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Conserved domains on  [gi|2754040503|dbj|BFO12845|]
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spike glycoprotein, partial [Bovine coronavirus]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
CoV_Spike_S1_RBD super family cl40478
receptor-binding domain of the S1 subunit of coronavirus spike (S) proteins; This family ...
 1-137 5.90e-94

receptor-binding domain of the S1 subunit of coronavirus spike (S) proteins; This family contains the receptor-binding domain (RBD) of the S1 subunit of coronavirus (CoV) spike (S) proteins from three highly pathogenic human coronaviruses (CoVs), including Middle East respiratory syndrome coronavirus (MERS-CoV), Severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV), and SARS coronavirus 2 (SARS-CoV-2), also known as a 2019 novel coronavirus (2019-nCoV), as well as S proteins from related coronaviruses. The CoV S protein is an envelope glycoprotein that plays the most important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains a hydrophobic fusion peptide and two heptad repeat regions. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the C-terminal domain (C-domain). Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBD of mouse hepatitis virus (MHV) is located at the NTD, most CoVs, including SARS-CoV-2, SARS-CoV and MERS-CoV use the C-domain to bind their receptors. MHV uses mouse carcinoembryonic antigen related cell adhesion molecule 1a (mCEACAM1a) as the receptor, and the receptors for SARS-CoV and MERS-CoV are human angiotensin-converting enzyme 2 (ACE2) and human dipeptidyl peptidase 4 (DPP4), respectively. Recent studies found that the RBD of SARS-CoV-2 S protein binds strongly to human and bat angiotensin-converting enzyme 2 (ACE2) receptors. Moreover, SARS-CoV-2 RBD exhibited significantly higher binding affinity to the ACE2 receptor than SARS-CoV RBD. Due to the key role of the S protein RBD in viral attachment, it is the major target for antibody-mediated neutralization. This model corresponds to the S1 subunit C-domain that serves as the RBD for most CoVs.


The actual alignment was detected with superfamily member cd21485:

Pssm-ID: 424109  Cd Length: 312  Bit Score: 273.81  E-value: 5.90e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754040503   1 EQSVFKPQPAGVFTDHDVVYAQHCFKAPTNFCPCKLGGSLCVGNGPGIDAGYKTTGIGICPAGTNYLTCHNAAQCDCLCT 80
Cdd:cd21485   146 EQSVFKPQPAGVFTDHDVVYAQHCFKAPTNFCPCKLDGSLCVGSGPGIDAGYKNNGIGTCPAGTNYLTCHNLCQCDCLCT 225

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2754040503  81 PDPITSKATGSYKCPQTKYLVGIGEHCSGLAIKSDHCGGNPCSCQPQAFLGWSVDSC 137
Cdd:cd21485   226 PDPITSKATGPYKCPQTKYLVGIGEHCSGLAIKSDYCGGNPCTCQPQAFLGWSVDSC 282
 
Name Accession Description Interval E-value
HCoV-OC43-like_Spike_S1_RBD cd21485
receptor-binding domain of the S1 subunit of the Spike (S) protein from human coronavirus OC43 ...
 1-137 5.90e-94

receptor-binding domain of the S1 subunit of the Spike (S) protein from human coronavirus OC43 and related proteins; This group contains the receptor-binding domain (RBD) of the S1 subunit of the spike (S) protein from several betacoronaviruses including human coronavirus OC43 (HCoV-OC43) and bovine respiratory coronavirus (BCoV), among others. HCoV-OC43 is of zoonotic origin and is endemic in the human population, causing mild respiratory tract infections and possible severe complications or fatalities in young children, the elderly, and immunocompromised individuals. These viruses are related to the zoonotic SARS and MERS betacoronaviruses, which have high fatality rates and pandemic potential. The CoV S protein is an envelope glycoprotein that plays the most important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains a hydrophobic fusion peptide and two heptad repeat regions. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the C-terminal domain (C-domain). Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBD of mouse hepatitis virus (MHV) is located at the NTD, most CoVs use the C-domain to bind their receptors. It has been reported that HCoV-OC43 uses 9-O-acetyl-sialic acid (9-O-Ac-Sia) as a receptor, which is terminally linked to oligosaccharides decorating glycoproteins and gangliosides at the host cell surface. HCoV-OC43 appears to bind 9-O-Ac-Sia at the NTD. Due to the key role of the S protein RBD in viral attachment, it is the major target for antibody-mediated neutralization. This model corresponds to the S1 subunit C-domain that serves as the RBD for most CoVs.


Pssm-ID: 394832  Cd Length: 312  Bit Score: 273.81  E-value: 5.90e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754040503   1 EQSVFKPQPAGVFTDHDVVYAQHCFKAPTNFCPCKLGGSLCVGNGPGIDAGYKTTGIGICPAGTNYLTCHNAAQCDCLCT 80
Cdd:cd21485   146 EQSVFKPQPAGVFTDHDVVYAQHCFKAPTNFCPCKLDGSLCVGSGPGIDAGYKNNGIGTCPAGTNYLTCHNLCQCDCLCT 225

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2754040503  81 PDPITSKATGSYKCPQTKYLVGIGEHCSGLAIKSDHCGGNPCSCQPQAFLGWSVDSC 137
Cdd:cd21485   226 PDPITSKATGPYKCPQTKYLVGIGEHCSGLAIKSDYCGGNPCTCQPQAFLGWSVDSC 282
 
Name Accession Description Interval E-value
HCoV-OC43-like_Spike_S1_RBD cd21485
receptor-binding domain of the S1 subunit of the Spike (S) protein from human coronavirus OC43 ...
 1-137 5.90e-94

receptor-binding domain of the S1 subunit of the Spike (S) protein from human coronavirus OC43 and related proteins; This group contains the receptor-binding domain (RBD) of the S1 subunit of the spike (S) protein from several betacoronaviruses including human coronavirus OC43 (HCoV-OC43) and bovine respiratory coronavirus (BCoV), among others. HCoV-OC43 is of zoonotic origin and is endemic in the human population, causing mild respiratory tract infections and possible severe complications or fatalities in young children, the elderly, and immunocompromised individuals. These viruses are related to the zoonotic SARS and MERS betacoronaviruses, which have high fatality rates and pandemic potential. The CoV S protein is an envelope glycoprotein that plays the most important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains a hydrophobic fusion peptide and two heptad repeat regions. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the C-terminal domain (C-domain). Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBD of mouse hepatitis virus (MHV) is located at the NTD, most CoVs use the C-domain to bind their receptors. It has been reported that HCoV-OC43 uses 9-O-acetyl-sialic acid (9-O-Ac-Sia) as a receptor, which is terminally linked to oligosaccharides decorating glycoproteins and gangliosides at the host cell surface. HCoV-OC43 appears to bind 9-O-Ac-Sia at the NTD. Due to the key role of the S protein RBD in viral attachment, it is the major target for antibody-mediated neutralization. This model corresponds to the S1 subunit C-domain that serves as the RBD for most CoVs.


Pssm-ID: 394832  Cd Length: 312  Bit Score: 273.81  E-value: 5.90e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754040503   1 EQSVFKPQPAGVFTDHDVVYAQHCFKAPTNFCPCKLGGSLCVGNGPGIDAGYKTTGIGICPAGTNYLTCHNAAQCDCLCT 80
Cdd:cd21485   146 EQSVFKPQPAGVFTDHDVVYAQHCFKAPTNFCPCKLDGSLCVGSGPGIDAGYKNNGIGTCPAGTNYLTCHNLCQCDCLCT 225

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2754040503  81 PDPITSKATGSYKCPQTKYLVGIGEHCSGLAIKSDHCGGNPCSCQPQAFLGWSVDSC 137
Cdd:cd21485   226 PDPITSKATGPYKCPQTKYLVGIGEHCSGLAIKSDYCGGNPCTCQPQAFLGWSVDSC 282
HEV_Spike_S1_RBD cd21508
receptor-binding domain of the S1 subunit of the Spike (S) protein from porcine ...
 16-137 4.63e-31

receptor-binding domain of the S1 subunit of the Spike (S) protein from porcine hemagglutinating encephalomyelitis virus; This group contains the receptor-binding domain (RBD) of the S1 subunit of the spike (S) protein from porcine hemagglutinating encephalomyelitis virus (HEV), which is associated with acute outbreaks of wasting and encephalitis in nursing piglets from pig farms. Porcine HEV is related to the zoonotic SARS and MERS betacoronaviruses, which have high fatality rates and pandemic potential. The CoV S protein is an envelope glycoprotein that plays the most important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains a hydrophobic fusion peptide and two heptad repeat regions. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the C-terminal domain (C-domain). Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBD of mouse hepatitis virus (MHV) is located at the NTD, most CoVs use the C-domain to bind their receptors. The protein receptor for porcine HEV has not yet been identified. Due to the key role of the S protein RBD in viral attachment, it is the major target for antibody-mediated neutralization. This model corresponds to the S1 subunit C-domain that serves as the RBD for most CoVs.


Pssm-ID: 394835  Cd Length: 298  Bit Score: 112.52  E-value: 4.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754040503  16 HDVVYAQHCFKAPTNFCPCKLggSLCVGNGpgidagykttGIGICPAGTNYLTCH----NAAQCDCLCTPDPITSKATGS 91
Cdd:cd21508   155 HDAVYSQQCFNTPNTYCPCRT--SQCIGGA----------GTGTCPVGTTVRKCFaavtNATKCTCWCQPDPSTYKGVNA 222

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2754040503  92 YKCPQTKYLVGIGEHCSGLAIKSDHCGGNPCSCQPQAFLGWSVDSC 137
Cdd:cd21508   223 WTCPQSKVSIQPGQHCPGLGLVEDDCSGNPCTCKPQAFIGWSSETC 268
HKU1_N5-like_CoV_Spike_S1_RBD cd21482
receptor-binding domain of the S1 subunit of the Spike (S) protein from human coronavirus HKU1, ...
 13-137 1.77e-23

receptor-binding domain of the S1 subunit of the Spike (S) protein from human coronavirus HKU1, isolate N5 and isolate N2; This group contains the receptor-binding domain (RBD) of the S1 subunit of the spike (S) protein from human coronavirus (CoV) HKU1, isolates N5 and N2. HKU1 is a human betacoronavirus that causes mild yet prevalent respiratory disease, and is related to the zoonotic SARS and MERS betacoronaviruses, which have high fatality rates and pandemic potential. The CoV S protein is an envelope glycoprotein that plays the most important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains a hydrophobic fusion peptide and two heptad repeat regions. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the C-terminal domain (C-domain). Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBD of mouse hepatitis virus (MHV) is located at the NTD, most CoVs use the C-domain to bind their receptors. Although a protein receptor has not yet been identified for HKU1, antibodies against the C-domain, but not those against the NTD, blocked HKU1 infection of cells, suggesting that the S1 C-domain is the primary HKU1 receptor-binding site. Due to the key role of the S protein RBD in viral attachment, it is the major target for antibody-mediated neutralization. This model corresponds to the S1 subunit C-domain that serves as the RBD for most CoVs, and most likely, for HKU1.


Pssm-ID: 394829  Cd Length: 304  Bit Score: 92.44  E-value: 1.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754040503  13 FTDHDVVYAQHCFKAPTNFCPCKLGG--SLCVGNGPGIdagykttgiGICPAGTNYLTC------HNAAQCDCLCTPDPI 84
Cdd:cd21482   149 VSSYDVVYSDHCFSVNSDFCPCADPSvvNSCVKSKPLS---------AICPAGTKYRHCdldttlYVKNWCRCSCLPDPI 219

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2754040503  85 TSKATGSykCPQTKYLVGIGEHCSGLAIKSDHCGG----NPCSCQPQAFLGWSVDSC 137
Cdd:cd21482   220 STYSPNT--CPQKKVVVGIGEHCPGLGINEEKCGTqlnhSSCSCSPDAFLGWSFDSC 274
HKU1_N1_CoV_Spike_S1_RBD cd21483
receptor-binding domain of the S1 subunit of the Spike (S) protein from human coronavirus HKU1, ...
 13-137 3.93e-20

receptor-binding domain of the S1 subunit of the Spike (S) protein from human coronavirus HKU1, isolate N1; This group contains the receptor-binding domain (RBD) of the S1 subunit of the spike (S) protein from human coronavirus (CoV) HKU1, isolate N1. HKU1 is a human betacoronavirus that causes mild yet prevalent respiratory disease, and is related to the zoonotic SARS and MERS betacoronaviruses, which have high fatality rates and pandemic potential. The CoV S protein is an envelope glycoprotein that plays the most important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains a hydrophobic fusion peptide and two heptad repeat regions. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the C-terminal domain (C-domain). Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBD of mouse hepatitis virus (MHV) is located at the NTD, most CoVs use the C-domain to bind their receptors. Although a protein receptor has not yet been identified for HKU1, antibodies against the C-domain, but not those against the NTD, blocked HKU1 infection of cells, suggesting that the S1 C-domain is the primary HKU1 receptor-binding site. Due to the key role of the S protein RBD in viral attachment, it is the major target for antibody-mediated neutralization. This model corresponds to the S1 subunit C-domain that serves as the RBD for most CoVs, and most likely, for HKU1.


Pssm-ID: 394830  Cd Length: 306  Bit Score: 83.62  E-value: 3.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754040503  13 FTDHDVVYAQHCFKAPTNFCPCKLG--GSLCVGNGPGIDAgykttgigiCPAGTNYLTCHNAA------QCDCLCTPDPI 84
Cdd:cd21483   149 LSSHSVVYSRYCFSVNNTFCPCAKPsfASSCKSHKPPSAS---------CPIGTNYRSCESTTvldhtdWCRCSCLPDPI 219

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2754040503  85 TskATGSYKCPQTKYLVGIGEHCSGLAIKSDHCG------GNPCSCQPQAFLGWSVDSC 137
Cdd:cd21483   220 T--AYDPRSCSQKKSLVGVGEHCAGFGVDEEKCGvldgsyNVSCLCSTDAFLGWSYDTC 276
MHV-like_Spike_S1_RBD cd21484
receptor-binding domain of the S1 subunit of the Spike (S) protein from mouse hepatitis virus ...
 10-137 6.03e-15

receptor-binding domain of the S1 subunit of the Spike (S) protein from mouse hepatitis virus and other rodent coronaviruses; This group contains the receptor-binding domain (RBD) of the S1 subunit of the spike (S) protein from mouse hepatitis virus (MHV) and other rodent coronaviruses. MHV is the most common viral pathogen in contemporary laboratory mouse colonies manifesting as a primary infection in the upper respiratory tract. The CoV S protein is an envelope glycoprotein that plays the most important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains a hydrophobic fusion peptide and two heptad repeat regions. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the C-terminal domain (C-domain). Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). MHV uses mouse carcinoembryonic antigen related cell adhesion molecule 1a (mCEACAM1a) as the receptor; the RBD of MHV is located at the NTD. Most CoVs, such as SARS-CoV and MERS-CoV, use the C-domain to bind their receptors. Due to the key role of the S protein RBD in viral attachment, it is the major target for antibody-mediated neutralization. This model corresponds to the S1 subunit C-domain that serves as the RBD for most CoVs.


Pssm-ID: 394831  Cd Length: 264  Bit Score: 69.14  E-value: 6.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754040503  10 AGVFTD--HDVVYAQHCFKAPTNFCPCklggslcvgngpgidagykttgigicpagtnyltchnaaqcdclCTPDPITSK 87
Cdd:cd21484   147 VATFGKgkHDVAYAQQCFTVGASYCPC--------------------------------------------AQPSIVSPC 182

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2754040503  88 ATGSYK-CPQTKYLVGIGEHCSGLAIKSDHCGG-NPCSCQPQAFLGWSVDSC 137
Cdd:cd21484   183 TTDKPKrCLQGDSCLGVGDHCDGLGVLEDKCGGsNGCNCAADAFVGWSHDSC 234
HKU1-like_CoV_Spike_S1_RBD cd21478
receptor-binding domain of the S1 subunit of the Spike (S) protein from human coronavirus HKU1 ...
 5-35 1.29e-09

receptor-binding domain of the S1 subunit of the Spike (S) protein from human coronavirus HKU1 and related coronaviruses; This family contains the receptor-binding domain (RBD) of the S1 subunit of the spike (S) protein from human coronavirus (CoV) HKU1, human coronavirus OC43 (HCoV-OC43), mouse hepatitis virus (MHV), porcine hemagglutinating encephalomyelitis virus (HEV), and other related coronaviruses. HKU1 is a human betacoronavirus that causes mild yet prevalent respiratory disease. HCoV-OC43 is of zoonotic origin and is endemic in the human population, causing mild respiratory tract infections and possible severe complications or fatalities in young children, the elderly, and immunocompromised individuals. MHV is the most common viral pathogen in contemporary laboratory mouse colonies manifesting as a primary infection in the upper respiratory tract. Porcine HEV is associated with acute outbreaks of wasting and encephalitis in nursing piglets from pig farms. These viruses are related to the zoonotic SARS and MERS betacoronaviruses, which have high fatality rates and pandemic potential. The CoV S protein is an envelope glycoprotein that plays the most important role in viral attachment, fusion and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains a hydrophobic fusion peptide and two heptad repeat regions. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the C-terminal domain (C-domain). Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBDs of MHV and HCoV-OC43 are located at the NTD, most CoVs use the C-domain to bind their receptors. Although a protein receptor has not yet been identified for HKU1, antibodies against the C-domain, but not those against the NTD, blocked HKU1 infection of cells, suggesting that the S1 C-domain is the primary HKU1 receptor-binding site. Due to the key role of the S protein RBD in viral attachment, it is the major target for antibody-mediated neutralization. This model corresponds to the S1 subunit C-domain that serves as the RBD for most CoVs.


Pssm-ID: 394825  Cd Length: 223  Bit Score: 54.00  E-value: 1.29e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2754040503   5 FKPQPAGVFTDHDVVYAQHCFKAPTNFCPCK 35
Cdd:cd21478   147 FKPKPAGNLGNHDVVYSQQCFNVPNTYCPCK 177
 
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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