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Conserved domains on  [gi|21465915|pdb|1KTJ|A]
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Chain A, ALLERGEN DER P 2

Protein Classification

Der-p2_like domain-containing protein( domain architecture ID 10097049)

Der-p2_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Der-p2_like cd00918
Several group 2 allergen proteins belong to the ML domain family. They include ...
5-126 2.67e-65

Several group 2 allergen proteins belong to the ML domain family. They include Dermatophagoides pteronyssinus, group 2 (Der p 2) and D. farinae, group 2 (Der f 2) allergens. These house dust mites cause heavy atopic diseases such as asthma and dermatitis. Although the allergenic properties of these proteins have been well characterized, their biological function in mites is unknown.


:

Pssm-ID: 238460  Cd Length: 120  Bit Score: 193.79  E-value: 2.67e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KTJ_A        5 VKDCANHEIKKVLVPGCHGSePCIIHRGKPFQLEAVFEANQNTKTAKIEIKASIDGLEVDVPGIDPNACHYMKCPLVKGQ 84
Cdd:cd00918   1 FKDCGKGEIKSLEVDGCSGD-YCVIHRGKPLTLEAKFTANQDTAKAKIKITASIDGLEIDVPGIETDGCKYVKCPIKKGQ 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
1KTJ_A       85 QYDIKYTWNVPKIAPKSENVVVTVKVmGDDGVLACAIATHAK 126
Cdd:cd00918  80 HYDIKYTWNVPAILPKIKAVVKAVLI-GDHGVLACGIVNGEV 120
 
Name Accession Description Interval E-value
Der-p2_like cd00918
Several group 2 allergen proteins belong to the ML domain family. They include ...
5-126 2.67e-65

Several group 2 allergen proteins belong to the ML domain family. They include Dermatophagoides pteronyssinus, group 2 (Der p 2) and D. farinae, group 2 (Der f 2) allergens. These house dust mites cause heavy atopic diseases such as asthma and dermatitis. Although the allergenic properties of these proteins have been well characterized, their biological function in mites is unknown.


Pssm-ID: 238460  Cd Length: 120  Bit Score: 193.79  E-value: 2.67e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KTJ_A        5 VKDCANHEIKKVLVPGCHGSePCIIHRGKPFQLEAVFEANQNTKTAKIEIKASIDGLEVDVPGIDPNACHYMKCPLVKGQ 84
Cdd:cd00918   1 FKDCGKGEIKSLEVDGCSGD-YCVIHRGKPLTLEAKFTANQDTAKAKIKITASIDGLEIDVPGIETDGCKYVKCPIKKGQ 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
1KTJ_A       85 QYDIKYTWNVPKIAPKSENVVVTVKVmGDDGVLACAIATHAK 126
Cdd:cd00918  80 HYDIKYTWNVPAILPKIKAVVKAVLI-GDHGVLACGIVNGEV 120
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
5-123 5.73e-26

Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) is a novel domain identified in MD-1, MD-2, GM2A, Npc2 and multiple proteins of unknown function in plants, animals and fungi. These single-domain proteins were predicted to form a beta-rich fold containing multiple strands, and to mediate diverse biological functions through interacting with specific lipids.


Pssm-ID: 214796  Cd Length: 119  Bit Score: 93.97  E-value: 5.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KTJ_A           5 VKDCAN---HEIKKVLVpgchgsEPCIIHRGKPFQLEAVFEANQNTKTAKIEIKASIDGLEVDVPGIDPNACHYM--KCP 79
Cdd:smart00737   1 FKDCGSndpGQISSVSI------SPCPPVRGKTLTISISFTLNEDISKLKVVVHVKIGGIEVPIPGETYDLCKLTgsKCP 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
1KTJ_A          80 LVKGQQYDIKYTWNVPKIAPKSeNVVVTVKVMGDDG-VLACAIAT 123
Cdd:smart00737  75 IEKGETVNYTNSLTVPGIFPPG-KYTVKWELTDEDGeELACINFT 118
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
3-119 1.55e-10

ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins from plants, animals and fungi, including dust mite allergen Der P 2. It has been implicate in lipid recognition, particularly in the recognition of pathogen related products. A mutation in Npc2 causes a rare form of Niemann-Pick type C2 disease. This domain has a similar topology to immunoglobulin domains.


Pssm-ID: 426667  Cd Length: 133  Bit Score: 54.69  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KTJ_A          3 VDVKDCANH-----EIKKVLVpgchgSEPCIIHRGKPFQLEAVFEANQN-TKTAKIEIKASIDGLEVDVP-GIDPNACHY 75
Cdd:pfam02221   2 VPFRDCGRNkddapTPKSVDI-----SPPCPLVRGQNLTISADGTTSDEiSQGLKVDVEVRLGGITLPFPlPETRDLCDE 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
1KTJ_A         76 M------KCPLVKGQQYDIKYTWNVPKIAPKSeNVVVTVKVMGDDG-VLAC 119
Cdd:pfam02221  77 LevglglSCPIKAGEYVTYTLTLPLPSEYPPG-KYTVEAELYDQDGkPLTC 126
 
Name Accession Description Interval E-value
Der-p2_like cd00918
Several group 2 allergen proteins belong to the ML domain family. They include ...
5-126 2.67e-65

Several group 2 allergen proteins belong to the ML domain family. They include Dermatophagoides pteronyssinus, group 2 (Der p 2) and D. farinae, group 2 (Der f 2) allergens. These house dust mites cause heavy atopic diseases such as asthma and dermatitis. Although the allergenic properties of these proteins have been well characterized, their biological function in mites is unknown.


Pssm-ID: 238460  Cd Length: 120  Bit Score: 193.79  E-value: 2.67e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KTJ_A        5 VKDCANHEIKKVLVPGCHGSePCIIHRGKPFQLEAVFEANQNTKTAKIEIKASIDGLEVDVPGIDPNACHYMKCPLVKGQ 84
Cdd:cd00918   1 FKDCGKGEIKSLEVDGCSGD-YCVIHRGKPLTLEAKFTANQDTAKAKIKITASIDGLEIDVPGIETDGCKYVKCPIKKGQ 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
1KTJ_A       85 QYDIKYTWNVPKIAPKSENVVVTVKVmGDDGVLACAIATHAK 126
Cdd:cd00918  80 HYDIKYTWNVPAILPKIKAVVKAVLI-GDHGVLACGIVNGEV 120
ML cd00912
The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, ...
5-124 3.96e-41

The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, Niemann-Pick type C2 (Npc2) protein, phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP), mite allergen Der p 2 and several proteins of unknown function in plants, animals and fungi. These single-domain proteins form two anti-parallel beta-pleated sheets stabilized by three disulfide bonds and with an accessible central hydrophobic cavity, and are predicted to mediate diverse biological functions through interaction with specific lipids.


Pssm-ID: 238454  Cd Length: 127  Bit Score: 132.64  E-value: 3.96e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KTJ_A        5 VKDCAN--HEIKKVLVPGCHGSePCIIHRGKPFQLEAVFEANQNTKTAKIEIKASIDGLEVDVPGIDPNACHYM-----K 77
Cdd:cd00912   1 LVDCSDnsANIKEVLLSPCDPL-PCPDHRGGNYNLSVTGTLREDIKSLYVDLALMSQGIKVLNPDNSYDFCEAGlpkpsF 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1KTJ_A       78 CPLVKGQQYDIKYTWNVPK-IAPKSENVVVTVKVMGDDGVLACAIATH 124
Cdd:cd00912  80 CPLRKGQQYSYAKTVNVPEfTIPTIEYQVVLEDVTDKGEVLACAQATI 127
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
5-123 5.73e-26

Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) is a novel domain identified in MD-1, MD-2, GM2A, Npc2 and multiple proteins of unknown function in plants, animals and fungi. These single-domain proteins were predicted to form a beta-rich fold containing multiple strands, and to mediate diverse biological functions through interacting with specific lipids.


Pssm-ID: 214796  Cd Length: 119  Bit Score: 93.97  E-value: 5.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KTJ_A           5 VKDCAN---HEIKKVLVpgchgsEPCIIHRGKPFQLEAVFEANQNTKTAKIEIKASIDGLEVDVPGIDPNACHYM--KCP 79
Cdd:smart00737   1 FKDCGSndpGQISSVSI------SPCPPVRGKTLTISISFTLNEDISKLKVVVHVKIGGIEVPIPGETYDLCKLTgsKCP 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
1KTJ_A          80 LVKGQQYDIKYTWNVPKIAPKSeNVVVTVKVMGDDG-VLACAIAT 123
Cdd:smart00737  75 IEKGETVNYTNSLTVPGIFPPG-KYTVKWELTDEDGeELACINFT 118
Npc2_like cd00916
Niemann-Pick type C2 (Npc2) is a lysosomal protein in which a mutation in the gene causes a ...
5-119 1.64e-13

Niemann-Pick type C2 (Npc2) is a lysosomal protein in which a mutation in the gene causes a rare form of Niemann-Pick type C disease, an autosomal recessive lipid storage disorder characterized by accumulation of low-density lipoprotein-derived cholesterol in lysosomes. Although Npc2 is known to bind cholesterol, the function of this protein is unknown. These proteins belong to the ML domain family.


Pssm-ID: 238458  Cd Length: 123  Bit Score: 62.33  E-value: 1.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KTJ_A        5 VKDCANHE--IKKVLVPGChGSEPCIIHRGKPFQLEAVFEANQNTKTAKIEIKASIDGLEVDVPGIDPNACHYMK--CPL 80
Cdd:cd00916   1 FRDCGSSRptPSEVRISGC-ATLPCKLKRGSTAKVSIDFTPNFDSTSLKTEVHAILLGVPVPFPLPNPDACKNLGtsCPL 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
1KTJ_A       81 VKGQQYDIKYTWNVPKIAPKSeNVVVTVKVMGDDG-VLAC 119
Cdd:cd00916  80 SAGEDVTYTLSLPVLAPYPGI-SVTVEWELTDDDGqVLTC 118
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
3-119 1.55e-10

ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins from plants, animals and fungi, including dust mite allergen Der P 2. It has been implicate in lipid recognition, particularly in the recognition of pathogen related products. A mutation in Npc2 causes a rare form of Niemann-Pick type C2 disease. This domain has a similar topology to immunoglobulin domains.


Pssm-ID: 426667  Cd Length: 133  Bit Score: 54.69  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KTJ_A          3 VDVKDCANH-----EIKKVLVpgchgSEPCIIHRGKPFQLEAVFEANQN-TKTAKIEIKASIDGLEVDVP-GIDPNACHY 75
Cdd:pfam02221   2 VPFRDCGRNkddapTPKSVDI-----SPPCPLVRGQNLTISADGTTSDEiSQGLKVDVEVRLGGITLPFPlPETRDLCDE 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
1KTJ_A         76 M------KCPLVKGQQYDIKYTWNVPKIAPKSeNVVVTVKVMGDDG-VLAC 119
Cdd:pfam02221  77 LevglglSCPIKAGEYVTYTLTLPLPSEYPPG-KYTVEAELYDQDGkPLTC 126
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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