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Conserved domains on  [gi|153946401|ref|NP_001196|]
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vesicle transport protein SEC20 isoform BNIP1 [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 ...
 132-224 1.23e-35

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: 121.57  E-value: 1.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946401 132 AQTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITKYNRRELTDKLLIFLALAL 211
Cdd:cd15865    1 AKTSSQITENLLRISRMLASQVQQSELTLQELASSSNTVTETHEEFKNMSGVIQTSAKLLTKYNRRELTDKLLIFLALLF 80

                         90
                 ....*....|...
gi 153946401 212 FLATVLYIVKKRL 224
Cdd:cd15865   81 FLATVLYVLKKRL 93
DUF3498 super family cl26404
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 46-175 8.06e-03

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


The actual alignment was detected with superfamily member pfam12004:

Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 37.05  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946401   46 KVKEKFQQLRHRIQDLEQLAKEQDKESEKQLLLQEvENHKKQMLSNQAswrkanltckiaidNLEKAEllqggDLLRQRK 125
Cdd:pfam12004 385 KQAEKYEQEISKLKERLRVSNRKLEEYERRLLAQE-EQTQKLLLEYQA--------------RLEDSE-----ERLRRQQ 444

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 153946401  126 TTKESlaQTSSTIteslmgiSRMMA--QQVQQSEEAMQSLVTSSRTILDANE 175
Cdd:pfam12004 445 EEKDS--QMKSII-------SRLMAveEELKKDHAEMQAVIDSKQKIIDAQE 487
 
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 ...
 132-224 1.23e-35

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: 121.57  E-value: 1.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946401 132 AQTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITKYNRRELTDKLLIFLALAL 211
Cdd:cd15865    1 AKTSSQITENLLRISRMLASQVQQSELTLQELASSSNTVTETHEEFKNMSGVIQTSAKLLTKYNRRELTDKLLIFLALLF 80

                         90
                 ....*....|...
gi 153946401 212 FLATVLYIVKKRL 224
Cdd:cd15865   81 FLATVLYVLKKRL 93
Sec20 pfam03908
Sec20; Sec20 is a membrane glycoprotein associated with secretory pathway.
 133-224 1.09e-26

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


Pssm-ID: 112708  Cd Length: 92  Bit Score: 98.26  E-value: 1.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946401  133 QTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITKYNRRELTDKLLIFLALALF 212
Cdd:pfam03908   1 SQAKQITESLRRISQLLVQGVLQSALNLDELVASTNSLEKANEEYKQFEGVLSRSRKLVKKLERRDHTDKRLVYLSFGFF 80

                          90
                  ....*....|..
gi 153946401  213 LATVLYIVKKRL 224
Cdd:pfam03908  81 LACVSYVVWKRI 92
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 46-175 8.06e-03

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 37.05  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946401   46 KVKEKFQQLRHRIQDLEQLAKEQDKESEKQLLLQEvENHKKQMLSNQAswrkanltckiaidNLEKAEllqggDLLRQRK 125
Cdd:pfam12004 385 KQAEKYEQEISKLKERLRVSNRKLEEYERRLLAQE-EQTQKLLLEYQA--------------RLEDSE-----ERLRRQQ 444

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 153946401  126 TTKESlaQTSSTIteslmgiSRMMA--QQVQQSEEAMQSLVTSSRTILDANE 175
Cdd:pfam12004 445 EEKDS--QMKSII-------SRLMAveEELKKDHAEMQAVIDSKQKIIDAQE 487
 
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 ...
 132-224 1.23e-35

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: 121.57  E-value: 1.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946401 132 AQTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITKYNRRELTDKLLIFLALAL 211
Cdd:cd15865    1 AKTSSQITENLLRISRMLASQVQQSELTLQELASSSNTVTETHEEFKNMSGVIQTSAKLLTKYNRRELTDKLLIFLALLF 80

                         90
                 ....*....|...
gi 153946401 212 FLATVLYIVKKRL 224
Cdd:cd15865   81 FLATVLYVLKKRL 93
Sec20 pfam03908
Sec20; Sec20 is a membrane glycoprotein associated with secretory pathway.
 133-224 1.09e-26

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


Pssm-ID: 112708  Cd Length: 92  Bit Score: 98.26  E-value: 1.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946401  133 QTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITKYNRRELTDKLLIFLALALF 212
Cdd:pfam03908   1 SQAKQITESLRRISQLLVQGVLQSALNLDELVASTNSLEKANEEYKQFEGVLSRSRKLVKKLERRDHTDKRLVYLSFGFF 80

                          90
                  ....*....|..
gi 153946401  213 LATVLYIVKKRL 224
Cdd:pfam03908  81 LACVSYVVWKRI 92
SNARE_Qb cd15842
SNARE motif, subgroup Qb; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
 132-193 2.77e-13

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: 62.51  E-value: 2.77e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153946401 132 AQTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITK 193
Cdd:cd15842    1 DQLSDQSTESLRRSHRGMEELKQAGIETLEMLDEQREQLERTEERINSINGDIKLSRKILRK 62
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 46-175 8.06e-03

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 37.05  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153946401   46 KVKEKFQQLRHRIQDLEQLAKEQDKESEKQLLLQEvENHKKQMLSNQAswrkanltckiaidNLEKAEllqggDLLRQRK 125
Cdd:pfam12004 385 KQAEKYEQEISKLKERLRVSNRKLEEYERRLLAQE-EQTQKLLLEYQA--------------RLEDSE-----ERLRRQQ 444

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 153946401  126 TTKESlaQTSSTIteslmgiSRMMA--QQVQQSEEAMQSLVTSSRTILDANE 175
Cdd:pfam12004 445 EEKDS--QMKSII-------SRLMAveEELKKDHAEMQAVIDSKQKIIDAQE 487
 
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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