NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1268092029|ref|WP_098659845|]
View 

LysR family transcriptional regulator [Bacillus thuringiensis]

Protein Classification

LysR family transcriptional regulator( domain architecture ID 11426483)

LysR family transcriptional regulator containing an N-terminal HTH (helix-turn-helix) DNA-binding domain and a C-terminal substrate binding domain, which is structurally homologous to the type 2 periplasmic-binding (PBP2) fold proteins

CATH:  3.40.190.10
Gene Ontology:  GO:0003700|GO:0003677|GO:0006355
PubMed:  19047729|8257110|15808743
SCOP:  4000316

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
1-150 1.28e-25

DNA-binding transcriptional regulator, LysR family [Transcription];


:

Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 102.25  E-value: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029   1 MNIEQLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEGLHIIKNAYDALEKIDEIFE 80
Cdd:COG0583     1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268092029  81 YTKDKRVYPKLRMKIAVVPGVIP-PLVEAISELNDEFPFVEVEITQGKTQQVFTLLQLEQVDCALIIDSDD 150
Cdd:COG0583    81 ELRALRGGPRGTLRIGAPPSLARyLLPPLLARFRARHPGVRLELREGNSDRLVDALLEGELDLAIRLGPPP 151
LysR_substrate super family cl47814
LysR substrate binding domain; The structure of this domain is known and is similar to the ...
 94-279 1.51e-09

LysR substrate binding domain; The structure of this domain is known and is similar to the periplasmic binding proteins. This domain binds a variety of ligands that caries in size and structure, such as amino acids, sugar phosphates, organic acids, metal cations, flavonoids, C6-ring carboxylic acids, H2O2, HOCl, homocysteine, NADPH, ATP, sulphate, muropeptides, acetate, salicylate, citrate, phenol- and quinolone derivatives, acetylserines, fatty acid CoA, shikimate, chorismate, homocysteine, indole-3-acetic acid, Na(I), c-di-GMP, ppGpp and hydrogen peroxide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


The actual alignment was detected with superfamily member pfam03466:

Pssm-ID: 460931 [Multi-domain]  Cd Length: 205  Bit Score: 56.53  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029  94 KIAVVPGVIP-PLVEAISELNDEFPFVEVEITQGKTQQVFTLLQLEQVDCALIIDSDDIKNknfpFNIRKVCNGKLYIAM 172
Cdd:pfam03466   5 RIGAPPTLASyLLPPLLARFRERYPDVELELTEGNSEELLDLLLEGELDLAIRRGPPDDPG----LEARPLGEEPLVLVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029 173 NRNSKLSLYNPLNYKTLIKEPLVLYKDEYIL-NYVKYIENKTGEHSNILFQTNNTNSIIYAVKNNFANTIALDFTFDNKY 251
Cdd:pfam03466  81 PPDHPLARGEPVSLEDLADEPLILLPPGSGLrDLLDRALRAAGLRPRVVLEVNSLEALLQLVAAGLGIALLPRSAVAREL 160

                         170       180
                  ....*....|....*....|....*...
gi 1268092029 252 RDfyNEIKQVPIEDDEnwKTISLWFCYP 279
Cdd:pfam03466 161 AD--GRLVALPLPEPP--LPRELYLVWR 184
 
Name Accession Description Interval E-value
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
1-150 1.28e-25

DNA-binding transcriptional regulator, LysR family [Transcription];


Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 102.25  E-value: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029   1 MNIEQLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEGLHIIKNAYDALEKIDEIFE 80
Cdd:COG0583     1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268092029  81 YTKDKRVYPKLRMKIAVVPGVIP-PLVEAISELNDEFPFVEVEITQGKTQQVFTLLQLEQVDCALIIDSDD 150
Cdd:COG0583    81 ELRALRGGPRGTLRIGAPPSLARyLLPPLLARFRARHPGVRLELREGNSDRLVDALLEGELDLAIRLGPPP 151
HTH_1 pfam00126
Bacterial regulatory helix-turn-helix protein, lysR family;
3-61 1.02e-15

Bacterial regulatory helix-turn-helix protein, lysR family;


Pssm-ID: 459683 [Multi-domain]  Cd Length: 60  Bit Score: 70.11  E-value: 1.02e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1268092029   3 IEQLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEG 61
Cdd:pfam00126   1 LRQLRLFVAVAETGSFTAAAERLGLSQPAVSRQIKRLEEELGVPLFERTTRGVRLTEAG 59
LysR_substrate pfam03466
LysR substrate binding domain; The structure of this domain is known and is similar to the ...
 94-279 1.51e-09

LysR substrate binding domain; The structure of this domain is known and is similar to the periplasmic binding proteins. This domain binds a variety of ligands that caries in size and structure, such as amino acids, sugar phosphates, organic acids, metal cations, flavonoids, C6-ring carboxylic acids, H2O2, HOCl, homocysteine, NADPH, ATP, sulphate, muropeptides, acetate, salicylate, citrate, phenol- and quinolone derivatives, acetylserines, fatty acid CoA, shikimate, chorismate, homocysteine, indole-3-acetic acid, Na(I), c-di-GMP, ppGpp and hydrogen peroxide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460931 [Multi-domain]  Cd Length: 205  Bit Score: 56.53  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029  94 KIAVVPGVIP-PLVEAISELNDEFPFVEVEITQGKTQQVFTLLQLEQVDCALIIDSDDIKNknfpFNIRKVCNGKLYIAM 172
Cdd:pfam03466   5 RIGAPPTLASyLLPPLLARFRERYPDVELELTEGNSEELLDLLLEGELDLAIRRGPPDDPG----LEARPLGEEPLVLVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029 173 NRNSKLSLYNPLNYKTLIKEPLVLYKDEYIL-NYVKYIENKTGEHSNILFQTNNTNSIIYAVKNNFANTIALDFTFDNKY 251
Cdd:pfam03466  81 PPDHPLARGEPVSLEDLADEPLILLPPGSGLrDLLDRALRAAGLRPRVVLEVNSLEALLQLVAAGLGIALLPRSAVAREL 160

                         170       180
                  ....*....|....*....|....*...
gi 1268092029 252 RDfyNEIKQVPIEDDEnwKTISLWFCYP 279
Cdd:pfam03466 161 AD--GRLVALPLPEPP--LPRELYLVWR 184
PBP2_LTTR_substrate cd05466
The substrate binding domain of LysR-type transcriptional regulators (LTTRs), a member of the ...
 92-243 2.09e-09

The substrate binding domain of LysR-type transcriptional regulators (LTTRs), a member of the type 2 periplasmic binding fold protein superfamily; This model and hierarchy represent the the substrate-binding domain of the LysR-type transcriptional regulators that form the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, oxidative stress responses, nodule formation of nitrogen-fixing bacteria, synthesis of virulence factors, toxin production, attachment and secretion, to name a few. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate-binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 176102 [Multi-domain]  Cd Length: 197  Bit Score: 56.07  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029  92 RMKIAVVPGVIPPLV-EAISELNDEFPFVEVEITQGKTQQVFTLLQLEQVDCALIIDSDDIKNknfpFNIRKVCNGKLYI 170
Cdd:cd05466     1 TLRIGASPSIAAYLLpPLLAAFRQRYPGVELSLVEGGSSELLEALLEGELDLAIVALPVDDPG----LESEPLFEEPLVL 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1268092029 171 AMNRNSKLSLYNPLNYKTLIKEPLVLYKDEYILN-YVKYIENKTGEHSNILFQTNNTNSIIYAVKNNFAntIAL 243
Cdd:cd05466    77 VVPPDHPLAKRKSVTLADLADEPLILFERGSGLRrLLDRAFAEAGFTPNIALEVDSLEAIKALVAAGLG--IAL 148
PRK11151 PRK11151
DNA-binding transcriptional regulator OxyR; Provisional
 1-145 1.24e-07

DNA-binding transcriptional regulator OxyR; Provisional


Pssm-ID: 182999 [Multi-domain]  Cd Length: 305  Bit Score: 51.95  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029   1 MNIEQLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEGLHIIKNAYDALEKIDEIFE 80
Cdd:PRK11151    1 MNIRDLEYLVALAEHRHFRRAADSCHVSQPTLSGQIRKLEDELGVMLLERTSRKVLFTQAGLLLVDQARTVLREVKVLKE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268092029  81 YTKDKRVYPKLRMKIAVVPGVIPPLV-EAISELNDEFPFVEVEITQGKTQQVftLLQLE--QVDCALI 145
Cdd:PRK11151   81 MASQQGETMSGPLHIGLIPTVGPYLLpHIIPMLHQTFPKLEMYLHEAQTHQL--LAQLDsgKLDCAIL 146
PBP2_CysL_like cd08420
C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which ...
 101-196 9.09e-05

C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which activates the transcription of the cysJI operon encoding sulfite reductase, contains the type 2 periplasmic binding fold; CysL, also known as YwfK, is a regular of sulfur metabolism in Bacillus subtilis. Sulfur is required for the synthesis of proteins and essential cofactors in all living organism. Sulfur can be assimilated either from inorganic sources (sulfate and thiosulfate), or from organic sources (sulfate esters, sulfamates, and sulfonates). CysL activates the transcription of the cysJI operon encoding sulfite reductase, which reduces sulfite to sulfide. Both cysL mutant and cysJI mutant are unable to grow using sulfate or sulfite as the sulfur source. Like other LysR-type regulators, CysL also negatively regulates its own transcription. In Escherichia coli, three LysR-type activators are involved in the regulation of sulfur metabolism: CysB, Cbl and MetR. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 176112 [Multi-domain]  Cd Length: 201  Bit Score: 42.48  E-value: 9.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029 101 VIPPLveaISELNDEFPFVEVEITQGKTQQVFTLLQLEQVDCALI---IDSDDIKnknfpfnIRKVCNGKLYIAMNRNSK 177
Cdd:cd08420    14 LLPRL---LARFRKRYPEVRVSLTIGNTEEIAERVLDGEIDLGLVegpVDHPDLI-------VEPFAEDELVLVVPPDHP 83

                          90
                  ....*....|....*....
gi 1268092029 178 LSLYNPLNYKTLIKEPLVL 196
Cdd:cd08420    84 LAGRKEVTAEELAAEPWIL 102
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
1-86 5.43e-03

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 35.65  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029    1 MNIEQLKLIVTLSEER--KLSRVAKKLNLTPSAVCQGIKKLEKElntPLFNRTKDGT-------YPTVEGLHIIKNAYDA 71
Cdd:smart00347   8 LTPTQFLVLRILYEEGplSVSELAKRLGVSPSTVTRVLDRLEKK---GLVRREPSPEdrrsvlvSLTEEGRELIEQLLEA 84

                           90
                   ....*....|....*..
gi 1268092029   72 LEK-IDEIF-EYTKDKR 86
Cdd:smart00347  85 RSEtLAELLaGLTAEEQ 101
 
Name Accession Description Interval E-value
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
1-150 1.28e-25

DNA-binding transcriptional regulator, LysR family [Transcription];


Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 102.25  E-value: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029   1 MNIEQLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEGLHIIKNAYDALEKIDEIFE 80
Cdd:COG0583     1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268092029  81 YTKDKRVYPKLRMKIAVVPGVIP-PLVEAISELNDEFPFVEVEITQGKTQQVFTLLQLEQVDCALIIDSDD 150
Cdd:COG0583    81 ELRALRGGPRGTLRIGAPPSLARyLLPPLLARFRARHPGVRLELREGNSDRLVDALLEGELDLAIRLGPPP 151
HTH_1 pfam00126
Bacterial regulatory helix-turn-helix protein, lysR family;
3-61 1.02e-15

Bacterial regulatory helix-turn-helix protein, lysR family;


Pssm-ID: 459683 [Multi-domain]  Cd Length: 60  Bit Score: 70.11  E-value: 1.02e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1268092029   3 IEQLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEG 61
Cdd:pfam00126   1 LRQLRLFVAVAETGSFTAAAERLGLSQPAVSRQIKRLEEELGVPLFERTTRGVRLTEAG 59
LysR_substrate pfam03466
LysR substrate binding domain; The structure of this domain is known and is similar to the ...
 94-279 1.51e-09

LysR substrate binding domain; The structure of this domain is known and is similar to the periplasmic binding proteins. This domain binds a variety of ligands that caries in size and structure, such as amino acids, sugar phosphates, organic acids, metal cations, flavonoids, C6-ring carboxylic acids, H2O2, HOCl, homocysteine, NADPH, ATP, sulphate, muropeptides, acetate, salicylate, citrate, phenol- and quinolone derivatives, acetylserines, fatty acid CoA, shikimate, chorismate, homocysteine, indole-3-acetic acid, Na(I), c-di-GMP, ppGpp and hydrogen peroxide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460931 [Multi-domain]  Cd Length: 205  Bit Score: 56.53  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029  94 KIAVVPGVIP-PLVEAISELNDEFPFVEVEITQGKTQQVFTLLQLEQVDCALIIDSDDIKNknfpFNIRKVCNGKLYIAM 172
Cdd:pfam03466   5 RIGAPPTLASyLLPPLLARFRERYPDVELELTEGNSEELLDLLLEGELDLAIRRGPPDDPG----LEARPLGEEPLVLVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029 173 NRNSKLSLYNPLNYKTLIKEPLVLYKDEYIL-NYVKYIENKTGEHSNILFQTNNTNSIIYAVKNNFANTIALDFTFDNKY 251
Cdd:pfam03466  81 PPDHPLARGEPVSLEDLADEPLILLPPGSGLrDLLDRALRAAGLRPRVVLEVNSLEALLQLVAAGLGIALLPRSAVAREL 160

                         170       180
                  ....*....|....*....|....*...
gi 1268092029 252 RDfyNEIKQVPIEDDEnwKTISLWFCYP 279
Cdd:pfam03466 161 AD--GRLVALPLPEPP--LPRELYLVWR 184
PBP2_LTTR_substrate cd05466
The substrate binding domain of LysR-type transcriptional regulators (LTTRs), a member of the ...
 92-243 2.09e-09

The substrate binding domain of LysR-type transcriptional regulators (LTTRs), a member of the type 2 periplasmic binding fold protein superfamily; This model and hierarchy represent the the substrate-binding domain of the LysR-type transcriptional regulators that form the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, oxidative stress responses, nodule formation of nitrogen-fixing bacteria, synthesis of virulence factors, toxin production, attachment and secretion, to name a few. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate-binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 176102 [Multi-domain]  Cd Length: 197  Bit Score: 56.07  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029  92 RMKIAVVPGVIPPLV-EAISELNDEFPFVEVEITQGKTQQVFTLLQLEQVDCALIIDSDDIKNknfpFNIRKVCNGKLYI 170
Cdd:cd05466     1 TLRIGASPSIAAYLLpPLLAAFRQRYPGVELSLVEGGSSELLEALLEGELDLAIVALPVDDPG----LESEPLFEEPLVL 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1268092029 171 AMNRNSKLSLYNPLNYKTLIKEPLVLYKDEYILN-YVKYIENKTGEHSNILFQTNNTNSIIYAVKNNFAntIAL 243
Cdd:cd05466    77 VVPPDHPLAKRKSVTLADLADEPLILFERGSGLRrLLDRAFAEAGFTPNIALEVDSLEAIKALVAAGLG--IAL 148
PRK11151 PRK11151
DNA-binding transcriptional regulator OxyR; Provisional
 1-145 1.24e-07

DNA-binding transcriptional regulator OxyR; Provisional


Pssm-ID: 182999 [Multi-domain]  Cd Length: 305  Bit Score: 51.95  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029   1 MNIEQLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEGLHIIKNAYDALEKIDEIFE 80
Cdd:PRK11151    1 MNIRDLEYLVALAEHRHFRRAADSCHVSQPTLSGQIRKLEDELGVMLLERTSRKVLFTQAGLLLVDQARTVLREVKVLKE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268092029  81 YTKDKRVYPKLRMKIAVVPGVIPPLV-EAISELNDEFPFVEVEITQGKTQQVftLLQLE--QVDCALI 145
Cdd:PRK11151   81 MASQQGETMSGPLHIGLIPTVGPYLLpHIIPMLHQTFPKLEMYLHEAQTHQL--LAQLDsgKLDCAIL 146
PRK11482 PRK11482
DNA-binding transcriptional regulator;
22-148 1.79e-07

DNA-binding transcriptional regulator;


Pssm-ID: 183159 [Multi-domain]  Cd Length: 317  Bit Score: 51.65  E-value: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029  22 AKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEGLHIIKNAYDALEKIDEIFEYTKDkrvYPKLR-MKIAVVPG 100
Cdd:PRK11482   50 AKILNLTPSAISQSIQKLRVIFPDPLFIRKGQGVTPTAYATHLHEYISQGLESILGALDITGS---YDKQRtITIATTPS 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1268092029 101 ----VIPPLVEAISELNDEFPFVEVEITQGKTQqvftlLQLEQVDcaLIIDS 148
Cdd:PRK11482  127 vgalVMPVIYQAIKTHYPQLLLRNIPISDAENQ-----LSQFQTD--LIIDT 171
PRK10094 PRK10094
HTH-type transcriptional activator AllS;
4-76 5.07e-07

HTH-type transcriptional activator AllS;


Pssm-ID: 182237 [Multi-domain]  Cd Length: 308  Bit Score: 50.19  E-value: 5.07e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1268092029   4 EQLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEGLHIIKNAYDALEKID 76
Cdd:PRK10094    5 ETLRTFIAVAETGSFSKAAERLCKTTATISYRIKLLEENTGVALFFRTTRSVTLTAAGEHLLSQARDWLSWLE 77
PRK13348 PRK13348
HTH-type transcriptional regulator ArgP;
5-52 5.48e-07

HTH-type transcriptional regulator ArgP;


Pssm-ID: 237357 [Multi-domain]  Cd Length: 294  Bit Score: 49.97  E-value: 5.48e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1268092029   5 QLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTK 52
Cdd:PRK13348    6 QLEALAAVVETGSFERAARRLHVTPSAVSQRIKALEESLGQPLLVRGR 53
PRK09906 PRK09906
DNA-binding transcriptional regulator HcaR; Provisional
 1-241 1.14e-06

DNA-binding transcriptional regulator HcaR; Provisional


Pssm-ID: 182137 [Multi-domain]  Cd Length: 296  Bit Score: 49.00  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029   1 MNIEQLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEGLHIIKNAYDALEKIDEIFE 80
Cdd:PRK09906    1 MELRHLRYFVAVAEELNFTKAAEKLHTAQPSLSQQIKDLENCVGVPLLVRDKRKVALTAAGEVFLQDARAILEQAEKAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029  81 YTKdKRVYPKLRMKIAVVPGV-IPPLVEAISELNDEFPFVEVE-ITQGKTQQVFTLLQLEqVDCALI---IDSDDIKNKn 155
Cdd:PRK09906   81 RAR-KIVQEDRQLTIGFVPSAeVNLLPKVLPMFRLRHPDTLIElVSLITTQQEEKLRRGE-LDVGFMrhpVYSDEIDYL- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029 156 fpfnirKVCNGKLYIAMNRNSKLSLYNPLNYKTLIKEPLVLYKDEYILNYVKYIENKTGEHS---NILFQTNNTNSIIYA 232
Cdd:PRK09906  158 ------ELLDEPLVVVLPVDHPLAHEKEITAAQLDGVNFISTDPAYSGSLAPIIKAWFAQHNsqpNIVQVATNILVTMNL 231


                  ....*....
gi 1268092029 233 VKNNFANTI 241
Cdd:PRK09906  232 VGMGLGCTI 240
PRK10216 PRK10216
HTH-type transcriptional regulator YidZ;
12-58 1.48e-06

HTH-type transcriptional regulator YidZ;


Pssm-ID: 182312 [Multi-domain]  Cd Length: 319  Bit Score: 49.05  E-value: 1.48e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1268092029  12 LSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPT 58
Cdd:PRK10216   19 LMQERSVTKAAKRMNVTPSAVSKSLAKLRAWFDDPLFVNTPLGLSPT 65
rbcR CHL00180
LysR transcriptional regulator; Provisional
 3-61 8.87e-06

LysR transcriptional regulator; Provisional


Pssm-ID: 177082 [Multi-domain]  Cd Length: 305  Bit Score: 46.55  E-value: 8.87e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1268092029   3 IEQLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEG 61
Cdd:CHL00180    7 LDQLRILKAIATEGSFKKAAESLYISQPAVSLQIKNLEKQLNIPLFDRSKNKASLTEAG 65
PRK12680 PRK12680
LysR family transcriptional regulator;
1-145 1.55e-05

LysR family transcriptional regulator;


Pssm-ID: 183677 [Multi-domain]  Cd Length: 327  Bit Score: 45.77  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029   1 MNIEQLKLIVTLSE-ERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLF---NRTKDGTYPTveGLHIIKNAYDALEKID 76
Cdd:PRK12680    1 MTLTQLRYLVAIADaELNITLAAARVHATQPGLSKQLKQLEDELGFLLFvrkGRSLESVTPA--GVEVIERARAVLSEAN 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1268092029  77 EIFEYTKDKRVYPKLRMKIAVVPG----VIPPlveAISELNDEFPFVEVEITQGKTQQVFTLLQLEQVDCALI 145
Cdd:PRK12680   79 NIRTYAANQRRESQGQLTLTTTHTqarfVLPP---AVAQIKQAYPQVSVHLQQAAESAALDLLGQGDADIAIV 148
PRK10086 PRK10086
DNA-binding transcriptional regulator DsdC;
19-147 1.84e-05

DNA-binding transcriptional regulator DsdC;


Pssm-ID: 182231 [Multi-domain]  Cd Length: 311  Bit Score: 45.38  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029  19 SRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEG---LHIIKNAYDALEKidEIFEytkdkrvypklrMKI 95
Cdd:PRK10086   32 ALAADELSLTPSAVSHRINQLEEELGIKLFVRSHRKVELTEEGkrvFWALKSSLDTLNQ--EILD------------IKN 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1268092029  96 AVVPGVI----PP------LVEAISELNDEFPFVEVEITQGKTQQVFtllQLEQVDCALIID 147
Cdd:PRK10086   98 QELSGTLtvysRPsiaqcwLVPRLADFTRRYPSISLTILTGNENVNF---QRAGIDLAIYFD 156
PRK11074 PRK11074
putative DNA-binding transcriptional regulator; Provisional
 22-132 2.01e-05

putative DNA-binding transcriptional regulator; Provisional


Pssm-ID: 182948 [Multi-domain]  Cd Length: 300  Bit Score: 45.32  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029  22 AKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEGLHIIKNAYDALEKIDEIFEYTkdKRVYPKLR--MKIA--- 96
Cdd:PRK11074   23 AQELHRVPSAVSYTVRQLEEWLAVPLFERRHRDVELTPAGEWFVKEARSVIKKMQETRRQC--QQVANGWRgqLSIAvdn 100

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1268092029  97 -VVPGVIPPLVEaisELNDEFPFVEVEItqgkTQQVF 132
Cdd:PRK11074  101 iVRPDRTRQLIV---DFYRHFDDVELII----RQEVF 130
PBP2_MleR cd08437
The substrate binding domain of LysR-type transcriptional regulator MleR which required for ...
 92-267 3.94e-05

The substrate binding domain of LysR-type transcriptional regulator MleR which required for malolactic fermentation, contains type 2 periplasmic binidning fold; MleR, a transcription activator of malolactic fermentation system, is found in gram-positive bacteria and belongs to the lysR family of bacterial transcriptional regulators. The mleR gene is required for the expression and induction of malolactic fermentation. This substrate binding domain has significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 176128  Cd Length: 198  Bit Score: 43.86  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029  92 RMKIAVVPGVI----PPLveaISELNDEFPFVEVEITQGKTQQVFTLLQLEQVDCALIIDSDDIKNKNfpFNIRKVCNGK 167
Cdd:cd08437     1 KLRFGLPPIIGnyyfPKL---AKDLIKTGLMIQIDTYEGGSAELLEQLLQGDLDIALLGSLTPLENSA--LHSKIIKTQH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029 168 LYIAMNRNSKLSLYNPLNYKTLIKEPLVLYKDEYILNYV-KYIENKTGEHSNILFQTNNTNSIIYAVKNNFANTIALDFT 246
Cdd:cd08437    76 FMIIVSKDHPLAKAKKVNFADLKKENFILLNEHFVHPKAfDSLCQQANFQPNIVYRTNDIHILKSMVRENVGIGFLTDIA 155

                         170       180
                  ....*....|....*....|.
gi 1268092029 247 FDNkyrdfYNEIKQVPIEDDE 267
Cdd:cd08437   156 VKP-----DDHLVAIPLLDNE 171
PRK03635 PRK03635
ArgP/LysG family DNA-binding transcriptional regulator;
7-52 5.88e-05

ArgP/LysG family DNA-binding transcriptional regulator;


Pssm-ID: 235144 [Multi-domain]  Cd Length: 294  Bit Score: 43.99  E-value: 5.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1268092029   7 KLIVTLS---EERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTK 52
Cdd:PRK03635    5 KQLEALAavvREGSFERAAQKLHITQSAVSQRIKALEERVGQVLLVRTQ 53
PBP2_CysL_like cd08420
C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which ...
 101-196 9.09e-05

C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which activates the transcription of the cysJI operon encoding sulfite reductase, contains the type 2 periplasmic binding fold; CysL, also known as YwfK, is a regular of sulfur metabolism in Bacillus subtilis. Sulfur is required for the synthesis of proteins and essential cofactors in all living organism. Sulfur can be assimilated either from inorganic sources (sulfate and thiosulfate), or from organic sources (sulfate esters, sulfamates, and sulfonates). CysL activates the transcription of the cysJI operon encoding sulfite reductase, which reduces sulfite to sulfide. Both cysL mutant and cysJI mutant are unable to grow using sulfate or sulfite as the sulfur source. Like other LysR-type regulators, CysL also negatively regulates its own transcription. In Escherichia coli, three LysR-type activators are involved in the regulation of sulfur metabolism: CysB, Cbl and MetR. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 176112 [Multi-domain]  Cd Length: 201  Bit Score: 42.48  E-value: 9.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029 101 VIPPLveaISELNDEFPFVEVEITQGKTQQVFTLLQLEQVDCALI---IDSDDIKnknfpfnIRKVCNGKLYIAMNRNSK 177
Cdd:cd08420    14 LLPRL---LARFRKRYPEVRVSLTIGNTEEIAERVLDGEIDLGLVegpVDHPDLI-------VEPFAEDELVLVVPPDHP 83

                          90
                  ....*....|....*....
gi 1268092029 178 LSLYNPLNYKTLIKEPLVL 196
Cdd:cd08420    84 LAGRKEVTAEELAAEPWIL 102
PBP2_CidR cd08438
The C-terminal substrate binding domain of LysR-like transcriptional regulator CidR, contains ...
 102-204 1.98e-04

The C-terminal substrate binding domain of LysR-like transcriptional regulator CidR, contains the type 2 periplasmic binding fold; This CD includes the substrate binding domain of CidR which positively up-regulates the expression of cidABC operon in the presence of acetic acid produced by the metabolism of excess glucose. The CidR affects the control of murein hydrolase activity by enhancing cidABC expression in the presence of acetic acid. Thus, up-regulation of cidABC expression results in increased murein hydrolase activity. This substrate binding domain has significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 176129 [Multi-domain]  Cd Length: 197  Bit Score: 41.39  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029 102 IPPLV------EAISELNDEFPFVEVEITQGKTQQVFTLLQLEQVD---CALIIDSDDiknknfpFNIRKVCNGKLYIAM 172
Cdd:cd08438     6 LPPLGgsllfaPLLAAFRQRYPNIELELVEYGGKKVEQAVLNGELDvgiTVLPVDEEE-------FDSQPLCNEPLVAVL 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1268092029 173 NRNSKLSLYNPLNYKTLIKEPLVLYKDEYILN 204
Cdd:cd08438    79 PRGHPLAGRKTVSLADLADEPFILFNEDFALH 110
PRK03601 PRK03601
HTH-type transcriptional regulator HdfR;
1-50 8.19e-04

HTH-type transcriptional regulator HdfR;


Pssm-ID: 235137 [Multi-domain]  Cd Length: 275  Bit Score: 40.39  E-value: 8.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1268092029   1 MNIEQLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNR 50
Cdd:PRK03601    1 MDTELLKTFLEVSRTRHFGRAAESLYLTQSAVSFRIRQLENQLGVNLFTR 50
PRK11233 PRK11233
nitrogen assimilation transcriptional regulator; Provisional
 1-61 8.70e-04

nitrogen assimilation transcriptional regulator; Provisional


Pssm-ID: 183045 [Multi-domain]  Cd Length: 305  Bit Score: 40.44  E-value: 8.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268092029   1 MNIEQLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEG 61
Cdd:PRK11233    1 MNFRRLKYFVKIVDIGSLTQAAEVLHIAQPALSQQVATLEGELNQQLLIRTKRGVTPTEAG 61
PRK12684 PRK12684
CysB family HTH-type transcriptional regulator;
1-144 1.49e-03

CysB family HTH-type transcriptional regulator;


Pssm-ID: 237173 [Multi-domain]  Cd Length: 313  Bit Score: 39.57  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029   1 MNIEQLKLIV-TLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRT-KDGTYPTVEGLHIIKNAYDALEKIDEI 78
Cdd:PRK12684    1 MNLHQLRFVReAVRQNFNLTEAAKALYTSQPGVSKAIIELEDELGVEIFTRHgKRLRGLTEPGRIILASVERILQEVENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1268092029  79 feytkdKRVYPKL------RMKIAVVPG----VIPPlveAISELNDEFPFVEVEITQGKTQQVFTLLQLEQVDCAL 144
Cdd:PRK12684   81 ------KRVGKEFaaqdqgNLTIATTHTqaryALPA---AIKEFKKRYPKVRLSILQGSPTQIAEMVLHGQADLAI 147
PRK09801 PRK09801
LysR family transcriptional regulator;
4-121 1.53e-03

LysR family transcriptional regulator;


Pssm-ID: 182085 [Multi-domain]  Cd Length: 310  Bit Score: 39.63  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029   4 EQLKLIVTLSEERKLSRVAKKLNLTPSAVCQGIKKLEKELNTPLFNRTKDGTYPTVEGLHIIKNAYDALEKIDEIFEYTK 83
Cdd:PRK09801    9 KDLQVLVEIVHSGSFSAAAATLGQTPAFVTKRIQILENTLATTLLNRSARGVALTESGQRCYEHALEILTQYQRLVDDVT 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1268092029  84 DKRVYPKLRMKIAVVPGV----IPPlveAISELNDEFPFVEV 121
Cdd:PRK09801   89 QIKTRPEGMIRIGCSFGFgrshIAP---AITELMRNYPELQV 127
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
6-42 1.58e-03

Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 37.88  E-value: 1.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1268092029   6 LKLIVTLSEER---KLSRVAKKLNLTPSAVCQGIKKLEKE 42
Cdd:COG1321    12 LKAIYELSEEGgpvRTSDIAERLGVSPPSVTEMLKKLEEK 51
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
1-86 5.43e-03

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 35.65  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268092029    1 MNIEQLKLIVTLSEER--KLSRVAKKLNLTPSAVCQGIKKLEKElntPLFNRTKDGT-------YPTVEGLHIIKNAYDA 71
Cdd:smart00347   8 LTPTQFLVLRILYEEGplSVSELAKRLGVSPSTVTRVLDRLEKK---GLVRREPSPEdrrsvlvSLTEEGRELIEQLLEA 84

                           90
                   ....*....|....*..
gi 1268092029   72 LEK-IDEIF-EYTKDKR 86
Cdd:smart00347  85 RSEtLAELLaGLTAEEQ 101
 
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