIDPHTDLVVAISQSGKSASTLEAMRKVQASGLPVFALTSDPQSPIAracdGVLDINTGIESVGFVTR 149
Cdd:PRK00414  99 YVFSRYvEAVGREGDVLLGISTSGNSGNIIKAIEAARAKGMKVITLTGKDGGKMA----GLADIEIRVPHFGYADR 170
 
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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