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Conserved domains on  [gi|515697328|ref|WP_017129928|]
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ABC transporter substrate-binding protein [Pseudomonas agarici]

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 ...
41-237 3.79e-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: 69.24  E-value: 3.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328  41 YTNADG--SGLAWDVLREVFEPLGVKVETRSEPYLRSVGLVERGEADAWVGSYS------KEI--SGVLYprwnfdTDHI 110
Cdd:COG0834   14 FRDEDGklVGFDVDLARAIAKRLGLKVEFVPVPWDRLIPALQSGKVDLIIAGMTitpereKQVdfSDPYY------TSGQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328 111 YALGLASNPAP-SLETLGAYRLAWVRGYKYQNYLPNAHHFNEIRRRDGI---LSMLRHSRADYYIDALTEVDYVLSQAPD 186
Cdd:COG0834   88 VLLVRKDNSGIkSLADLKGKTVGVQAGTTYEEYLKKLGPNAEIVEFDSYaeaLQALASGRVDAVVTDEPVAAYLLAKNPG 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515697328 187 PSV-FRRTHLVELPLYLGFSDSErgRALLALYDRRMDELVKGARLRKLFERW 237
Cdd:COG0834  168 DDLkIVGEPLSGEPYGIAVRKGD--PELLEAVNKALAALKADGTLDKILEKW 217
 
Name Accession Description Interval E-value
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
41-237 3.79e-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: 69.24  E-value: 3.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328  41 YTNADG--SGLAWDVLREVFEPLGVKVETRSEPYLRSVGLVERGEADAWVGSYS------KEI--SGVLYprwnfdTDHI 110
Cdd:COG0834   14 FRDEDGklVGFDVDLARAIAKRLGLKVEFVPVPWDRLIPALQSGKVDLIIAGMTitpereKQVdfSDPYY------TSGQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328 111 YALGLASNPAP-SLETLGAYRLAWVRGYKYQNYLPNAHHFNEIRRRDGI---LSMLRHSRADYYIDALTEVDYVLSQAPD 186
Cdd:COG0834   88 VLLVRKDNSGIkSLADLKGKTVGVQAGTTYEEYLKKLGPNAEIVEFDSYaeaLQALASGRVDAVVTDEPVAAYLLAKNPG 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515697328 187 PSV-FRRTHLVELPLYLGFSDSErgRALLALYDRRMDELVKGARLRKLFERW 237
Cdd:COG0834  168 DDLkIVGEPLSGEPYGIAVRKGD--PELLEAVNKALAALKADGTLDKILEKW 217
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
41-237 9.75e-09

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: 54.22  E-value: 9.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328   41 YTNADG--SGLAWDVLREVFEPLGVKVETRSEPYLRSVGLVERGEADAWVGSYS-----KEIsgVLY--PRWNFDTDHIY 111
Cdd:pfam00497  14 YVDENGklVGFDVDLAKAIAKRLGVKVEFVPVSWDGLIPALQSGKVDLIIAGMTitperAKQ--VDFsdPYYYSGQVILV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328  112 ALGLASNPAPSLETLGAYRLAWVRGYKYQNYLPNAHHFN-EIRRRDGI---LSMLRHSRADYYIDALTEVDYVLSQAPDP 187
Cdd:pfam00497  92 RKKDSSKSIKSLADLKGKTVGVQKGSTAEELLKNLKLPGaEIVEYDDDaeaLQALANGRVDAVVADSPVAAYLIKKNPGL 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 515697328  188 SVFRRThLVELPLYLGFSDSERGRALLALYDRRMDELVKGARLRKLFERW 237
Cdd:pfam00497 172 NLVVVG-EPLSPEPYGIAVRKGDPELLAAVNKALAELKADGTLAKIYEKW 220
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
41-237 1.30e-06

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: 47.96  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328  41 YTNADG--SGLAWDVLREVFEPLGVKVETRSEPYLRSVGLVERGEADAWVG-SYSKEISGVLyprwNFDTDHIYALGL-- 115
Cdd:cd13704   17 FLDENGnpTGFNVDLLRAIAEEMGLKVEIRLGPWSEVLQALENGEIDVLIGmAYSEERAKLF----DFSDPYLEVSVSif 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328 116 ---ASNPAPSLETLGAYRLAWVRGYKYQNYLPNAHHFNEIRRRDGILSMLRH---SRADYYIDALTEVDYVLSQAPDPSV 189
Cdd:cd13704   93 vrkGSSIINSLEDLKGKKVAVQRGDIMHEYLKERGLGINLVLVDSPEEALRLlasGKVDAAVVDRLVGLYLIKELGLTNV 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 515697328 190 frRTHLVEL-PLYLGFSDSERGRALLALYDRRMDELVKGARLRKLFERW 237
Cdd:cd13704  173 --KIVGPPLlPLKYCFAVRKGNPELLAKLNEGLAILKASGEYDEIYEKW 219
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
41-237 6.07e-06

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 45.78  E-value: 6.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328    41 YTNADGS--GLAWDVLREVFEPLGVKVE-TRSEPYLRsVGLVERGEADAwvgsyskeISGVLYPRWNFD----------T 107
Cdd:smart00062  15 FADEDGEltGFDVDLAKAIAKELGLKVEfVEVSFDSL-LTALKSGKIDV--------VAAGMTITPERAkqvdfsdpyyR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328   108 DHIYALGLASNPAPSLETLGAYRLAWVRGYKYQNYLPNAHHFNEIRRRDGI---LSMLRHSRADYYIDALTEVDYVLSQA 184
Cdd:smart00062  86 SGQVILVRKDSPIKSLEDLKGKKVAVVAGTTAEELLKKLYPEAKIVSYDSNaeaLAALKAGRADAAVADAPLLAALVKQH 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 515697328   185 PDPSVFRRTHLVELPLYLGFSDSERGRALLALYDRRMDELVKGARLRKLFERW 237
Cdd:smart00062 166 GLPELKIVPDPLDTPEGYAIAVRKGDPELLDKINKALKELKADGTLKKISEKW 218
 
Name Accession Description Interval E-value
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
41-237 3.79e-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: 69.24  E-value: 3.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328  41 YTNADG--SGLAWDVLREVFEPLGVKVETRSEPYLRSVGLVERGEADAWVGSYS------KEI--SGVLYprwnfdTDHI 110
Cdd:COG0834   14 FRDEDGklVGFDVDLARAIAKRLGLKVEFVPVPWDRLIPALQSGKVDLIIAGMTitpereKQVdfSDPYY------TSGQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328 111 YALGLASNPAP-SLETLGAYRLAWVRGYKYQNYLPNAHHFNEIRRRDGI---LSMLRHSRADYYIDALTEVDYVLSQAPD 186
Cdd:COG0834   88 VLLVRKDNSGIkSLADLKGKTVGVQAGTTYEEYLKKLGPNAEIVEFDSYaeaLQALASGRVDAVVTDEPVAAYLLAKNPG 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515697328 187 PSV-FRRTHLVELPLYLGFSDSErgRALLALYDRRMDELVKGARLRKLFERW 237
Cdd:COG0834  168 DDLkIVGEPLSGEPYGIAVRKGD--PELLEAVNKALAALKADGTLDKILEKW 217
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
41-237 9.75e-09

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: 54.22  E-value: 9.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328   41 YTNADG--SGLAWDVLREVFEPLGVKVETRSEPYLRSVGLVERGEADAWVGSYS-----KEIsgVLY--PRWNFDTDHIY 111
Cdd:pfam00497  14 YVDENGklVGFDVDLAKAIAKRLGVKVEFVPVSWDGLIPALQSGKVDLIIAGMTitperAKQ--VDFsdPYYYSGQVILV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328  112 ALGLASNPAPSLETLGAYRLAWVRGYKYQNYLPNAHHFN-EIRRRDGI---LSMLRHSRADYYIDALTEVDYVLSQAPDP 187
Cdd:pfam00497  92 RKKDSSKSIKSLADLKGKTVGVQKGSTAEELLKNLKLPGaEIVEYDDDaeaLQALANGRVDAVVADSPVAAYLIKKNPGL 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 515697328  188 SVFRRThLVELPLYLGFSDSERGRALLALYDRRMDELVKGARLRKLFERW 237
Cdd:pfam00497 172 NLVVVG-EPLSPEPYGIAVRKGDPELLAAVNKALAELKADGTLAKIYEKW 220
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
41-237 1.30e-06

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: 47.96  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328  41 YTNADG--SGLAWDVLREVFEPLGVKVETRSEPYLRSVGLVERGEADAWVG-SYSKEISGVLyprwNFDTDHIYALGL-- 115
Cdd:cd13704   17 FLDENGnpTGFNVDLLRAIAEEMGLKVEIRLGPWSEVLQALENGEIDVLIGmAYSEERAKLF----DFSDPYLEVSVSif 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328 116 ---ASNPAPSLETLGAYRLAWVRGYKYQNYLPNAHHFNEIRRRDGILSMLRH---SRADYYIDALTEVDYVLSQAPDPSV 189
Cdd:cd13704   93 vrkGSSIINSLEDLKGKKVAVQRGDIMHEYLKERGLGINLVLVDSPEEALRLlasGKVDAAVVDRLVGLYLIKELGLTNV 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 515697328 190 frRTHLVEL-PLYLGFSDSERGRALLALYDRRMDELVKGARLRKLFERW 237
Cdd:cd13704  173 --KIVGPPLlPLKYCFAVRKGNPELLAKLNEGLAILKASGEYDEIYEKW 219
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
41-237 6.07e-06

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 45.78  E-value: 6.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328    41 YTNADGS--GLAWDVLREVFEPLGVKVE-TRSEPYLRsVGLVERGEADAwvgsyskeISGVLYPRWNFD----------T 107
Cdd:smart00062  15 FADEDGEltGFDVDLAKAIAKELGLKVEfVEVSFDSL-LTALKSGKIDV--------VAAGMTITPERAkqvdfsdpyyR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328   108 DHIYALGLASNPAPSLETLGAYRLAWVRGYKYQNYLPNAHHFNEIRRRDGI---LSMLRHSRADYYIDALTEVDYVLSQA 184
Cdd:smart00062  86 SGQVILVRKDSPIKSLEDLKGKKVAVVAGTTAEELLKKLYPEAKIVSYDSNaeaLAALKAGRADAAVADAPLLAALVKQH 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 515697328   185 PDPSVFRRTHLVELPLYLGFSDSERGRALLALYDRRMDELVKGARLRKLFERW 237
Cdd:smart00062 166 GLPELKIVPDPLDTPEGYAIAVRKGDPELLDKINKALKELKADGTLKKISEKW 218
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
39-183 4.02e-05

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: 43.29  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328  39 LDYTNADG--SGLAWDVLREVFEPLGVKVETRSEP-YLRSVGLVERGEADAwvgsyskeISGVLY-----PRWNFdTDHI 110
Cdd:cd01007   15 FEFIDEGGepQGIAADYLKLIAKKLGLKFEYVPGDsWSELLEALKAGEIDL--------LSSVSKtpereKYLLF-TKPY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328 111 YALGLA------SNPAPSLETLGAYRLAWVRGYKYQNYLpnAHHFNEIRR------RDGiLSMLRHSRADYYIDALTEVD 178
Cdd:cd01007   86 LSSPLVivtrkdAPFINSLSDLAGKRVAVVKGYALEELL--RERYPNINLvevdstEEA-LEAVASGEADAYIGNLAVAS 162

                 ....*
gi 515697328 179 YVLSQ 183
Cdd:cd01007  163 YLIQK 167
PBP2_YxeM cd13709
Substrate binding domain of an ABC transporter YxeMNO; the type 2 periplasmic binding protein ...
52-237 1.86e-03

Substrate binding domain of an ABC transporter YxeMNO; the type 2 periplasmic binding protein fold; This group contains cystine-binding domain (YxeM) of a periplasmic receptor-dependent ATP-binding cassette transporter and its closely 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: 270427 [Multi-domain]  Cd Length: 227  Bit Score: 38.48  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328  52 DVLREVFEPLGVKVETRSEPYLRSVGLVERGEADAwVGSyskEISgVLYPR---WNFDTDHIY-----ALGLASNPAPSL 123
Cdd:cd13709   28 DVWNAIGKRTGYKVEFVTADFSGLFGMLDSGKVDT-IAN---QIT-ITPERqekYDFSEPYVYdgaqiVVKKDNNSIKSL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515697328 124 ETLGAYRLAWVRGYKYQNYLPNAHHFNEIR-----RRDGILSMLRHSRADYYIDALTEVDYVLSQAPDPSVFRRTHLVEL 198
Cdd:cd13709  103 EDLKGKTVAVNLGSNYEKILKAVDKDNKITiktydDDEGALQDVALGRVDAYVNDRVSLLAKIKKRGLPLKLAGEPLVEE 182
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515697328 199 PLYLGFSDSERGRALLALYDRRMDELVKGARLRKLFERW 237
Cdd:cd13709  183 EIAFPFVKNEKGKKLLEKVNKALEEMRKDGTLKKISEKW 221
 
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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