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Conserved domains on  [gi|1247049365|ref|XP_022463297|]
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hypothetical protein KNAG_0B06210 [Huiozyma naganishii CBS 8797]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Seipin_Sei1_like cd23994
Saccharomyces cerevisiae Seipin and similar proteins; Seipin is a homo-oligomeric integral ...
 48-210 6.54e-52

Saccharomyces cerevisiae Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane protein in the endoplasmic reticulum (ER) that concentrates at junctions with cytoplasmic lipid droplets (LDs). It acts as a cell-autonomous regulator of lipolysis essential for adipocyte differentiation. Seipin is predicted to contain two transmembrane domains at N-terminus and C-terminus, respectively. This model corresponds to a group of seipins from Saccharomycotina. Saccharomyces cerevisiae seipin (Sei1), also called few lipid droplets protein 1 (Fld1p), is involved in lipid metabolism and lipid droplet (LD) morphology, number, and size. It facilitates initiation of LD formation and ensures that vectorial budding of LDs from the ER is directed towards the cytoplasm. In contrast to human seipin, Sei1-mediated LD formation depends on Ldb16, a yeast specific binding partner. Sei1 forms a homodecameric ring that scaffolds and positions Ldb16.


:

Pssm-ID: 467828  Cd Length: 176  Bit Score: 167.08  E-value: 6.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247049365  48 DSMLHIPLSKLYKTNHG----SLCLEIDRMG-EGDLPVVANDGLtNQRTFLHGGTTYNLDFKIKFYCLTT---KEQVLHT 119
Cdd:cd23994     1 DSSQWVPLSTFNLTDGEwsgtSFKQDIKRIStDADLPQVIDNGL-SQNIPLRDDIPYKLDLDLKFYCLNKvtdPRLNLDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247049365 120 VFVELESN----HVKMFMREIPVVCARG-DAFVETLLSSSRDTaLRDKYATQWVNELDVEDAVVIPPQTHNFFLSLK--S 192
Cdd:cd23994    80 VTISVSSNnksaDSLLFRKTIPIVCLNTnDSINLSELGKLGPS-RLELYQKEWLNSIHLEDKISIPPDVKHIEVSLKlpG 158

                         170
                  ....*....|....*...
gi 1247049365 193 SSELIFDPDSRIQLRATF 210
Cdd:cd23994   159 AAELIFDPDSGLKFRMNF 176
 
Name Accession Description Interval E-value
Seipin_Sei1_like cd23994
Saccharomyces cerevisiae Seipin and similar proteins; Seipin is a homo-oligomeric integral ...
 48-210 6.54e-52

Saccharomyces cerevisiae Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane protein in the endoplasmic reticulum (ER) that concentrates at junctions with cytoplasmic lipid droplets (LDs). It acts as a cell-autonomous regulator of lipolysis essential for adipocyte differentiation. Seipin is predicted to contain two transmembrane domains at N-terminus and C-terminus, respectively. This model corresponds to a group of seipins from Saccharomycotina. Saccharomyces cerevisiae seipin (Sei1), also called few lipid droplets protein 1 (Fld1p), is involved in lipid metabolism and lipid droplet (LD) morphology, number, and size. It facilitates initiation of LD formation and ensures that vectorial budding of LDs from the ER is directed towards the cytoplasm. In contrast to human seipin, Sei1-mediated LD formation depends on Ldb16, a yeast specific binding partner. Sei1 forms a homodecameric ring that scaffolds and positions Ldb16.


Pssm-ID: 467828  Cd Length: 176  Bit Score: 167.08  E-value: 6.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247049365  48 DSMLHIPLSKLYKTNHG----SLCLEIDRMG-EGDLPVVANDGLtNQRTFLHGGTTYNLDFKIKFYCLTT---KEQVLHT 119
Cdd:cd23994     1 DSSQWVPLSTFNLTDGEwsgtSFKQDIKRIStDADLPQVIDNGL-SQNIPLRDDIPYKLDLDLKFYCLNKvtdPRLNLDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247049365 120 VFVELESN----HVKMFMREIPVVCARG-DAFVETLLSSSRDTaLRDKYATQWVNELDVEDAVVIPPQTHNFFLSLK--S 192
Cdd:cd23994    80 VTISVSSNnksaDSLLFRKTIPIVCLNTnDSINLSELGKLGPS-RLELYQKEWLNSIHLEDKISIPPDVKHIEVSLKlpG 158

                         170
                  ....*....|....*...
gi 1247049365 193 SSELIFDPDSRIQLRATF 210
Cdd:cd23994   159 AAELIFDPDSGLKFRMNF 176
 
Name Accession Description Interval E-value
Seipin_Sei1_like cd23994
Saccharomyces cerevisiae Seipin and similar proteins; Seipin is a homo-oligomeric integral ...
 48-210 6.54e-52

Saccharomyces cerevisiae Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane protein in the endoplasmic reticulum (ER) that concentrates at junctions with cytoplasmic lipid droplets (LDs). It acts as a cell-autonomous regulator of lipolysis essential for adipocyte differentiation. Seipin is predicted to contain two transmembrane domains at N-terminus and C-terminus, respectively. This model corresponds to a group of seipins from Saccharomycotina. Saccharomyces cerevisiae seipin (Sei1), also called few lipid droplets protein 1 (Fld1p), is involved in lipid metabolism and lipid droplet (LD) morphology, number, and size. It facilitates initiation of LD formation and ensures that vectorial budding of LDs from the ER is directed towards the cytoplasm. In contrast to human seipin, Sei1-mediated LD formation depends on Ldb16, a yeast specific binding partner. Sei1 forms a homodecameric ring that scaffolds and positions Ldb16.


Pssm-ID: 467828  Cd Length: 176  Bit Score: 167.08  E-value: 6.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247049365  48 DSMLHIPLSKLYKTNHG----SLCLEIDRMG-EGDLPVVANDGLtNQRTFLHGGTTYNLDFKIKFYCLTT---KEQVLHT 119
Cdd:cd23994     1 DSSQWVPLSTFNLTDGEwsgtSFKQDIKRIStDADLPQVIDNGL-SQNIPLRDDIPYKLDLDLKFYCLNKvtdPRLNLDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247049365 120 VFVELESN----HVKMFMREIPVVCARG-DAFVETLLSSSRDTaLRDKYATQWVNELDVEDAVVIPPQTHNFFLSLK--S 192
Cdd:cd23994    80 VTISVSSNnksaDSLLFRKTIPIVCLNTnDSINLSELGKLGPS-RLELYQKEWLNSIHLEDKISIPPDVKHIEVSLKlpG 158

                         170
                  ....*....|....*...
gi 1247049365 193 SSELIFDPDSRIQLRATF 210
Cdd:cd23994   159 AAELIFDPDSGLKFRMNF 176
 
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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