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Conserved domains on  [gi|1952707055|ref|XP_038311272|]
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junctional sarcoplasmic reticulum protein 1 isoform X1 [Canis lupus familiaris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
JSRP super family cl21157
Junctional sarcoplasmic reticulum protein; JSRP, junctional sarcoplasmic reticulum protein 1, ...
 207-268 3.22e-08

Junctional sarcoplasmic reticulum protein; JSRP, junctional sarcoplasmic reticulum protein 1, or junctional-face membrane protein of 45 kDa homolog, is a family of eukaryotic proteins. The family is to the junctional face membrane of the skeletal muscle sarcoplasmic reticulum (SR); it colocalizes with its Ca2+-release channel (the ryanodine receptor), and interacts with calsequestrin and the skeletal-muscle dihydro-pyridine receptor Cav1. It is key for the functional expression of voltage-dependent Ca2+ channels.


The actual alignment was detected with superfamily member pfam15312:

Pssm-ID: 464637  Cd Length: 63  Bit Score: 49.75  E-value: 3.22e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952707055 207 DELPWGDLSLNKCLVLASLVALLGSAFQLCRDAVAGDAAAPAPVPEPWVPRSSAPERASPPP 268
Cdd:pfam15312   1 EELPWGDVTLNKCLVLASLVALLGSAFQLCHDAVRGERAAPAPAPEPWRPPSSLRKGPASPL 62
 
Name Accession Description Interval E-value
JSRP pfam15312
Junctional sarcoplasmic reticulum protein; JSRP, junctional sarcoplasmic reticulum protein 1, ...
 207-268 3.22e-08

Junctional sarcoplasmic reticulum protein; JSRP, junctional sarcoplasmic reticulum protein 1, or junctional-face membrane protein of 45 kDa homolog, is a family of eukaryotic proteins. The family is to the junctional face membrane of the skeletal muscle sarcoplasmic reticulum (SR); it colocalizes with its Ca2+-release channel (the ryanodine receptor), and interacts with calsequestrin and the skeletal-muscle dihydro-pyridine receptor Cav1. It is key for the functional expression of voltage-dependent Ca2+ channels.


Pssm-ID: 464637  Cd Length: 63  Bit Score: 49.75  E-value: 3.22e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952707055 207 DELPWGDLSLNKCLVLASLVALLGSAFQLCRDAVAGDAAAPAPVPEPWVPRSSAPERASPPP 268
Cdd:pfam15312   1 EELPWGDVTLNKCLVLASLVALLGSAFQLCHDAVRGERAAPAPAPEPWRPPSSLRKGPASPL 62
 
Name Accession Description Interval E-value
JSRP pfam15312
Junctional sarcoplasmic reticulum protein; JSRP, junctional sarcoplasmic reticulum protein 1, ...
 207-268 3.22e-08

Junctional sarcoplasmic reticulum protein; JSRP, junctional sarcoplasmic reticulum protein 1, or junctional-face membrane protein of 45 kDa homolog, is a family of eukaryotic proteins. The family is to the junctional face membrane of the skeletal muscle sarcoplasmic reticulum (SR); it colocalizes with its Ca2+-release channel (the ryanodine receptor), and interacts with calsequestrin and the skeletal-muscle dihydro-pyridine receptor Cav1. It is key for the functional expression of voltage-dependent Ca2+ channels.


Pssm-ID: 464637  Cd Length: 63  Bit Score: 49.75  E-value: 3.22e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952707055 207 DELPWGDLSLNKCLVLASLVALLGSAFQLCRDAVAGDAAAPAPVPEPWVPRSSAPERASPPP 268
Cdd:pfam15312   1 EELPWGDVTLNKCLVLASLVALLGSAFQLCHDAVRGERAAPAPAPEPWRPPSSLRKGPASPL 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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