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Conserved domains on  [gi|543855|sp|P36576|]
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RecName: Full=Arrestin-C; AltName: Full=Cone arrestin; Short=cArr; AltName: Full=Retinal cone arrestin-3

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Arrestin_C super family cl47063
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 1-64 3.25e-05

Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain. Arrestins comprise a family of closely-related proteins that includes beta-arrestin-1 and -2, which regulate the function of beta-adrenergic receptors by binding to their phosphorylated forms, impairing their capacity to activate G(S) proteins; Cone photoreceptors C-arrestin (arrestin-X). which could bind to phosphorylated red/green opsins; and Drosophila phosrestins I and II, which undergo light-induced phosphorylation, and probably play a role in photoreceptor transduction.


The actual alignment was detected with superfamily member smart01017:

Pssm-ID: 214976 [Multi-domain]  Cd Length: 142  Bit Score: 39.63  E-value: 3.25e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543855        1 LKHEDTNLASSTILrpgmnkellGILVSYKVKVNLMVSYGgilgglpASDVGVELPLILIHPKP 64
Cdd:smart01017  95 LKVPPLPPTSRTCR---------LIKVEYKLKVKLRLSGK-------HSELRLELPITIGTVPL 142
 
Name Accession Description Interval E-value
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 1-64 3.25e-05

Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain. Arrestins comprise a family of closely-related proteins that includes beta-arrestin-1 and -2, which regulate the function of beta-adrenergic receptors by binding to their phosphorylated forms, impairing their capacity to activate G(S) proteins; Cone photoreceptors C-arrestin (arrestin-X). which could bind to phosphorylated red/green opsins; and Drosophila phosrestins I and II, which undergo light-induced phosphorylation, and probably play a role in photoreceptor transduction.


Pssm-ID: 214976 [Multi-domain]  Cd Length: 142  Bit Score: 39.63  E-value: 3.25e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543855        1 LKHEDTNLASSTILrpgmnkellGILVSYKVKVNLMVSYGgilgglpASDVGVELPLILIHPKP 64
Cdd:smart01017  95 LKVPPLPPTSRTCR---------LIKVEYKLKVKLRLSGK-------HSELRLELPITIGTVPL 142
 
Name Accession Description Interval E-value
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 1-64 3.25e-05

Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain. Arrestins comprise a family of closely-related proteins that includes beta-arrestin-1 and -2, which regulate the function of beta-adrenergic receptors by binding to their phosphorylated forms, impairing their capacity to activate G(S) proteins; Cone photoreceptors C-arrestin (arrestin-X). which could bind to phosphorylated red/green opsins; and Drosophila phosrestins I and II, which undergo light-induced phosphorylation, and probably play a role in photoreceptor transduction.


Pssm-ID: 214976 [Multi-domain]  Cd Length: 142  Bit Score: 39.63  E-value: 3.25e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543855        1 LKHEDTNLASSTILrpgmnkellGILVSYKVKVNLMVSYGgilgglpASDVGVELPLILIHPKP 64
Cdd:smart01017  95 LKVPPLPPTSRTCR---------LIKVEYKLKVKLRLSGK-------HSELRLELPITIGTVPL 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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