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Conserved domains on  [gi|442625572|ref|NP_001259965|]
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synaptotagmin 1, isoform F [Drosophila melanogaster]

Protein Classification

Syt1_2_N superfamily-containing protein( domain architecture ID 1770927)

Syt1_2_N superfamily-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Syt1_2_N super family cl41733
N-terminal domain of synaptotagmin-1 and -2; The synaptotagmins are integral membrane proteins ...
 62-161 8.75e-06

N-terminal domain of synaptotagmin-1 and -2; The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin-1 participates in triggering neurotransmitter release at the synapse. In general, synaptotagmins contain 2 calcium binding C2 domains. Synaptotagmin-1 and -2 have an additional N-terminal domain that has been shown to bind to Botulinum neurotoxin B.


The actual alignment was detected with superfamily member cd21963:

Pssm-ID: 425364  Cd Length: 108  Bit Score: 42.56  E-value: 8.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625572  62 SQRIAQVESTTRSATTEAQESTTTAVPVIKKIEHVGEVVTEVIAE--RTGLPTWGVVAIIILVFLVVFGIIF-FCVRRFL 138
Cdd:cd21963    1 HHEALAAPPVTTVAAVLPGNATEAAGPGGGKEDAFSKLKDKFMNElhKIPLPPWALIAIAIVAVLLILTCCFcICKKCLF 80

                         90       100
                 ....*....|....*....|....*.
gi 442625572 139 KKRRTKDGK---GKKGVDMKSVQLLG 161
Cdd:cd21963   81 KKKNKKKGKekgGKNAINMKDVKDLG 106
 
Name Accession Description Interval E-value
Syt1_N cd21963
N-terminal domain of synaptotagmin-1 (Syt1) and similar proteins; Syt1, also called ...
 62-161 8.75e-06

N-terminal domain of synaptotagmin-1 (Syt1) and similar proteins; Syt1, also called synaptotagmin I (SytI), or p65, is a calcium sensor that participates in triggering neurotransmitter release at the synapse. It may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. Syt1 binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. Syt1 also plays a role in dendrite formation by melanocytes. The model corresponds to N-terminal domain of Syt1, which is a recognition domain responsible for the binding of botulinum neurotoxin B (BoNT B).


Pssm-ID: 409248  Cd Length: 108  Bit Score: 42.56  E-value: 8.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625572  62 SQRIAQVESTTRSATTEAQESTTTAVPVIKKIEHVGEVVTEVIAE--RTGLPTWGVVAIIILVFLVVFGIIF-FCVRRFL 138
Cdd:cd21963    1 HHEALAAPPVTTVAAVLPGNATEAAGPGGGKEDAFSKLKDKFMNElhKIPLPPWALIAIAIVAVLLILTCCFcICKKCLF 80

                         90       100
                 ....*....|....*....|....*.
gi 442625572 139 KKRRTKDGK---GKKGVDMKSVQLLG 161
Cdd:cd21963   81 KKKNKKKGKekgGKNAINMKDVKDLG 106
Podoplanin pfam05808
Podoplanin; This family consists of several mammalian podoplanin like proteins which are ...
 69-136 4.78e-04

Podoplanin; This family consists of several mammalian podoplanin like proteins which are thought to control specifically the unique shape of podocytes.


Pssm-ID: 461746  Cd Length: 135  Bit Score: 38.25  E-value: 4.78e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442625572   69 ESTTRsATTEAQESTTTAVPVIKKIEHVGEVvTEVIAERTGLPTWGVVAIIILVFL---VVFGIIFFCVRR 136
Cdd:pfam05808  61 ESTVH-AHEESQSTTTPNVATSHSREKVGEE-TQTTVEKDGLATVTLVGIIVGVLLaigFIGGIIIVVVRK 129
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
113-147 1.65e-03

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 37.50  E-value: 1.65e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 442625572 113 WGVVAIIILVFLVVFGIIFFCVRRFLKKRRTKDGK 147
Cdd:COG1622   37 WVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPA 71
SA1362_fam NF041554
SA1362 family protein; Members of this family include SA1362 from Staphylococcus aureus. The ...
 120-152 4.68e-03

SA1362 family protein; Members of this family include SA1362 from Staphylococcus aureus. The N-terminal 50 amino acids are highly hydrophobic and suggest two transmembrane alpha-helical regions. The C-terminal region rich in basic residues, variable in length, and often somewhat repetitive. The family is widespread in Gram-positive species.


Pssm-ID: 469439  Cd Length: 70  Bit Score: 34.34  E-value: 4.68e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 442625572 120 ILVFLVVFGIIFFCVRRFLKKRRTK--DGKGKKGV 152
Cdd:NF041554  31 ILIIAVIGAIIYFIYYFFFLRRRGGgeQKKYKKAV 65
 
Name Accession Description Interval E-value
Syt1_N cd21963
N-terminal domain of synaptotagmin-1 (Syt1) and similar proteins; Syt1, also called ...
 62-161 8.75e-06

N-terminal domain of synaptotagmin-1 (Syt1) and similar proteins; Syt1, also called synaptotagmin I (SytI), or p65, is a calcium sensor that participates in triggering neurotransmitter release at the synapse. It may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. Syt1 binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. Syt1 also plays a role in dendrite formation by melanocytes. The model corresponds to N-terminal domain of Syt1, which is a recognition domain responsible for the binding of botulinum neurotoxin B (BoNT B).


Pssm-ID: 409248  Cd Length: 108  Bit Score: 42.56  E-value: 8.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625572  62 SQRIAQVESTTRSATTEAQESTTTAVPVIKKIEHVGEVVTEVIAE--RTGLPTWGVVAIIILVFLVVFGIIF-FCVRRFL 138
Cdd:cd21963    1 HHEALAAPPVTTVAAVLPGNATEAAGPGGGKEDAFSKLKDKFMNElhKIPLPPWALIAIAIVAVLLILTCCFcICKKCLF 80

                         90       100
                 ....*....|....*....|....*.
gi 442625572 139 KKRRTKDGK---GKKGVDMKSVQLLG 161
Cdd:cd21963   81 KKKNKKKGKekgGKNAINMKDVKDLG 106
Syt1_2_N cd21342
N-terminal domain of synaptotagmin-1 and -2; The synaptotagmins are integral membrane proteins ...
 110-158 1.83e-05

N-terminal domain of synaptotagmin-1 and -2; The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin-1 participates in triggering neurotransmitter release at the synapse. In general, synaptotagmins contain 2 calcium binding C2 domains. Synaptotagmin-1 and -2 have an additional N-terminal domain that has been shown to bind to Botulinum neurotoxin B.


Pssm-ID: 409247  Cd Length: 93  Bit Score: 41.26  E-value: 1.83e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442625572 110 LPTWGVVAIIILVFLVVFGIIFFCVRRFL---KKRRTKDGKGKKGVDMKSVQ 158
Cdd:cd21342   41 LPPWALAAIAIVAGLLLLSCCFCICKKCCfkkKKKKEGKKKGKAQINMKSVK 92
Podoplanin pfam05808
Podoplanin; This family consists of several mammalian podoplanin like proteins which are ...
 69-136 4.78e-04

Podoplanin; This family consists of several mammalian podoplanin like proteins which are thought to control specifically the unique shape of podocytes.


Pssm-ID: 461746  Cd Length: 135  Bit Score: 38.25  E-value: 4.78e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442625572   69 ESTTRsATTEAQESTTTAVPVIKKIEHVGEVvTEVIAERTGLPTWGVVAIIILVFL---VVFGIIFFCVRR 136
Cdd:pfam05808  61 ESTVH-AHEESQSTTTPNVATSHSREKVGEE-TQTTVEKDGLATVTLVGIIVGVLLaigFIGGIIIVVVRK 129
FeoB_associated pfam12669
FeoB-associated Cys-rich membrane protein; Members of this family typically are small proteins ...
 120-148 1.01e-03

FeoB-associated Cys-rich membrane protein; Members of this family typically are small proteins encoded next to FeoB, part of a ferrous iron uptake system. They consist of a highly hydrophobic predicted membrane segment, followed by a short, Cys-rich region, for an average length of less than sixty amino acids. In some cases, member proteins are fusion proteins, with the region described by this family occurring as a C-terminal extension to FeoB.


Pssm-ID: 463663  Cd Length: 45  Bit Score: 35.34  E-value: 1.01e-03
                          10        20
                  ....*....|....*....|....*....
gi 442625572  120 ILVFLVVFGIIFFCVRRFLKKRrtKDGKG 148
Cdd:pfam12669   3 IIVGAILLAIVALIIRRMVKDK--KKGKS 29
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
113-147 1.65e-03

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 37.50  E-value: 1.65e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 442625572 113 WGVVAIIILVFLVVFGIIFFCVRRFLKKRRTKDGK 147
Cdd:COG1622   37 WVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPA 71
SA1362_fam NF041554
SA1362 family protein; Members of this family include SA1362 from Staphylococcus aureus. The ...
 120-152 4.68e-03

SA1362 family protein; Members of this family include SA1362 from Staphylococcus aureus. The N-terminal 50 amino acids are highly hydrophobic and suggest two transmembrane alpha-helical regions. The C-terminal region rich in basic residues, variable in length, and often somewhat repetitive. The family is widespread in Gram-positive species.


Pssm-ID: 469439  Cd Length: 70  Bit Score: 34.34  E-value: 4.68e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 442625572 120 ILVFLVVFGIIFFCVRRFLKKRRTK--DGKGKKGV 152
Cdd:NF041554  31 ILIIAVIGAIIYFIYYFFFLRRRGGgeQKKYKKAV 65
 
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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