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Conserved domains on  [gi|170287745|ref|NP_061212|]
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BET1-like protein [Mus musculus]

Protein Classification

SNARE domain- containing protein( domain architecture ID 10205159)

SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) domain-containing protein such as Bet1, which forms complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B (R-SNARE) or GS28 (Qb), syntaxin-5 (Qa) and Ykt6 (R-SNARE); these complexes regulate the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) and from ERGIC to the cis-Golgi, respectively.

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SNARE_Bet1 cd15853
SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B ...
18-76 7.77e-18

SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B (R-SNARE) or GS28 (Qb), syntaxin-5 (Qa) and Ykt6 (R-SNARE). These complexes regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) and from ERGIC to the cis-Golgi, respectively. Bet1 is a member of the Qc subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


:

Pssm-ID: 277206  Cd Length: 59  Bit Score: 70.99  E-value: 7.77e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 170287745  18 DRENKRMADSLASKVTRLKSLALDIDRDTEDQNRYLDGMDSDFTSVTGLLTGSVKRFST 76
Cdd:cd15853    1 ESQNDRRLDELSSKVSALKSLTIDIGDEVRDQNKLLDGMGDDFDSTGGLLGGTMKRLKR 59
 
Name Accession Description Interval E-value
SNARE_Bet1 cd15853
SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B ...
18-76 7.77e-18

SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B (R-SNARE) or GS28 (Qb), syntaxin-5 (Qa) and Ykt6 (R-SNARE). These complexes regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) and from ERGIC to the cis-Golgi, respectively. Bet1 is a member of the Qc subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277206  Cd Length: 59  Bit Score: 70.99  E-value: 7.77e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 170287745  18 DRENKRMADSLASKVTRLKSLALDIDRDTEDQNRYLDGMDSDFTSVTGLLTGSVKRFST 76
Cdd:cd15853    1 ESQNDRRLDELSSKVSALKSLTIDIGDEVRDQNKLLDGMGDDFDSTGGLLGGTMKRLKR 59
 
Name Accession Description Interval E-value
SNARE_Bet1 cd15853
SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B ...
18-76 7.77e-18

SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B (R-SNARE) or GS28 (Qb), syntaxin-5 (Qa) and Ykt6 (R-SNARE). These complexes regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) and from ERGIC to the cis-Golgi, respectively. Bet1 is a member of the Qc subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277206  Cd Length: 59  Bit Score: 70.99  E-value: 7.77e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 170287745  18 DRENKRMADSLASKVTRLKSLALDIDRDTEDQNRYLDGMDSDFTSVTGLLTGSVKRFST 76
Cdd:cd15853    1 ESQNDRRLDELSSKVSALKSLTIDIGDEVRDQNKLLDGMGDDFDSTGGLLGGTMKRLKR 59
SNARE_Qc cd15841
SNARE motif, subgroup Qc; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
26-75 2.66e-04

SNARE motif, subgroup Qc; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qc SNAREs are C-terminal domains of SNAP23 and SNAP25, syntaxin 8, syntaxin 6, and Bet1.


Pssm-ID: 277194 [Multi-domain]  Cd Length: 59  Bit Score: 36.38  E-value: 2.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 170287745  26 DSLASKVTRLKSLALDIDRDTEDQNRYLDGMDSDFTSVTGLLTGSVKRFS 75
Cdd:cd15841    9 DELSGSVGRLKNIALAINEELDLQNRLLDDLDEDVDKTQSRLKKVNKKLK 58
SNARE_SYN8 cd15859
SNARE motif of SYN8; Fungal SYN8 is a member of the Qc subfamily of SNARE (soluble ...
26-84 5.01e-04

SNARE motif of SYN8; Fungal SYN8 is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family presetn in the endosomes. SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.


Pssm-ID: 277212  Cd Length: 68  Bit Score: 35.59  E-value: 5.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 170287745  26 DSLASKVTRLKSLALDIDRDTEDQNRYLDGMDSDFTSVTGLLTGSVKRFSTMARSGRDN 84
Cdd:cd15859    9 DHLSASIRRQHELSLQINDELDEQNELLDDLENGVDRTGRRLNRARRRLDKFRRKAREN 67
 
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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