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Conserved domains on  [gi|984290526|ref|NP_001306119|]
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SLP adapter and CSK-interacting membrane protein isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCIMP super family cl20923
SCIMP protein; This family contains the SCIMP proteins which are a a transmembrane adaptor ...
 12-87 1.04e-51

SCIMP protein; This family contains the SCIMP proteins which are a a transmembrane adaptor protein involved in major histocompatibility complex class II signaling.


The actual alignment was detected with superfamily member pfam15050:

Pssm-ID: 434419  Cd Length: 132  Bit Score: 159.60  E-value: 1.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984290526   12 MSWWRNNFWIILAVAIIVVSVGLGLILYCVC-------KKWEIAKPLKHKQVDEEKMYENVLNESPVQLPPLPPRNWPSL 84
Cdd:pfam15050   1 MSWWRNNFWIILAVAIIVVSVVLGLILYCVCrwqlrqgKKWEIAKPLKQNQRDEEKMYENVINQSPVQLPPLPPRGLPSP 80


                  ...
gi 984290526   85 EDS 87
Cdd:pfam15050  81 EDS 83
 
Name Accession Description Interval E-value
SCIMP pfam15050
SCIMP protein; This family contains the SCIMP proteins which are a a transmembrane adaptor ...
 12-87 1.04e-51

SCIMP protein; This family contains the SCIMP proteins which are a a transmembrane adaptor protein involved in major histocompatibility complex class II signaling.


Pssm-ID: 434419  Cd Length: 132  Bit Score: 159.60  E-value: 1.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984290526   12 MSWWRNNFWIILAVAIIVVSVGLGLILYCVC-------KKWEIAKPLKHKQVDEEKMYENVLNESPVQLPPLPPRNWPSL 84
Cdd:pfam15050   1 MSWWRNNFWIILAVAIIVVSVVLGLILYCVCrwqlrqgKKWEIAKPLKQNQRDEEKMYENVINQSPVQLPPLPPRGLPSP 80


                  ...
gi 984290526   85 EDS 87
Cdd:pfam15050  81 EDS 83
Syt1_N cd21963
N-terminal domain of synaptotagmin-1 (Syt1) and similar proteins; Syt1, also called ...
 20-72 7.08e-04

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: 36.40  E-value: 7.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 984290526  20 WIILAVAIIVVSvglgLIL---YCVCKKWEIAKplKHKQVDEEKMYENVLNESPVQ 72
Cdd:cd21963   54 WALIAIAIVAVL----LILtccFCICKKCLFKK--KNKKKGKEKGGKNAINMKDVK 103
 
Name Accession Description Interval E-value
SCIMP pfam15050
SCIMP protein; This family contains the SCIMP proteins which are a a transmembrane adaptor ...
 12-87 1.04e-51

SCIMP protein; This family contains the SCIMP proteins which are a a transmembrane adaptor protein involved in major histocompatibility complex class II signaling.


Pssm-ID: 434419  Cd Length: 132  Bit Score: 159.60  E-value: 1.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984290526   12 MSWWRNNFWIILAVAIIVVSVGLGLILYCVC-------KKWEIAKPLKHKQVDEEKMYENVLNESPVQLPPLPPRNWPSL 84
Cdd:pfam15050   1 MSWWRNNFWIILAVAIIVVSVVLGLILYCVCrwqlrqgKKWEIAKPLKQNQRDEEKMYENVINQSPVQLPPLPPRGLPSP 80


                  ...
gi 984290526   85 EDS 87
Cdd:pfam15050  81 EDS 83
Syt1_N cd21963
N-terminal domain of synaptotagmin-1 (Syt1) and similar proteins; Syt1, also called ...
 20-72 7.08e-04

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: 36.40  E-value: 7.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 984290526  20 WIILAVAIIVVSvglgLIL---YCVCKKWEIAKplKHKQVDEEKMYENVLNESPVQ 72
Cdd:cd21963   54 WALIAIAIVAVL----LILtccFCICKKCLFKK--KNKKKGKEKGGKNAINMKDVK 103
 
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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