NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490724341|ref|WP_004586889|]
View 

MULTISPECIES: ABC transporter substrate-binding protein [Pseudoalteromonas]

Protein Classification

substrate-binding periplasmic protein( domain architecture ID 11435556)

substrate-binding periplasmic protein similar to ABC transporter substrate-binding proteins, which function as the initial receptor in the ABC transport of a variety of substrates including amino acids and peptides, and to the periplasmic sensor domain of the histidine kinase receptors (HisK), which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes

PubMed:  15313245

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
26-251 4.02e-19

ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms];


:

Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 83.11  E-value: 4.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341  26 VAENSPP--YIGERLIDNGWVTALTKAALANQNINNDIEFTSWNRALELTKINKKDAILGAF-YTKSRTDLFYYSRPLAN 102
Cdd:COG0834    5 VDPDYPPfsFRDEDGKLVGFDVDLARAIAKRLGLKVEFVPVPWDRLIPALQSGKVDLIIAGMtITPEREKQVDFSDPYYT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341 103 VYVGLFKLKDR-QINydgSMDSLQPYSICKGVGYAVSEVFSESNGLA-VTSTRGLINSLYMLQKGRIDLVAGTKEVGEYW 180
Cdd:COG0834   85 SGQVLLVRKDNsGIK---SLADLKGKTVGVQAGTTYEEYLKKLGPNAeIVEFDSYAEALQALASGRVDAVVTDEPVAAYL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490724341 181 LKnteklnEPGAPQVEYISPDLEHHQLHVMFPKSDPDAkqkRDALEQGFSTILYNGTAKELLVKHGFSQST 251
Cdd:COG0834  162 LA------KNPGDDLKIVGEPLSGEPYGIAVRKGDPEL---LEAVNKALAALKADGTLDKILEKWFGEDVP 223
 
Name Accession Description Interval E-value
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
26-251 4.02e-19

ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 83.11  E-value: 4.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341  26 VAENSPP--YIGERLIDNGWVTALTKAALANQNINNDIEFTSWNRALELTKINKKDAILGAF-YTKSRTDLFYYSRPLAN 102
Cdd:COG0834    5 VDPDYPPfsFRDEDGKLVGFDVDLARAIAKRLGLKVEFVPVPWDRLIPALQSGKVDLIIAGMtITPEREKQVDFSDPYYT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341 103 VYVGLFKLKDR-QINydgSMDSLQPYSICKGVGYAVSEVFSESNGLA-VTSTRGLINSLYMLQKGRIDLVAGTKEVGEYW 180
Cdd:COG0834   85 SGQVLLVRKDNsGIK---SLADLKGKTVGVQAGTTYEEYLKKLGPNAeIVEFDSYAEALQALASGRVDAVVTDEPVAAYL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490724341 181 LKnteklnEPGAPQVEYISPDLEHHQLHVMFPKSDPDAkqkRDALEQGFSTILYNGTAKELLVKHGFSQST 251
Cdd:COG0834  162 LA------KNPGDDLKIVGEPLSGEPYGIAVRKGDPEL---LEAVNKALAALKADGTLDKILEKWFGEDVP 223
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
26-188 2.66e-11

The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding fold protein; This subfamily includes the periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270422 [Multi-domain]  Cd Length: 220  Bit Score: 61.45  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341  26 VAENSPPYigERLIDNGWVTA----LTKAALANQNINNDIEFTSWNRALELTKINKKDAILGAFYTKSRTDLFYYSRPLA 101
Cdd:cd13704    8 GDKNYPPY--EFLDENGNPTGfnvdLLRAIAEEMGLKVEIRLGPWSEVLQALENGEIDVLIGMAYSEERAKLFDFSDPYL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341 102 NVYVGLFKLKDRQINydGSMDSLQPYSIC--KGvgyAVSEVFSESNGLA--VTSTRGLINSLYMLQKGRIDLVAGTKEVG 177
Cdd:cd13704   86 EVSVSIFVRKGSSII--NSLEDLKGKKVAvqRG---DIMHEYLKERGLGinLVLVDSPEEALRLLASGKVDAAVVDRLVG 160
                        170
                 ....*....|.
gi 490724341 178 EYWLKNTEKLN 188
Cdd:cd13704  161 LYLIKELGLTN 171
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
60-246 1.64e-08

Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 53.45  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341   60 DIEFTSWNRALELTKINKKDAILGA-FYTKSRTDLFYYSRPLANVYVGLFKLKDRQINYDGSMDSLQPYSICKGVGYAVS 138
Cdd:pfam00497  41 EFVPVSWDGLIPALQSGKVDLIIAGmTITPERAKQVDFSDPYYYSGQVILVRKKDSSKSIKSLADLKGKTVGVQKGSTAE 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341  139 EV--FSESNGLAVTSTRGLINSLYMLQKGRIDLVAGTKEVGEYWLKNTEKLNEPGAPQVEYISPdlehhqLHVMFPKSDP 216
Cdd:pfam00497 121 ELlkNLKLPGAEIVEYDDDAEALQALANGRVDAVVADSPVAAYLIKKNPGLNLVVVGEPLSPEP------YGIAVRKGDP 194
                         170       180       190
                  ....*....|....*....|....*....|
gi 490724341  217 DAkqkRDALEQGFSTILYNGTAKELLVKHG 246
Cdd:pfam00497 195 EL---LAAVNKALAELKADGTLAKIYEKWF 221
 
Name Accession Description Interval E-value
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
26-251 4.02e-19

ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 83.11  E-value: 4.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341  26 VAENSPP--YIGERLIDNGWVTALTKAALANQNINNDIEFTSWNRALELTKINKKDAILGAF-YTKSRTDLFYYSRPLAN 102
Cdd:COG0834    5 VDPDYPPfsFRDEDGKLVGFDVDLARAIAKRLGLKVEFVPVPWDRLIPALQSGKVDLIIAGMtITPEREKQVDFSDPYYT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341 103 VYVGLFKLKDR-QINydgSMDSLQPYSICKGVGYAVSEVFSESNGLA-VTSTRGLINSLYMLQKGRIDLVAGTKEVGEYW 180
Cdd:COG0834   85 SGQVLLVRKDNsGIK---SLADLKGKTVGVQAGTTYEEYLKKLGPNAeIVEFDSYAEALQALASGRVDAVVTDEPVAAYL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490724341 181 LKnteklnEPGAPQVEYISPDLEHHQLHVMFPKSDPDAkqkRDALEQGFSTILYNGTAKELLVKHGFSQST 251
Cdd:COG0834  162 LA------KNPGDDLKIVGEPLSGEPYGIAVRKGDPEL---LEAVNKALAALKADGTLDKILEKWFGEDVP 223
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
26-188 2.66e-11

The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding fold protein; This subfamily includes the periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270422 [Multi-domain]  Cd Length: 220  Bit Score: 61.45  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341  26 VAENSPPYigERLIDNGWVTA----LTKAALANQNINNDIEFTSWNRALELTKINKKDAILGAFYTKSRTDLFYYSRPLA 101
Cdd:cd13704    8 GDKNYPPY--EFLDENGNPTGfnvdLLRAIAEEMGLKVEIRLGPWSEVLQALENGEIDVLIGMAYSEERAKLFDFSDPYL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341 102 NVYVGLFKLKDRQINydGSMDSLQPYSIC--KGvgyAVSEVFSESNGLA--VTSTRGLINSLYMLQKGRIDLVAGTKEVG 177
Cdd:cd13704   86 EVSVSIFVRKGSSII--NSLEDLKGKKVAvqRG---DIMHEYLKERGLGinLVLVDSPEEALRLLASGKVDAAVVDRLVG 160
                        170
                 ....*....|.
gi 490724341 178 EYWLKNTEKLN 188
Cdd:cd13704  161 LYLIKELGLTN 171
PBP2_HisK_like_1 cd13706
Putative sensor domain similar to HisK; the type 2 periplasmic binding fold protein; This ...
60-232 1.69e-10

Putative sensor domain similar to HisK; the type 2 periplasmic binding fold protein; This group includes periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270424 [Multi-domain]  Cd Length: 219  Bit Score: 59.11  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341  60 DIEF--TSWNRALELTKINKKDAILGAFYTKSRTDLFYYSRPLANVYVGLFKLKDrqINYDGSMDSLQPYSIckGV---G 134
Cdd:cd13706   42 PVEFvlLDWNESLEAVRQGEADVHDGLFKSPEREKYLDFSQPIATIDTYLYFHKD--LSGITNLSDLKGFRV--GVvkgD 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341 135 YAVSEVFSESNGLAVT--STRGLInsLYMLQKGRIDLVAGTKEVGEYWLKNTEKLNEpgapqvEYISPDLEHHQLHVMFP 212
Cdd:cd13706  118 AEEEFLRAHGPILSLVyyDNYEAM--IEAAKAGEIDVFVADEPVANYYLYKYGLPDE------FRPAFRLYSGQLHPAVA 189
                        170       180
                 ....*....|....*....|
gi 490724341 213 KSDPDakqKRDALEQGFSTI 232
Cdd:cd13706  190 KGNSA---LLDLINRGFALI 206
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
60-246 1.64e-08

Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 53.45  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341   60 DIEFTSWNRALELTKINKKDAILGA-FYTKSRTDLFYYSRPLANVYVGLFKLKDRQINYDGSMDSLQPYSICKGVGYAVS 138
Cdd:pfam00497  41 EFVPVSWDGLIPALQSGKVDLIIAGmTITPERAKQVDFSDPYYYSGQVILVRKKDSSKSIKSLADLKGKTVGVQKGSTAE 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341  139 EV--FSESNGLAVTSTRGLINSLYMLQKGRIDLVAGTKEVGEYWLKNTEKLNEPGAPQVEYISPdlehhqLHVMFPKSDP 216
Cdd:pfam00497 121 ELlkNLKLPGAEIVEYDDDAEALQALANGRVDAVVADSPVAAYLIKKNPGLNLVVVGEPLSPEP------YGIAVRKGDP 194
                         170       180       190
                  ....*....|....*....|....*....|
gi 490724341  217 DAkqkRDALEQGFSTILYNGTAKELLVKHG 246
Cdd:pfam00497 195 EL---LAAVNKALAELKADGTLAKIYEKWF 221
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
61-232 5.38e-08

The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine kinase receptors, and related proteins; This family comprises the periplasmic sensor domain of the two-component sensor-kinase systems, such as the sensor protein BvgS of Bordetella pertussis and histidine kinase receptors (HisK), and uncharacterized related proteins. Typically, the two-component system consists of a membrane spanning sensor-kinase and a cytoplasmic response regulator. It serves as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. The N-terminal sensing domain of the sensor kinase detects extracellular signals, such as small molecule ligands and ions, which then modulate the catalytic activity of the cytoplasmic kinase domain through a phosphorylation cascade. The periplasmic sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270228 [Multi-domain]  Cd Length: 220  Bit Score: 52.15  E-value: 5.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341  61 IEFTSWNRALELTKINKKDAILGAFYTKSRTDLFYYSRPLANVYVGLFKLKDRQinYDGSMDSLQPYSICKGVGYAVSEV 140
Cdd:cd01007   46 VPGDSWSELLEALKAGEIDLLSSVSKTPEREKYLLFTKPYLSSPLVIVTRKDAP--FINSLSDLAGKRVAVVKGYALEEL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341 141 FSES----NGLAVTSTRgliNSLYMLQKGRIDLVAGTKEVGEYWLKnteklnEPGAPQVEYISPDLEHHQLHVMFPKSDP 216
Cdd:cd01007  124 LRERypniNLVEVDSTE---EALEAVASGEADAYIGNLAVASYLIQ------KYGLSNLKIAGLTDYPQDLSFAVRKDWP 194
                        170
                 ....*....|....*.
gi 490724341 217 DAkqkRDALEQGFSTI 232
Cdd:cd01007  195 EL---LSILNKALASI 207
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
60-245 9.55e-05

Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. 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 family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 270248 [Multi-domain]  Cd Length: 217  Bit Score: 42.62  E-value: 9.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341  60 DIEF--TSWNRALELTKINKKDAILGAFY-TKSRTDLFYYSRPLANVYVGLFKLKDRQINYDgsMDSLQPYSICKGVGYA 136
Cdd:cd13530   40 KVEFvdTDFDGLIPALQSGKIDVAISGMTiTPERAKVVDFSDPYYYTGQVLVVKKDSKITKT--VADLKGKKVGVQAGTT 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490724341 137 VSEVFSESNGLA-VTSTRGLINSLYMLQKGRIDLVAGTKEVGEYWLKNteklnepGAPQVEYISPDLEHHQLHVMFPKSD 215
Cdd:cd13530  118 GEDYAKKNLPNAeVVTYDNYPEALQALKAGRIDAVITDAPVAKYYVKK-------NGPDLKVVGEPLTPEPYGIAVRKGN 190
                        170       180       190
                 ....*....|....*....|....*....|
gi 490724341 216 PDAKqkrDALEQGFSTILYNGTAKELLVKH 245
Cdd:cd13530  191 PELL---DAINKALAELKADGTLDKLLEKW 217
 
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