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Conserved domains on  [gi|62122946|ref|NP_032915|]
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protein phosphatase 1 regulatory subunit 14B [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PP1_inhibitor super family cl05100
PKC-activated protein phosphatase-1 inhibitor; Contractility of vascular smooth muscle depends ...
 51-147 1.36e-30

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.


The actual alignment was detected with superfamily member pfam05361:

Pssm-ID: 461630  Cd Length: 141  Bit Score: 107.28  E-value: 1.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62122946    51 RRQGKVTVKYDRKELRKRLNLEEWILEQLTRLYDCQEEEIPElEIDVDELLDMESDDTRAARVKELLVDCYKPTEAFISG 130
Cdd:pfam05361  29 KRQARVTVKYDRKELQKRLDVEKWIDERLEELYLGREDEMPD-EVNIDELLDLESDEERSQKLQDLLKSCTNNTEAFITE 107

                          90
                  ....*....|....*..
gi 62122946   131 LLDKIRGMQKLSTPQKK 147
Cdd:pfam05361 108 LLQKLHGLQKQEELQNN 124
 
Name Accession Description Interval E-value
PP1_inhibitor pfam05361
PKC-activated protein phosphatase-1 inhibitor; Contractility of vascular smooth muscle depends ...
 51-147 1.36e-30

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: 107.28  E-value: 1.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62122946    51 RRQGKVTVKYDRKELRKRLNLEEWILEQLTRLYDCQEEEIPElEIDVDELLDMESDDTRAARVKELLVDCYKPTEAFISG 130
Cdd:pfam05361  29 KRQARVTVKYDRKELQKRLDVEKWIDERLEELYLGREDEMPD-EVNIDELLDLESDEERSQKLQDLLKSCTNNTEAFITE 107

                          90
                  ....*....|....*..
gi 62122946   131 LLDKIRGMQKLSTPQKK 147
Cdd:pfam05361 108 LLQKLHGLQKQEELQNN 124
 
Name Accession Description Interval E-value
PP1_inhibitor pfam05361
PKC-activated protein phosphatase-1 inhibitor; Contractility of vascular smooth muscle depends ...
 51-147 1.36e-30

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: 107.28  E-value: 1.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62122946    51 RRQGKVTVKYDRKELRKRLNLEEWILEQLTRLYDCQEEEIPElEIDVDELLDMESDDTRAARVKELLVDCYKPTEAFISG 130
Cdd:pfam05361  29 KRQARVTVKYDRKELQKRLDVEKWIDERLEELYLGREDEMPD-EVNIDELLDLESDEERSQKLQDLLKSCTNNTEAFITE 107

                          90
                  ....*....|....*..
gi 62122946   131 LLDKIRGMQKLSTPQKK 147
Cdd:pfam05361 108 LLQKLHGLQKQEELQNN 124
 
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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