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Conserved domains on  [gi|268557650|ref|XP_002636815|]
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Protein CBR-JAMP-1 [Caenorhabditis briggsae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
JAMP pfam05571
JNK1/MAPK8-associated membrane protein; This family consists of several eukaryotic proteins ...
 236-534 2.31e-127

JNK1/MAPK8-associated membrane protein; This family consists of several eukaryotic proteins including JAMP, a Jun N-terminal kinase 1 (JNK1)-associated membrane protein. It associates with JNK1 through its C-terminal domain and regulates the duration of JNK1 activity in response to diverse stress stimuli. It is an important component for coordinated clearance of misfolded proteins from the ER.


:

Pssm-ID: 398936  Cd Length: 292  Bit Score: 373.89  E-value: 2.31e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650  236 CLG-FCGRSFISTNyseeatstsSLSQCGACSFGYRSNATSICVPCETPLQAYDWMYLLFIALLPLLLHMQFIRVARKYC 314
Cdd:pfam05571   1 CPGlYCGRTLLENG---------TWSECGACPRGYRVNASSICQPCTDSPELYDWLYLGFMALLPLVLHWFFIDMTSKYR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650  315 RTRYYEVSEYLCVILENVIACVISVLIYPPRFSFFLNGCEKTGLKEWYPACYNPKIGYTKTMRCTYEVVFPLYSITFVHH 394
Cdd:pfam05571  72 RFSKKVIILHLSALIEIVLAALITLLVYEPIGSLTLNSCRVRRLSDWYTLFYNPSPDYETTLHCTQEAVYPLYSIVFIFY 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650  395 MILMGAIFTLRSILYC-AMLYKAYNAKPYYLAIVSVPLLVMIHSVLSGLIFYSFPYILLIGSLWAMCFHLALEGKRPLKE 473
Cdd:pfam05571 152 ALCLVLMLLIRPLLYSkFLLRKGKNTKSIYAALYFFPILALIHAVLGGLIYYSFPYIVIVLSVISNAVHFALKLDQSLKA 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 268557650  474 MIVRLATSPTHWVFLTITMLMLSFGVVALITPLDIQYRWSLLCLVPVPLVFYLITIPFSNP 534
Cdd:pfam05571 232 LIVSSVTNPRNVVILFGHWLLHAYGIIAITELKEPKYHWALLLLVPLPALFYILTARFTDP 292
Seipin pfam06775
Putative adipose-regulatory protein (Seipin); Seipin is a protein of approximately 400 ...
 17-212 3.37e-38

Putative adipose-regulatory protein (Seipin); Seipin is a protein of approximately 400 residues, in humans, which is the product of a gene homologous to the murine guanine nucleotide-binding protein (G protein) gamma-3 linked gene. This gene is implicated in the regulation of body fat distribution and insulin resistance and particularly in the auto-immune disease Berardinelli-Seip congenital lipodystrophy type 2. Seipin has no similarity with other known proteins or consensus motifs that might predict its function, but it is predicted to contain two transmembrane domains at residues 28-49 and 237-258, in human, and a third transmembrane domain might be present at residues 155-173. Seipin may also be implicated in Silver spastic paraplegia syndrome and distal hereditary motor neuropathy type V.


:

Pssm-ID: 462007  Cd Length: 195  Bit Score: 138.82  E-value: 3.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650   17 SIVAFIAAFLPLLIRYAALPTSVHhQYPLNVVFRTCDHdlhsvcsfPSATLEYEK-NSLFSPNVAYYLNVRLKFADIASS 95
Cdd:pfam06775   1 LLLLVLSVVAYGLFYYAYVPEPVL-SRPLHFQYGTGSN--------PYATVSLTSrASLLPPGQPYDVSVELTLPESPYN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650   96 KKLGFFQSVISITEENGKVVQQYTKSA---YVKEPglITKASQVFLFPLYILGYLYDYSTLTISMSENYLEQLGSPSTKL 172
Cdd:pfam06775  72 LELGNFMVRLELLSSNGKVLASSRRPAmlpYRSPL--VRLLRTLLLLPPYLLGLREESQTLRVPMFESVVEGRENPPTSA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 268557650  173 IFTVQD-KFANIEEAELTVTARFGLIRHLIYYWPVMSYTAI 212
Cdd:pfam06775 150 RVEIQSaGLLQIYSAELIFEARLPGLRYLMYNWPITSFVVG 190
 
Name Accession Description Interval E-value
JAMP pfam05571
JNK1/MAPK8-associated membrane protein; This family consists of several eukaryotic proteins ...
 236-534 2.31e-127

JNK1/MAPK8-associated membrane protein; This family consists of several eukaryotic proteins including JAMP, a Jun N-terminal kinase 1 (JNK1)-associated membrane protein. It associates with JNK1 through its C-terminal domain and regulates the duration of JNK1 activity in response to diverse stress stimuli. It is an important component for coordinated clearance of misfolded proteins from the ER.


Pssm-ID: 398936  Cd Length: 292  Bit Score: 373.89  E-value: 2.31e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650  236 CLG-FCGRSFISTNyseeatstsSLSQCGACSFGYRSNATSICVPCETPLQAYDWMYLLFIALLPLLLHMQFIRVARKYC 314
Cdd:pfam05571   1 CPGlYCGRTLLENG---------TWSECGACPRGYRVNASSICQPCTDSPELYDWLYLGFMALLPLVLHWFFIDMTSKYR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650  315 RTRYYEVSEYLCVILENVIACVISVLIYPPRFSFFLNGCEKTGLKEWYPACYNPKIGYTKTMRCTYEVVFPLYSITFVHH 394
Cdd:pfam05571  72 RFSKKVIILHLSALIEIVLAALITLLVYEPIGSLTLNSCRVRRLSDWYTLFYNPSPDYETTLHCTQEAVYPLYSIVFIFY 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650  395 MILMGAIFTLRSILYC-AMLYKAYNAKPYYLAIVSVPLLVMIHSVLSGLIFYSFPYILLIGSLWAMCFHLALEGKRPLKE 473
Cdd:pfam05571 152 ALCLVLMLLIRPLLYSkFLLRKGKNTKSIYAALYFFPILALIHAVLGGLIYYSFPYIVIVLSVISNAVHFALKLDQSLKA 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 268557650  474 MIVRLATSPTHWVFLTITMLMLSFGVVALITPLDIQYRWSLLCLVPVPLVFYLITIPFSNP 534
Cdd:pfam05571 232 LIVSSVTNPRNVVILFGHWLLHAYGIIAITELKEPKYHWALLLLVPLPALFYILTARFTDP 292
Seipin pfam06775
Putative adipose-regulatory protein (Seipin); Seipin is a protein of approximately 400 ...
 17-212 3.37e-38

Putative adipose-regulatory protein (Seipin); Seipin is a protein of approximately 400 residues, in humans, which is the product of a gene homologous to the murine guanine nucleotide-binding protein (G protein) gamma-3 linked gene. This gene is implicated in the regulation of body fat distribution and insulin resistance and particularly in the auto-immune disease Berardinelli-Seip congenital lipodystrophy type 2. Seipin has no similarity with other known proteins or consensus motifs that might predict its function, but it is predicted to contain two transmembrane domains at residues 28-49 and 237-258, in human, and a third transmembrane domain might be present at residues 155-173. Seipin may also be implicated in Silver spastic paraplegia syndrome and distal hereditary motor neuropathy type V.


Pssm-ID: 462007  Cd Length: 195  Bit Score: 138.82  E-value: 3.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650   17 SIVAFIAAFLPLLIRYAALPTSVHhQYPLNVVFRTCDHdlhsvcsfPSATLEYEK-NSLFSPNVAYYLNVRLKFADIASS 95
Cdd:pfam06775   1 LLLLVLSVVAYGLFYYAYVPEPVL-SRPLHFQYGTGSN--------PYATVSLTSrASLLPPGQPYDVSVELTLPESPYN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650   96 KKLGFFQSVISITEENGKVVQQYTKSA---YVKEPglITKASQVFLFPLYILGYLYDYSTLTISMSENYLEQLGSPSTKL 172
Cdd:pfam06775  72 LELGNFMVRLELLSSNGKVLASSRRPAmlpYRSPL--VRLLRTLLLLPPYLLGLREESQTLRVPMFESVVEGRENPPTSA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 268557650  173 IFTVQD-KFANIEEAELTVTARFGLIRHLIYYWPVMSYTAI 212
Cdd:pfam06775 150 RVEIQSaGLLQIYSAELIFEARLPGLRYLMYNWPITSFVVG 190
Seipin_BSCL2_like cd23995
Homo sapiens Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane ...
 38-195 4.21e-27

Homo sapiens 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. Human seipin, also called Bernardinelli-Seip congenital lipodystrophy type 2 protein (BSCL2), may contain a third transmembrane domain in the middle region. Mutations in the seipin gene underlie Human congenital generalized lipodystrophy. Seipin may also be implicated in Silver spastic paraplegia syndrome and distal hereditary motor neuropathy type V. Human seipin exists as an undecamer, and this oligomerization state is critical for its physiological function. Seipin homologs from fungi, plants and insects are also included in this family. There are three SEIPIN homologs in Arabidopsis thaliana, designated SEIPIN1, SEIPIN2, and SEIPIN3.


Pssm-ID: 467829  Cd Length: 162  Bit Score: 106.94  E-value: 4.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650  38 SVHHQYPLNVVFRTCDHdlHSVCSFPSATLEYEKNS---LFSPNVAYYLNVRLKFADIASSKKLGFFQSVISITEENGKV 114
Cdd:cd23995    2 PVSHERPVHFQYGTCCD--AGVCSFPSATVSLTPGGlsqLLSPGQPYDVSLELELPESPVNRDLGNFMVSLELLSADGTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650 115 VQQYTKSAYVK-EPGLITKASQVFLFPLYILGYLYDYSTLTISMSENYLEQLGSPSTKLIFTVQDKFANIEEAELTVTAR 193
Cdd:cd23995   80 LASSSRPAILRyRSPLVRLLRTLLFLPPLLLGLSEETQTLSVPLFEGFVEDPDNPTTSARVELQSRLLQIYSASLRIHAR 159


                 ..
gi 268557650 194 FG 195
Cdd:cd23995  160 LS 161
 
Name Accession Description Interval E-value
JAMP pfam05571
JNK1/MAPK8-associated membrane protein; This family consists of several eukaryotic proteins ...
 236-534 2.31e-127

JNK1/MAPK8-associated membrane protein; This family consists of several eukaryotic proteins including JAMP, a Jun N-terminal kinase 1 (JNK1)-associated membrane protein. It associates with JNK1 through its C-terminal domain and regulates the duration of JNK1 activity in response to diverse stress stimuli. It is an important component for coordinated clearance of misfolded proteins from the ER.


Pssm-ID: 398936  Cd Length: 292  Bit Score: 373.89  E-value: 2.31e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650  236 CLG-FCGRSFISTNyseeatstsSLSQCGACSFGYRSNATSICVPCETPLQAYDWMYLLFIALLPLLLHMQFIRVARKYC 314
Cdd:pfam05571   1 CPGlYCGRTLLENG---------TWSECGACPRGYRVNASSICQPCTDSPELYDWLYLGFMALLPLVLHWFFIDMTSKYR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650  315 RTRYYEVSEYLCVILENVIACVISVLIYPPRFSFFLNGCEKTGLKEWYPACYNPKIGYTKTMRCTYEVVFPLYSITFVHH 394
Cdd:pfam05571  72 RFSKKVIILHLSALIEIVLAALITLLVYEPIGSLTLNSCRVRRLSDWYTLFYNPSPDYETTLHCTQEAVYPLYSIVFIFY 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650  395 MILMGAIFTLRSILYC-AMLYKAYNAKPYYLAIVSVPLLVMIHSVLSGLIFYSFPYILLIGSLWAMCFHLALEGKRPLKE 473
Cdd:pfam05571 152 ALCLVLMLLIRPLLYSkFLLRKGKNTKSIYAALYFFPILALIHAVLGGLIYYSFPYIVIVLSVISNAVHFALKLDQSLKA 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 268557650  474 MIVRLATSPTHWVFLTITMLMLSFGVVALITPLDIQYRWSLLCLVPVPLVFYLITIPFSNP 534
Cdd:pfam05571 232 LIVSSVTNPRNVVILFGHWLLHAYGIIAITELKEPKYHWALLLLVPLPALFYILTARFTDP 292
Seipin pfam06775
Putative adipose-regulatory protein (Seipin); Seipin is a protein of approximately 400 ...
 17-212 3.37e-38

Putative adipose-regulatory protein (Seipin); Seipin is a protein of approximately 400 residues, in humans, which is the product of a gene homologous to the murine guanine nucleotide-binding protein (G protein) gamma-3 linked gene. This gene is implicated in the regulation of body fat distribution and insulin resistance and particularly in the auto-immune disease Berardinelli-Seip congenital lipodystrophy type 2. Seipin has no similarity with other known proteins or consensus motifs that might predict its function, but it is predicted to contain two transmembrane domains at residues 28-49 and 237-258, in human, and a third transmembrane domain might be present at residues 155-173. Seipin may also be implicated in Silver spastic paraplegia syndrome and distal hereditary motor neuropathy type V.


Pssm-ID: 462007  Cd Length: 195  Bit Score: 138.82  E-value: 3.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650   17 SIVAFIAAFLPLLIRYAALPTSVHhQYPLNVVFRTCDHdlhsvcsfPSATLEYEK-NSLFSPNVAYYLNVRLKFADIASS 95
Cdd:pfam06775   1 LLLLVLSVVAYGLFYYAYVPEPVL-SRPLHFQYGTGSN--------PYATVSLTSrASLLPPGQPYDVSVELTLPESPYN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650   96 KKLGFFQSVISITEENGKVVQQYTKSA---YVKEPglITKASQVFLFPLYILGYLYDYSTLTISMSENYLEQLGSPSTKL 172
Cdd:pfam06775  72 LELGNFMVRLELLSSNGKVLASSRRPAmlpYRSPL--VRLLRTLLLLPPYLLGLREESQTLRVPMFESVVEGRENPPTSA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 268557650  173 IFTVQD-KFANIEEAELTVTARFGLIRHLIYYWPVMSYTAI 212
Cdd:pfam06775 150 RVEIQSaGLLQIYSAELIFEARLPGLRYLMYNWPITSFVVG 190
Seipin_BSCL2_like cd23995
Homo sapiens Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane ...
 38-195 4.21e-27

Homo sapiens 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. Human seipin, also called Bernardinelli-Seip congenital lipodystrophy type 2 protein (BSCL2), may contain a third transmembrane domain in the middle region. Mutations in the seipin gene underlie Human congenital generalized lipodystrophy. Seipin may also be implicated in Silver spastic paraplegia syndrome and distal hereditary motor neuropathy type V. Human seipin exists as an undecamer, and this oligomerization state is critical for its physiological function. Seipin homologs from fungi, plants and insects are also included in this family. There are three SEIPIN homologs in Arabidopsis thaliana, designated SEIPIN1, SEIPIN2, and SEIPIN3.


Pssm-ID: 467829  Cd Length: 162  Bit Score: 106.94  E-value: 4.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650  38 SVHHQYPLNVVFRTCDHdlHSVCSFPSATLEYEKNS---LFSPNVAYYLNVRLKFADIASSKKLGFFQSVISITEENGKV 114
Cdd:cd23995    2 PVSHERPVHFQYGTCCD--AGVCSFPSATVSLTPGGlsqLLSPGQPYDVSLELELPESPVNRDLGNFMVSLELLSADGTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650 115 VQQYTKSAYVK-EPGLITKASQVFLFPLYILGYLYDYSTLTISMSENYLEQLGSPSTKLIFTVQDKFANIEEAELTVTAR 193
Cdd:cd23995   80 LASSSRPAILRyRSPLVRLLRTLLFLPPLLLGLSEETQTLSVPLFEGFVEDPDNPTTSARVELQSRLLQIYSASLRIHAR 159


                 ..
gi 268557650 194 FG 195
Cdd:cd23995  160 LS 161
Seipin cd23993
Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane protein in the ...
 38-194 6.88e-04

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. Human seipin, also called Bernardinelli-Seip congenital lipodystrophy type 2 protein (BSCL2), may contain a third transmembrane domain in the middle region. Mutations in the seipin gene underlie human congenital generalized lipodystrophy. Seipin may also be implicated in Silver spastic paraplegia syndrome and distal hereditary motor neuropathy type V. Seipin homologs from fungi, plants, and insects are also included in this family. There are three SEIPIN homologs in Arabidopsis thaliana, designated SEIPIN1, SEIPIN2, and SEIPIN3. Saccharomyces cerevisiae Seipin (Sei1) is also called few lipid droplets protein 1 (Fld1p). Similar to their animal homologs, plant and yeast seipins also play roles in lipid droplet (LD) biogenesis. Human seipin exists as an undecamer, and this oligomerization state is critical for its physiological function. In contrast to Human seipin, S. cerevisiae Sei1-mediated LD formation depends on Ldb16, a yeast specific binding partner. Sei1 forms a homodecameric ring that scaffolds and positions Ldb16.


Pssm-ID: 467827  Cd Length: 163  Bit Score: 40.36  E-value: 6.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650  38 SVHHQYPLNVVFRTCdHDLHSVCSFPSATLEYEKNS-LFSPNV--AYYLNVRLKFADIASSKKLGFFQSVISITEENGKV 114
Cdd:cd23993    2 SNSHPLPVHNGVQTC-LETSTPCTFPGAKVSLTKKSiPVGDMMgqKYDVNLQLYCPESPQNDHLGMFNVLIDVYRGPDEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268557650 115 VQQYTKSAYVK-EPGLITKASQVFLFPLYILGYLYDYSTLTISMSENYLEQLGSPSTKLIFTVQDKFANIEEAELTVTAR 193
Cdd:cd23993   81 IFHSSRSIMCLyRSDLMSMQETEVQSGLSRLGVYEEEQLNTVEIEDKYSEESSYPTTSVFLEIESAQIQLYIHPLGIKAR 160


                 .
gi 268557650 194 F 194
Cdd:cd23993  161 F 161
 
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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