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Conserved domains on  [gi|25282425|ref|NP_742008|]
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protein phosphatase 1 regulatory subunit 14D [Rattus norvegicus]

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 ...
 53-140 5.67e-21

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: 82.63  E-value: 5.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282425    53 RRPSRLTVKYDRGHLQRWLEMEQWVDAQVQELFQGQADTSEPEIDLEALMELSTDEQRTQ-LEAILQDCPGNREPFISEL 131
Cdd:pfam05361  29 KRQARVTVKYDRKELQKRLDVEKWIDERLEELYLGREDEMPDEVNIDELLDLESDEERSQkLQDLLKSCTNNTEAFITEL 108


                  ....*....
gi 25282425   132 LSQLKRLRR 140
Cdd:pfam05361 109 LQKLHGLQK 117
 
Name Accession Description Interval E-value
PP1_inhibitor pfam05361
PKC-activated protein phosphatase-1 inhibitor; Contractility of vascular smooth muscle depends ...
 53-140 5.67e-21

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: 82.63  E-value: 5.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282425    53 RRPSRLTVKYDRGHLQRWLEMEQWVDAQVQELFQGQADTSEPEIDLEALMELSTDEQRTQ-LEAILQDCPGNREPFISEL 131
Cdd:pfam05361  29 KRQARVTVKYDRKELQKRLDVEKWIDERLEELYLGREDEMPDEVNIDELLDLESDEERSQkLQDLLKSCTNNTEAFITEL 108


                  ....*....
gi 25282425   132 LSQLKRLRR 140
Cdd:pfam05361 109 LQKLHGLQK 117
 
Name Accession Description Interval E-value
PP1_inhibitor pfam05361
PKC-activated protein phosphatase-1 inhibitor; Contractility of vascular smooth muscle depends ...
 53-140 5.67e-21

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: 82.63  E-value: 5.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282425    53 RRPSRLTVKYDRGHLQRWLEMEQWVDAQVQELFQGQADTSEPEIDLEALMELSTDEQRTQ-LEAILQDCPGNREPFISEL 131
Cdd:pfam05361  29 KRQARVTVKYDRKELQKRLDVEKWIDERLEELYLGREDEMPDEVNIDELLDLESDEERSQkLQDLLKSCTNNTEAFITEL 108


                  ....*....
gi 25282425   132 LSQLKRLRR 140
Cdd:pfam05361 109 LQKLHGLQK 117
 
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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