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Conserved domains on  [gi|41387132|ref|NP_957104|]
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protein phosphatase 1, regulatory (inhibitor) subunit 14Ab [Danio rerio]

Protein Classification

PP1_inhibitor domain-containing protein( domain architecture ID 10526602)

PP1_inhibitor domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PP1_inhibitor pfam05361
PKC-activated protein phosphatase-1 inhibitor; Contractility of vascular smooth muscle depends ...
 1-143 2.27e-85

PKC-activated protein phosphatase-1 inhibitor; Contractility of vascular smooth muscle depends on phosphorylation of myosin light chains, and is modulated by hormonal control of myosin phosphatase activity. Signaling pathways activate kinases such as PKC or Rho-dependent kinases that phosphorylate the myosin phosphatase inhibitor protein called CPI-17. Phosphorylation of CPI-17 at Thr-38 enhances its inhibitory potency 1000-fold, creating a molecular switch for regulating contraction.


:

Pssm-ID: 461630  Cd Length: 141  Bit Score: 245.95  E-value: 2.27e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387132     1 MAANRVGRRYNNKIHSPNRgaSREAGLSVQKRQARVTVKYNRKELQRRLDVEKWIDCGLDELYLGREDEMPEEVNIDELL 80
Cdd:pfam05361   1 MAANKVGKREENKEHSPSR--AREAGLSVQKRQARVTVKYDRKELQKRLDVEKWIDERLEELYLGREDEMPDEVNIDELL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41387132    81 DLQSDEERTQKLKDILHACSNNTEVFITELVKKLHGLQKQEDLHNNGIEHPQLHIFPERQGSS 143
Cdd:pfam05361  79 DLESDEERSQKLQDLLKSCTNNTEAFITELLQKLHGLQKQEELQNNGIEHPSLHSYPEHHGSH 141
 
Name Accession Description Interval E-value
PP1_inhibitor pfam05361
PKC-activated protein phosphatase-1 inhibitor; Contractility of vascular smooth muscle depends ...
 1-143 2.27e-85

PKC-activated protein phosphatase-1 inhibitor; Contractility of vascular smooth muscle depends on phosphorylation of myosin light chains, and is modulated by hormonal control of myosin phosphatase activity. Signaling pathways activate kinases such as PKC or Rho-dependent kinases that phosphorylate the myosin phosphatase inhibitor protein called CPI-17. Phosphorylation of CPI-17 at Thr-38 enhances its inhibitory potency 1000-fold, creating a molecular switch for regulating contraction.


Pssm-ID: 461630  Cd Length: 141  Bit Score: 245.95  E-value: 2.27e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387132     1 MAANRVGRRYNNKIHSPNRgaSREAGLSVQKRQARVTVKYNRKELQRRLDVEKWIDCGLDELYLGREDEMPEEVNIDELL 80
Cdd:pfam05361   1 MAANKVGKREENKEHSPSR--AREAGLSVQKRQARVTVKYDRKELQKRLDVEKWIDERLEELYLGREDEMPDEVNIDELL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41387132    81 DLQSDEERTQKLKDILHACSNNTEVFITELVKKLHGLQKQEDLHNNGIEHPQLHIFPERQGSS 143
Cdd:pfam05361  79 DLESDEERSQKLQDLLKSCTNNTEAFITELLQKLHGLQKQEELQNNGIEHPSLHSYPEHHGSH 141
 
Name Accession Description Interval E-value
PP1_inhibitor pfam05361
PKC-activated protein phosphatase-1 inhibitor; Contractility of vascular smooth muscle depends ...
 1-143 2.27e-85

PKC-activated protein phosphatase-1 inhibitor; Contractility of vascular smooth muscle depends on phosphorylation of myosin light chains, and is modulated by hormonal control of myosin phosphatase activity. Signaling pathways activate kinases such as PKC or Rho-dependent kinases that phosphorylate the myosin phosphatase inhibitor protein called CPI-17. Phosphorylation of CPI-17 at Thr-38 enhances its inhibitory potency 1000-fold, creating a molecular switch for regulating contraction.


Pssm-ID: 461630  Cd Length: 141  Bit Score: 245.95  E-value: 2.27e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387132     1 MAANRVGRRYNNKIHSPNRgaSREAGLSVQKRQARVTVKYNRKELQRRLDVEKWIDCGLDELYLGREDEMPEEVNIDELL 80
Cdd:pfam05361   1 MAANKVGKREENKEHSPSR--AREAGLSVQKRQARVTVKYDRKELQKRLDVEKWIDERLEELYLGREDEMPDEVNIDELL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41387132    81 DLQSDEERTQKLKDILHACSNNTEVFITELVKKLHGLQKQEDLHNNGIEHPQLHIFPERQGSS 143
Cdd:pfam05361  79 DLESDEERSQKLQDLLKSCTNNTEAFITELLQKLHGLQKQEELQNNGIEHPSLHSYPEHHGSH 141
 
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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