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Conserved domains on  [gi|1273236958|gb|PIA68572|]
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amino acid ABC transporter substrate-binding protein [Pseudomonas toyotomiensis]

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

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List of domain hits

Name Accession Description Interval E-value
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
29-244 1.63e-14

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: 70.39  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958  29 TDESWVPY-WIVDEQRVSGILHEFMLALDERLPEQLQaSHPLPPLRTQKLFREGQVQIECCVSkSWRSDGDQGAgsLWTV 107
Cdd:COG0834     5 VDPDYPPFsFRDEDGKLVGFDVDLARAIAKRLGLKVE-FVPVPWDRLIPALQSGKVDLIIAGM-TITPEREKQV--DFSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958 108 PVLETEEMLIFAPGRhFPYQHLQDLRGRSIATVRGYGYAgsEYFQRNDG-------ADARALIYLVAQGRSEAGILDRLE 180
Cdd:COG0834    81 PYYTSGQVLLVRKDN-SGIKSLADLKGKTVGVQAGTTYE--EYLKKLGPnaeivefDSYAEALQALASGRVDAVVTDEPV 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1273236958 181 WRYL--QHEDAQLQAPrwqveeGPTINRSQLRLRLHRQLAGRLEVFNAAIRSLQVDGTLARIIARY 244
Cdd:COG0834   158 AAYLlaKNPGDDLKIV------GEPLSGEPYGIAVRKGDPELLEAVNKALAALKADGTLDKILEKW 217
 
Name Accession Description Interval E-value
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
29-244 1.63e-14

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: 70.39  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958  29 TDESWVPY-WIVDEQRVSGILHEFMLALDERLPEQLQaSHPLPPLRTQKLFREGQVQIECCVSkSWRSDGDQGAgsLWTV 107
Cdd:COG0834     5 VDPDYPPFsFRDEDGKLVGFDVDLARAIAKRLGLKVE-FVPVPWDRLIPALQSGKVDLIIAGM-TITPEREKQV--DFSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958 108 PVLETEEMLIFAPGRhFPYQHLQDLRGRSIATVRGYGYAgsEYFQRNDG-------ADARALIYLVAQGRSEAGILDRLE 180
Cdd:COG0834    81 PYYTSGQVLLVRKDN-SGIKSLADLKGKTVGVQAGTTYE--EYLKKLGPnaeivefDSYAEALQALASGRVDAVVTDEPV 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1273236958 181 WRYL--QHEDAQLQAPrwqveeGPTINRSQLRLRLHRQLAGRLEVFNAAIRSLQVDGTLARIIARY 244
Cdd:COG0834   158 AAYLlaKNPGDDLKIV------GEPLSGEPYGIAVRKGDPELLEAVNKALAALKADGTLDKILEKW 217
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
22-244 1.10e-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: 53.69  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958  22 KTLTYAVtDESWVPYWIVDEQ-RVSGILHEFMLALDERLPEQLQASHPLPPLRTQKLFREGQVQIECCVSKSwrSDGDQG 100
Cdd:cd01007     2 PVIRVGV-DPDWPPFEFIDEGgEPQGIAADYLKLIAKKLGLKFEYVPGDSWSELLEALKAGEIDLLSSVSKT--PEREKY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958 101 AgsLWTVPVLETEeMLIFAPGRHFPYQHLQDLRGRSIATVRGYGYAgsEYFQRNDG-------ADARALIYLVAQGRSEA 173
Cdd:cd01007    79 L--LFTKPYLSSP-LVIVTRKDAPFINSLSDLAGKRVAVVKGYALE--ELLRERYPninlvevDSTEEALEAVASGEADA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1273236958 174 GILDRLEWRYL--QHEDAQLQAprwqveEGPTINRSQLRLRLHRQLAGRLEVFNAAIRSLQvDGTLARIIARY 244
Cdd:cd01007   154 YIGNLAVASYLiqKYGLSNLKI------AGLTDYPQDLSFAVRKDWPELLSILNKALASIS-PEERQAIRNKW 219
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
106-244 4.11e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 52.29  E-value: 4.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958 106 TVPVLETEEMLIFAPGRHFP-YQHLQDLRGRSIATVRGYGYAGSEYFQRNDGADAR------ALIYLVAQGRSEAGILDR 178
Cdd:pfam00497  79 SDPYYYSGQVILVRKKDSSKsIKSLADLKGKTVGVQKGSTAEELLKNLKLPGAEIVeydddaEALQALANGRVDAVVADS 158
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1273236958 179 LEWRYLQHEDAQLQAprwqVEEGPTINRSQLRLRLHRQLAGRLEVFNAAIRSLQVDGTLARIIARY 244
Cdd:pfam00497 159 PVAAYLIKKNPGLNL----VVVGEPLSPEPYGIAVRKGDPELLAAVNKALAELKADGTLAKIYEKW 220
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
125-244 1.29e-07

Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 50.79  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958  125 PYQHLQDLRGRSIATVRGYGYAgsEYFQRN----------DGADARALiylVAQGRSEAGILDRLEWRYLQHedaQLQAP 194
Cdd:smart00062  97 PIKSLEDLKGKKVAVVAGTTAE--ELLKKLypeakivsydSNAEALAA---LKAGRADAAVADAPLLAALVK---QHGLP 168
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1273236958  195 RWQVEEGPTINRSQLRLRLHRQLAGRLEVFNAAIRSLQVDGTLARIIARY 244
Cdd:smart00062 169 ELKIVPDPLDTPEGYAIAVRKGDPELLDKINKALKELKADGTLKKISEKW 218
 
Name Accession Description Interval E-value
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
29-244 1.63e-14

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: 70.39  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958  29 TDESWVPY-WIVDEQRVSGILHEFMLALDERLPEQLQaSHPLPPLRTQKLFREGQVQIECCVSkSWRSDGDQGAgsLWTV 107
Cdd:COG0834     5 VDPDYPPFsFRDEDGKLVGFDVDLARAIAKRLGLKVE-FVPVPWDRLIPALQSGKVDLIIAGM-TITPEREKQV--DFSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958 108 PVLETEEMLIFAPGRhFPYQHLQDLRGRSIATVRGYGYAgsEYFQRNDG-------ADARALIYLVAQGRSEAGILDRLE 180
Cdd:COG0834    81 PYYTSGQVLLVRKDN-SGIKSLADLKGKTVGVQAGTTYE--EYLKKLGPnaeivefDSYAEALQALASGRVDAVVTDEPV 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1273236958 181 WRYL--QHEDAQLQAPrwqveeGPTINRSQLRLRLHRQLAGRLEVFNAAIRSLQVDGTLARIIARY 244
Cdd:COG0834   158 AAYLlaKNPGDDLKIV------GEPLSGEPYGIAVRKGDPELLEAVNKALAALKADGTLDKILEKW 217
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
22-244 1.10e-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: 53.69  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958  22 KTLTYAVtDESWVPYWIVDEQ-RVSGILHEFMLALDERLPEQLQASHPLPPLRTQKLFREGQVQIECCVSKSwrSDGDQG 100
Cdd:cd01007     2 PVIRVGV-DPDWPPFEFIDEGgEPQGIAADYLKLIAKKLGLKFEYVPGDSWSELLEALKAGEIDLLSSVSKT--PEREKY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958 101 AgsLWTVPVLETEeMLIFAPGRHFPYQHLQDLRGRSIATVRGYGYAgsEYFQRNDG-------ADARALIYLVAQGRSEA 173
Cdd:cd01007    79 L--LFTKPYLSSP-LVIVTRKDAPFINSLSDLAGKRVAVVKGYALE--ELLRERYPninlvevDSTEEALEAVASGEADA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1273236958 174 GILDRLEWRYL--QHEDAQLQAprwqveEGPTINRSQLRLRLHRQLAGRLEVFNAAIRSLQvDGTLARIIARY 244
Cdd:cd01007   154 YIGNLAVASYLiqKYGLSNLKI------AGLTDYPQDLSFAVRKDWPELLSILNKALASIS-PEERQAIRNKW 219
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
106-244 4.11e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 52.29  E-value: 4.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958 106 TVPVLETEEMLIFAPGRHFP-YQHLQDLRGRSIATVRGYGYAGSEYFQRNDGADAR------ALIYLVAQGRSEAGILDR 178
Cdd:pfam00497  79 SDPYYYSGQVILVRKKDSSKsIKSLADLKGKTVGVQKGSTAEELLKNLKLPGAEIVeydddaEALQALANGRVDAVVADS 158
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1273236958 179 LEWRYLQHEDAQLQAprwqVEEGPTINRSQLRLRLHRQLAGRLEVFNAAIRSLQVDGTLARIIARY 244
Cdd:pfam00497 159 PVAAYLIKKNPGLNL----VVVGEPLSPEPYGIAVRKGDPELLAAVNKALAELKADGTLAKIYEKW 220
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
125-244 1.29e-07

Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 50.79  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958  125 PYQHLQDLRGRSIATVRGYGYAgsEYFQRN----------DGADARALiylVAQGRSEAGILDRLEWRYLQHedaQLQAP 194
Cdd:smart00062  97 PIKSLEDLKGKKVAVVAGTTAE--ELLKKLypeakivsydSNAEALAA---LKAGRADAAVADAPLLAALVK---QHGLP 168
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1273236958  195 RWQVEEGPTINRSQLRLRLHRQLAGRLEVFNAAIRSLQVDGTLARIIARY 244
Cdd:smart00062 169 ELKIVPDPLDTPEGYAIAVRKGDPELLDKINKALKELKADGTLKKISEKW 218
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
21-244 4.91e-05

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: 42.96  E-value: 4.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958  21 AKTLTYAVtDESWVPYWIVDEQ-RVSGILHEFMLALDERLpeQLQAS-HPLPPLRTQKLFREGQVQIeccVSKSWRSDgD 98
Cdd:cd13704     1 ARTVIVGG-DKNYPPYEFLDENgNPTGFNVDLLRAIAEEM--GLKVEiRLGPWSEVLQALENGEIDV---LIGMAYSE-E 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958  99 QGAGSLWTVPVLETEEMLIFAPGRHFPyQHLQDLRGRSIATVRGyGYAGsEYFQRNDGA-------DARALIYLVAQGRS 171
Cdd:cd13704    74 RAKLFDFSDPYLEVSVSIFVRKGSSII-NSLEDLKGKKVAVQRG-DIMH-EYLKERGLGinlvlvdSPEEALRLLASGKV 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1273236958 172 EAGILDRLEWRYL--QHEDAQLQA---PRWQVEEGPTINRSQLRLrlhrqlagrLEVFNAAIRSLQVDGTLARIIARY 244
Cdd:cd13704   151 DAAVVDRLVGLYLikELGLTNVKIvgpPLLPLKYCFAVRKGNPEL---------LAKLNEGLAILKASGEYDEIYEKW 219
PBP2_Ngo0372_TcyA cd13711
Substrate binding domain of ABC transporters involved in cystine import; the type 2 ...
163-244 6.58e-04

Substrate binding domain of ABC transporters involved in cystine import; the type 2 periplasmic binding protein fold; This subgroup includes cystine-binding domain of periplasmic receptor-dependent ATP-binding cassette transporters from Neisseria gonorrhoeae and Bacillus subtilis and their related proteins. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins 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. 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: 270429 [Multi-domain]  Cd Length: 222  Bit Score: 39.97  E-value: 6.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273236958 163 IYLVAQGRSEAGILDRLEWRYL--QHEDA--QLQAPRWQVEE-GPTINRSQLRLRlhrqlagrlEVFNAAIRSLQVDGTL 237
Cdd:cd13711   140 VELITQGRADATINDSLAFLDYkkQHPDApvKIAAETDDASEsAFLVRKGNDELV---------AAINKALKELKADGTL 210

                  ....*..
gi 1273236958 238 ARIIARY 244
Cdd:cd13711   211 KKISEKY 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.
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