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Conserved domains on  [gi|530788326|ref|NP_001269059|]
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protein phosphatase Slingshot homolog 2 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SSH-N super family cl17009
N-terminal domain conserved in slingshot (SSH) phosphatases; This domain or region conserved ...
 3-178 3.47e-97

N-terminal domain conserved in slingshot (SSH) phosphatases; This domain or region conserved in Bilateria is found N-terminal to the DEK_C-like and catalytic domains of slingshot phosphatases. Slingshot is a cofilin-specific phosphatase. Dephosphorylation reactivates cofilin, which in turn depolymerizes actin and is thus required for actin filament reorganization. Slingshot is a member of the dual-specificity protein phosphatase family. This N-terminal SSH region may be involved in P-cofilin binding (the model C-terminus plus the DEK_C-like domain, which are characterized as the "B" domain in some of the literature), and may be required for the F-actin mediated activation of slingshot (the N-terminal region of this model, sometimes referred to as the "A" domain).


The actual alignment was detected with superfamily member cd11652:

Pssm-ID: 212166  Cd Length: 233  Bit Score: 281.54  E-value: 3.47e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788326   3 LVTVQRSPTPSTTSSPCAS-EADSGEEECRSQPRSISESFLTVKGAALFLPRGNGSSTPRiSHRRNKHAGDLQQHLQAMF 81
Cdd:cd11652    1 LVTVQRSPTPSGNSNPDGSdDEEEGDEEQRRKRLQRSESFFAVKGAALILPQGDRTNRPR-EIASHKHAGELQQHLQAMF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788326  82 ILLRPEDNIRLAVRLESTYQNRTRYMVVVSTNGRQDTEESIVLGMDFSSNDSStCTMGLVLPLWSDTLIHLDGDGGFSVS 161
Cdd:cd11652   80 NLLRPEDTIKLAVRLESVRSNRTRYLVVVSTLGRQDTEESILLGVDFPPKESS-CTIGLVLPIWSDTQVHLDGDGGFSVT 158

                        170
                 ....*....|....*..
gi 530788326 162 TDNRVHIFKPVSVQAMW 178
Cdd:cd11652  159 SDGKTHIFKPVSVQAMW 175
 
Name Accession Description Interval E-value
SSH-N cd11652
N-terminal domain conserved in slingshot (SSH) phosphatases; This domain or region conserved ...
 3-178 3.47e-97

N-terminal domain conserved in slingshot (SSH) phosphatases; This domain or region conserved in Bilateria is found N-terminal to the DEK_C-like and catalytic domains of slingshot phosphatases. Slingshot is a cofilin-specific phosphatase. Dephosphorylation reactivates cofilin, which in turn depolymerizes actin and is thus required for actin filament reorganization. Slingshot is a member of the dual-specificity protein phosphatase family. This N-terminal SSH region may be involved in P-cofilin binding (the model C-terminus plus the DEK_C-like domain, which are characterized as the "B" domain in some of the literature), and may be required for the F-actin mediated activation of slingshot (the N-terminal region of this model, sometimes referred to as the "A" domain).


Pssm-ID: 212166  Cd Length: 233  Bit Score: 281.54  E-value: 3.47e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788326   3 LVTVQRSPTPSTTSSPCAS-EADSGEEECRSQPRSISESFLTVKGAALFLPRGNGSSTPRiSHRRNKHAGDLQQHLQAMF 81
Cdd:cd11652    1 LVTVQRSPTPSGNSNPDGSdDEEEGDEEQRRKRLQRSESFFAVKGAALILPQGDRTNRPR-EIASHKHAGELQQHLQAMF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788326  82 ILLRPEDNIRLAVRLESTYQNRTRYMVVVSTNGRQDTEESIVLGMDFSSNDSStCTMGLVLPLWSDTLIHLDGDGGFSVS 161
Cdd:cd11652   80 NLLRPEDTIKLAVRLESVRSNRTRYLVVVSTLGRQDTEESILLGVDFPPKESS-CTIGLVLPIWSDTQVHLDGDGGFSVT 158

                        170
                 ....*....|....*..
gi 530788326 162 TDNRVHIFKPVSVQAMW 178
Cdd:cd11652  159 SDGKTHIFKPVSVQAMW 175
 
Name Accession Description Interval E-value
SSH-N cd11652
N-terminal domain conserved in slingshot (SSH) phosphatases; This domain or region conserved ...
 3-178 3.47e-97

N-terminal domain conserved in slingshot (SSH) phosphatases; This domain or region conserved in Bilateria is found N-terminal to the DEK_C-like and catalytic domains of slingshot phosphatases. Slingshot is a cofilin-specific phosphatase. Dephosphorylation reactivates cofilin, which in turn depolymerizes actin and is thus required for actin filament reorganization. Slingshot is a member of the dual-specificity protein phosphatase family. This N-terminal SSH region may be involved in P-cofilin binding (the model C-terminus plus the DEK_C-like domain, which are characterized as the "B" domain in some of the literature), and may be required for the F-actin mediated activation of slingshot (the N-terminal region of this model, sometimes referred to as the "A" domain).


Pssm-ID: 212166  Cd Length: 233  Bit Score: 281.54  E-value: 3.47e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788326   3 LVTVQRSPTPSTTSSPCAS-EADSGEEECRSQPRSISESFLTVKGAALFLPRGNGSSTPRiSHRRNKHAGDLQQHLQAMF 81
Cdd:cd11652    1 LVTVQRSPTPSGNSNPDGSdDEEEGDEEQRRKRLQRSESFFAVKGAALILPQGDRTNRPR-EIASHKHAGELQQHLQAMF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788326  82 ILLRPEDNIRLAVRLESTYQNRTRYMVVVSTNGRQDTEESIVLGMDFSSNDSStCTMGLVLPLWSDTLIHLDGDGGFSVS 161
Cdd:cd11652   80 NLLRPEDTIKLAVRLESVRSNRTRYLVVVSTLGRQDTEESILLGVDFPPKESS-CTIGLVLPIWSDTQVHLDGDGGFSVT 158

                        170
                 ....*....|....*..
gi 530788326 162 TDNRVHIFKPVSVQAMW 178
Cdd:cd11652  159 SDGKTHIFKPVSVQAMW 175
 
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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