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Conserved domains on  [gi|153946405|ref|NP_053583|]
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vesicle transport protein SEC20 isoform BNIP1-c [Homo sapiens]

Protein Classification

SNARE domain-containing protein; syntaxin family protein( domain architecture ID 10205212)

SNARE domain-containing protein such as SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which interact to form a SNARE complex that mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation; syntaxin family protein similar to syntaxin 5 (Syn5) that regulates the transport from the ER to the Golgi, as well as the early/recycling endosomes to the trans-Golgi network and participates in the assembly of transitional ER and the Golgi, lipid droplet fusion, and cytokinesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SNARE_SEC20 cd15865
SNARE motif of SEC20; SEC20 (also known as BNIP1, NIP1, or TRG-8) forms a complex with ...
 141-233 4.83e-36

SNARE motif of SEC20; SEC20 (also known as BNIP1, NIP1, or TRG-8) forms a complex with syntaxin 18 (Qa), SEC22 (R-SNARE)and USE1 (Qc), and is involved in the transport from cis-Golgi to the endoplasmic reticulum (ER). SEC20 is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that 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). 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. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.


:

Pssm-ID: 277218  Cd Length: 93  Bit Score: 122.73  E-value: 4.83e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946405 141 AQTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITKYNRRELTDKLLIFLALAL 220
Cdd:cd15865    1 AKTSSQITENLLRISRMLASQVQQSELTLQELASSSNTVTETHEEFKNMSGVIQTSAKLLTKYNRRELTDKLLIFLALLF 80

                         90
                 ....*....|...
gi 153946405 221 FLATVLYIVKKRL 233
Cdd:cd15865   81 FLATVLYVLKKRL 93
 
Name Accession Description Interval E-value
SNARE_SEC20 cd15865
SNARE motif of SEC20; SEC20 (also known as BNIP1, NIP1, or TRG-8) forms a complex with ...
 141-233 4.83e-36

SNARE motif of SEC20; SEC20 (also known as BNIP1, NIP1, or TRG-8) forms a complex with syntaxin 18 (Qa), SEC22 (R-SNARE)and USE1 (Qc), and is involved in the transport from cis-Golgi to the endoplasmic reticulum (ER). SEC20 is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that 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). 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. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.


Pssm-ID: 277218  Cd Length: 93  Bit Score: 122.73  E-value: 4.83e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946405 141 AQTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITKYNRRELTDKLLIFLALAL 220
Cdd:cd15865    1 AKTSSQITENLLRISRMLASQVQQSELTLQELASSSNTVTETHEEFKNMSGVIQTSAKLLTKYNRRELTDKLLIFLALLF 80

                         90
                 ....*....|...
gi 153946405 221 FLATVLYIVKKRL 233
Cdd:cd15865   81 FLATVLYVLKKRL 93
Sec20 pfam03908
Sec20; Sec20 is a membrane glycoprotein associated with secretory pathway.
 142-233 4.13e-27

Sec20; Sec20 is a membrane glycoprotein associated with secretory pathway.


Pssm-ID: 112708  Cd Length: 92  Bit Score: 99.80  E-value: 4.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946405  142 QTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITKYNRRELTDKLLIFLALALF 221
Cdd:pfam03908   1 SQAKQITESLRRISQLLVQGVLQSALNLDELVASTNSLEKANEEYKQFEGVLSRSRKLVKKLERRDHTDKRLVYLSFGFF 80

                          90
                  ....*....|..
gi 153946405  222 LATVLYIVKKRL 233
Cdd:pfam03908  81 LACVSYVVWKRI 92
 
Name Accession Description Interval E-value
SNARE_SEC20 cd15865
SNARE motif of SEC20; SEC20 (also known as BNIP1, NIP1, or TRG-8) forms a complex with ...
 141-233 4.83e-36

SNARE motif of SEC20; SEC20 (also known as BNIP1, NIP1, or TRG-8) forms a complex with syntaxin 18 (Qa), SEC22 (R-SNARE)and USE1 (Qc), and is involved in the transport from cis-Golgi to the endoplasmic reticulum (ER). SEC20 is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that 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). 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. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.


Pssm-ID: 277218  Cd Length: 93  Bit Score: 122.73  E-value: 4.83e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946405 141 AQTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITKYNRRELTDKLLIFLALAL 220
Cdd:cd15865    1 AKTSSQITENLLRISRMLASQVQQSELTLQELASSSNTVTETHEEFKNMSGVIQTSAKLLTKYNRRELTDKLLIFLALLF 80

                         90
                 ....*....|...
gi 153946405 221 FLATVLYIVKKRL 233
Cdd:cd15865   81 FLATVLYVLKKRL 93
Sec20 pfam03908
Sec20; Sec20 is a membrane glycoprotein associated with secretory pathway.
 142-233 4.13e-27

Sec20; Sec20 is a membrane glycoprotein associated with secretory pathway.


Pssm-ID: 112708  Cd Length: 92  Bit Score: 99.80  E-value: 4.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946405  142 QTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITKYNRRELTDKLLIFLALALF 221
Cdd:pfam03908   1 SQAKQITESLRRISQLLVQGVLQSALNLDELVASTNSLEKANEEYKQFEGVLSRSRKLVKKLERRDHTDKRLVYLSFGFF 80

                          90
                  ....*....|..
gi 153946405  222 LATVLYIVKKRL 233
Cdd:pfam03908  81 LACVSYVVWKRI 92
SNARE_Qb cd15842
SNARE motif, subgroup Qb; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
 141-202 3.68e-15

SNARE motif, subgroup Qb; 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). 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. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.


Pssm-ID: 277195  Cd Length: 62  Bit Score: 67.51  E-value: 3.68e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153946405 141 AQTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITK 202
Cdd:cd15842    1 DQLSDQSTESLRRSHRGMEELKQAGIETLEMLDEQREQLERTEERINSINGDIKLSRKILRK 62
 
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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