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Conserved domains on  [gi|62472365|ref|NP_001014602|]
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complexin, isoform K [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Synaphin super family cl05420
Synaphin protein; This family consists of several eukaryotic synaphin 1 and 2 proteins. ...
1-74 5.94e-09

Synaphin protein; This family consists of several eukaryotic synaphin 1 and 2 proteins. Synaphin/complexin is a cytosolic protein that preferentially binds to syntaxin within the SNARE complex. Synaphin promotes SNAREs to form precomplexes that oligomerise into higher order structures. A peptide from the central, syntaxin binding domain of synaphin competitively inhibits these two proteins from interacting and prevents SNARE complexes from oligomerising. It is thought that oligomerization of SNARE complexes into a higher order structure creates a SNARE scaffold for efficient, regulated fusion of synaptic vesicles. Synaphin promotes neuronal exocytosis by promoting interaction between the complementary syntaxin and synaptobrevin transmembrane regions that reside in opposing membranes prior to fusion.


The actual alignment was detected with superfamily member pfam05835:

Pssm-ID: 461755 [Multi-domain]  Cd Length: 142  Bit Score: 49.37  E-value: 5.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472365     1 MEEEREKMRQDIRDKYNIKKKEEIVE----AAPQEEPNPLMRKKKTPEELAAEAEQEELDD------FTKLKNQIETQVN 70
Cdd:pfam05835  59 MEAEREKMRQHIRDKYRLKKKEEDEAeiqaAMEPSTEGRLGRDKKTPEELAKMVEEDEEEEeekdsvLGKLQNTLNTDVD 138

                  ....
gi 62472365    71 ELKT 74
Cdd:pfam05835 139 ELKE 142
 
Name Accession Description Interval E-value
Synaphin pfam05835
Synaphin protein; This family consists of several eukaryotic synaphin 1 and 2 proteins. ...
1-74 5.94e-09

Synaphin protein; This family consists of several eukaryotic synaphin 1 and 2 proteins. Synaphin/complexin is a cytosolic protein that preferentially binds to syntaxin within the SNARE complex. Synaphin promotes SNAREs to form precomplexes that oligomerise into higher order structures. A peptide from the central, syntaxin binding domain of synaphin competitively inhibits these two proteins from interacting and prevents SNARE complexes from oligomerising. It is thought that oligomerization of SNARE complexes into a higher order structure creates a SNARE scaffold for efficient, regulated fusion of synaptic vesicles. Synaphin promotes neuronal exocytosis by promoting interaction between the complementary syntaxin and synaptobrevin transmembrane regions that reside in opposing membranes prior to fusion.


Pssm-ID: 461755 [Multi-domain]  Cd Length: 142  Bit Score: 49.37  E-value: 5.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472365     1 MEEEREKMRQDIRDKYNIKKKEEIVE----AAPQEEPNPLMRKKKTPEELAAEAEQEELDD------FTKLKNQIETQVN 70
Cdd:pfam05835  59 MEAEREKMRQHIRDKYRLKKKEEDEAeiqaAMEPSTEGRLGRDKKTPEELAKMVEEDEEEEeekdsvLGKLQNTLNTDVD 138

                  ....
gi 62472365    71 ELKT 74
Cdd:pfam05835 139 ELKE 142
 
Name Accession Description Interval E-value
Synaphin pfam05835
Synaphin protein; This family consists of several eukaryotic synaphin 1 and 2 proteins. ...
1-74 5.94e-09

Synaphin protein; This family consists of several eukaryotic synaphin 1 and 2 proteins. Synaphin/complexin is a cytosolic protein that preferentially binds to syntaxin within the SNARE complex. Synaphin promotes SNAREs to form precomplexes that oligomerise into higher order structures. A peptide from the central, syntaxin binding domain of synaphin competitively inhibits these two proteins from interacting and prevents SNARE complexes from oligomerising. It is thought that oligomerization of SNARE complexes into a higher order structure creates a SNARE scaffold for efficient, regulated fusion of synaptic vesicles. Synaphin promotes neuronal exocytosis by promoting interaction between the complementary syntaxin and synaptobrevin transmembrane regions that reside in opposing membranes prior to fusion.


Pssm-ID: 461755 [Multi-domain]  Cd Length: 142  Bit Score: 49.37  E-value: 5.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472365     1 MEEEREKMRQDIRDKYNIKKKEEIVE----AAPQEEPNPLMRKKKTPEELAAEAEQEELDD------FTKLKNQIETQVN 70
Cdd:pfam05835  59 MEAEREKMRQHIRDKYRLKKKEEDEAeiqaAMEPSTEGRLGRDKKTPEELAKMVEEDEEEEeekdsvLGKLQNTLNTDVD 138

                  ....
gi 62472365    71 ELKT 74
Cdd:pfam05835 139 ELKE 142
 
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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