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Conserved domains on  [gi|1000211132|gb|KXJ80970|]
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hypothetical protein RP20_CCG022429 [Aedes albopictus]

Protein Classification

NPC2 family protein( domain architecture ID 10097044)

NPC2 (Niemann-Pick proteins type C2) family protein similar to Homo sapiens NPC intracellular cholesterol transporter 2 (NPC2) that acts as intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the lysosomal compartment

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Npc2_like cd00916
Niemann-Pick type C2 (Npc2) is a lysosomal protein in which a mutation in the gene causes a ...
 1-105 1.43e-36

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: 120.49  E-value: 1.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000211132   1 MPCLLPRGRDANMAMDFTAVQDASNLRTQVTATALGITAPYELPpeRAAACNWLvQSRCPISAGEDLTYHLSMPVTAIYP 80
Cdd:cd00916    22 LPCKLKRGSTAKVSIDFTPNFDSTSLKTEVHAILLGVPVPFPLP--NPDACKNL-GTSCPLSAGEDVTYTLSLPVLAPYP 98

                          90       100
                  ....*....|....*....|....*
gi 1000211132  81 LVSVTIEMDLVDQSGQSHGCFVVDA 105
Cdd:cd00916    99 GISVTVEWELTDDDGQVLTCFQIPA 123
 
Name Accession Description Interval E-value
Npc2_like cd00916
Niemann-Pick type C2 (Npc2) is a lysosomal protein in which a mutation in the gene causes a ...
 1-105 1.43e-36

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: 120.49  E-value: 1.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000211132   1 MPCLLPRGRDANMAMDFTAVQDASNLRTQVTATALGITAPYELPpeRAAACNWLvQSRCPISAGEDLTYHLSMPVTAIYP 80
Cdd:cd00916    22 LPCKLKRGSTAKVSIDFTPNFDSTSLKTEVHAILLGVPVPFPLP--NPDACKNL-GTSCPLSAGEDVTYTLSLPVLAPYP 98

                          90       100
                  ....*....|....*....|....*
gi 1000211132  81 LVSVTIEMDLVDQSGQSHGCFVVDA 105
Cdd:cd00916    99 GISVTVEWELTDDDGQVLTCFQIPA 123
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 1-107 4.58e-32

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: 460498  Cd Length: 133  Bit Score: 109.38  E-value: 4.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000211132   1 MPCLLPRGRDANMAMDF-TAVQDASNLRTQVTATALGITAPYELPPERAAaCNWLVQ---SRCPISAGEDLTYHLSMPVT 76
Cdd:pfam02221  24 PPCPLVRGQNLTISASGtTSDEISQGLKVDVEVRLGGITLPFPLPETRDL-CDELEVgsgLSCPIKAGEYVTYTLTLPLP 102

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1000211132  77 AIYPLVSVTIEMDLVDQSGQSHGCFVVDARV 107
Cdd:pfam02221 103 SEYPPGKYTVEAELYDQDGKPLTCFKIDVSI 133
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 2-105 1.13e-17

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: 72.01  E-value: 1.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000211132    2 PCLLPRGRDANMAMDFTAVQDASNLRTQVTATALGITAPyeLPPERAAACNwLVQSRCPISAGEDLTYHLSMPVTAIYPL 81
Cdd:smart00737  19 PCPPVRGKTLTISISFTLNEDISKLKVVVHVKIGGIEVP--IPGETYDLCK-LTGSKCPIEKGETVNYTNSLTVPGIFPP 95

                           90       100
                   ....*....|....*....|....
gi 1000211132   82 VSVTIEMDLVDQSGQSHGCFVVDA 105
Cdd:smart00737  96 GKYTVKWELTDEDGEELACINFTV 119
 
Name Accession Description Interval E-value
Npc2_like cd00916
Niemann-Pick type C2 (Npc2) is a lysosomal protein in which a mutation in the gene causes a ...
 1-105 1.43e-36

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: 120.49  E-value: 1.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000211132   1 MPCLLPRGRDANMAMDFTAVQDASNLRTQVTATALGITAPYELPpeRAAACNWLvQSRCPISAGEDLTYHLSMPVTAIYP 80
Cdd:cd00916    22 LPCKLKRGSTAKVSIDFTPNFDSTSLKTEVHAILLGVPVPFPLP--NPDACKNL-GTSCPLSAGEDVTYTLSLPVLAPYP 98

                          90       100
                  ....*....|....*....|....*
gi 1000211132  81 LVSVTIEMDLVDQSGQSHGCFVVDA 105
Cdd:cd00916    99 GISVTVEWELTDDDGQVLTCFQIPA 123
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 1-107 4.58e-32

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: 460498  Cd Length: 133  Bit Score: 109.38  E-value: 4.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000211132   1 MPCLLPRGRDANMAMDF-TAVQDASNLRTQVTATALGITAPYELPPERAAaCNWLVQ---SRCPISAGEDLTYHLSMPVT 76
Cdd:pfam02221  24 PPCPLVRGQNLTISASGtTSDEISQGLKVDVEVRLGGITLPFPLPETRDL-CDELEVgsgLSCPIKAGEYVTYTLTLPLP 102

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1000211132  77 AIYPLVSVTIEMDLVDQSGQSHGCFVVDARV 107
Cdd:pfam02221 103 SEYPPGKYTVEAELYDQDGKPLTCFKIDVSI 133
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 2-105 1.13e-17

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: 72.01  E-value: 1.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000211132    2 PCLLPRGRDANMAMDFTAVQDASNLRTQVTATALGITAPyeLPPERAAACNwLVQSRCPISAGEDLTYHLSMPVTAIYPL 81
Cdd:smart00737  19 PCPPVRGKTLTISISFTLNEDISKLKVVVHVKIGGIEVP--IPGETYDLCK-LTGSKCPIEKGETVNYTNSLTVPGIFPP 95

                           90       100
                   ....*....|....*....|....
gi 1000211132   82 VSVTIEMDLVDQSGQSHGCFVVDA 105
Cdd:smart00737  96 GKYTVKWELTDEDGEELACINFTV 119
Der-p2_like cd00918
Several group 2 allergen proteins belong to the ML domain family. They include ...
 2-107 1.17e-05

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: 41.26  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000211132   2 PCLLPRGRDANMAMDFTAVQDASNLRTQVTATALGItaPYELPPERAAACNWLvqsRCPISAGE--DLTYHLSMPvtAIY 79
Cdd:cd00918    21 YCVIHRGKPLTLEAKFTANQDTAKAKIKITASIDGL--EIDVPGIETDGCKYV---KCPIKKGQhyDIKYTWNVP--AIL 93

                          90       100
                  ....*....|....*....|....*...
gi 1000211132  80 PLVSVTIEMDLVDQSGQShGCFVVDARV 107
Cdd:cd00918    94 PKIKAVVKAVLIGDHGVL-ACGIVNGEV 120
ML cd00912
The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, ...
 2-100 1.34e-04

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: 38.27  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000211132   2 PCLLPRGRDANMAMDFTAVQDASNLRTQVTATALGITAPYELPPERAAACNWLVQSRCPISAGEDLTYHLSMPV-TAIYP 80
Cdd:cd00912    23 PCPDHRGGNYNLSVTGTLREDIKSLYVDLALMSQGIKVLNPDNSYDFCEAGLPKPSFCPLRKGQQYSYAKTVNVpEFTIP 102

                          90       100
                  ....*....|....*....|
gi 1000211132  81 LVSVTIEMDLVDQSGQSHGC 100
Cdd:cd00912   103 TIEYQVVLEDVTDKGEVLAC 122
 
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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