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Conserved domains on  [gi|56117818|ref|NP_001007272|]
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dual specificity protein phosphatase 13 isoform 1 [Homo sapiens]

Protein Classification

DSPc domain-containing protein (domain architecture ID 10062770)

DSPc domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DSPc cd00127
Dual specificity phosphatases (DSP); Ser/Thr and Tyr protein phosphatases. Structurally ...
38-179 1.12e-55

Dual specificity phosphatases (DSP); Ser/Thr and Tyr protein phosphatases. Structurally similar to tyrosine-specific phosphatases but with a shallower active site cleft and a distinctive active site signature motif, HCxxGxxR. Characterized as VHR- or Cdc25-like.


:

Pssm-ID: 238073  Cd Length: 139  Bit Score: 175.87  E-value: 1.12e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56117818  38 VDEVWPNLFIGDAATANNRFELWKLGITHVLNAAHKGLYcqggPDFYGSSVSYLGVPAHDLPDFDISAYFSSAADFIHRA 117
Cdd:cd00127   2 LSEITPGLYLGSYPAASDKELLKKLGITHVLNVAKEVPN----ENLFLSDFNYLYVPILDLPSQDISKYFDEAVDFIDDA 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56117818 118 LNTpGAKVLVHCVVGVSRSATLVLAYLMLHQRLSLRQAVITVRQHR-WVFPNRGFLHQLCRLD 179
Cdd:cd00127  78 REK-GGKVLVHCLAGVSRSATLVIAYLMKTLGLSLREAYEFVKSRRpIISPNAGFMRQLKEYE 139
 
Name Accession Description Interval E-value
DSPc cd00127
Dual specificity phosphatases (DSP); Ser/Thr and Tyr protein phosphatases. Structurally ...
38-179 1.12e-55

Dual specificity phosphatases (DSP); Ser/Thr and Tyr protein phosphatases. Structurally similar to tyrosine-specific phosphatases but with a shallower active site cleft and a distinctive active site signature motif, HCxxGxxR. Characterized as VHR- or Cdc25-like.


Pssm-ID: 238073  Cd Length: 139  Bit Score: 175.87  E-value: 1.12e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56117818  38 VDEVWPNLFIGDAATANNRFELWKLGITHVLNAAHKGLYcqggPDFYGSSVSYLGVPAHDLPDFDISAYFSSAADFIHRA 117
Cdd:cd00127   2 LSEITPGLYLGSYPAASDKELLKKLGITHVLNVAKEVPN----ENLFLSDFNYLYVPILDLPSQDISKYFDEAVDFIDDA 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56117818 118 LNTpGAKVLVHCVVGVSRSATLVLAYLMLHQRLSLRQAVITVRQHR-WVFPNRGFLHQLCRLD 179
Cdd:cd00127  78 REK-GGKVLVHCLAGVSRSATLVIAYLMKTLGLSLREAYEFVKSRRpIISPNAGFMRQLKEYE 139
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
40-176 1.72e-36

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551  Cd Length: 138  Bit Score: 126.63  E-value: 1.72e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56117818     40 EVWPNLFIGDAATANNRFELWKLGITHVLNAAhKGLYCQGGPDFYgssvsYLGVPAHDLPDFDISAYFSSAADFIHRALN 119
Cdd:smart00195   3 EILPHLYLGSYSDALNLALLKKLGITHVINVT-NEVPNYNGSDFT-----YLGVPIDDNTETKISPYFPEAVEFIEDAES 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 56117818    120 TpGAKVLVHCVVGVSRSATLVLAYLMLHQRLSLRQAVITVRQHRWVF-PNRGFLHQLC 176
Cdd:smart00195  77 K-GGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIIsPNFGFLRQLI 133
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
45-176 5.52e-32

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 307089  Cd Length: 127  Bit Score: 114.28  E-value: 5.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56117818    45 LFIGDAATANNRFeLWKLGITHVLNaahkglyCQGGPDFYGSSVSYLGVPAHDLPDFDISAYFSSAADFIHRALNTpGAK 124
Cdd:pfam00782   1 LYLGSKPTASDAF-LSKLGITAVIN-------VTREVDLYNSGILYLRIPVEDNHETNISKYLEEAVEFIDDARQK-GGK 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 56117818   125 VLVHCVVGVSRSATLVLAYLMLHQRLSLRQAVITVRQHR-WVFPNRGFLHQLC 176
Cdd:pfam00782  72 VLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRpGISPNFGFKRQLI 124
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
87-163 9.35e-15

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 225297  Cd Length: 180  Bit Score: 69.02  E-value: 9.35e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56117818  87 SVSYLGVPAHDLPDFdisAYFSSAADFIHRALNTpGAKVLVHCVVGVSRSATLVLAYLMLHQRLSLRQAVITVRQHR 163
Cdd:COG2453  74 QVLHLPILDGTVPDL---EDLDKIVDFIEEALSK-GKKVVVHCQGGIGRSGTVIAAYLMLYGGLSLADEAIAVKRRR 146
PRK12361 PRK12361
hypothetical protein; Provisional
43-163 4.42e-05

hypothetical protein; Provisional


Pssm-ID: 183473  Cd Length: 547  Bit Score: 43.07  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56117818   43 PNLFIGDAATANNRFELWKLGITHVLN--AAHKGLycqgGPDFYGSSVSYLGVPA--HDLPDfdiSAYFSSAADFIHRAL 118
Cdd:PRK12361 100 ENLYLGCRLFPADLEKLKSNKITAILDvtAEFDGL----DWSLTEEDIDYLNIPIldHSVPT---LAQLNQAINWIHRQV 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 56117818  119 NTpGAKVLVHCVVGVSRSATLVLAYLMLHQR-LSLRQAVITVRQHR 163
Cdd:PRK12361 173 RA-NKSVVVHCALGRGRSVLVLAAYLLCKDPdLTVEEVLQQIKQIR 217
 
Name Accession Description Interval E-value
DSPc cd00127
Dual specificity phosphatases (DSP); Ser/Thr and Tyr protein phosphatases. Structurally ...
38-179 1.12e-55

Dual specificity phosphatases (DSP); Ser/Thr and Tyr protein phosphatases. Structurally similar to tyrosine-specific phosphatases but with a shallower active site cleft and a distinctive active site signature motif, HCxxGxxR. Characterized as VHR- or Cdc25-like.


Pssm-ID: 238073  Cd Length: 139  Bit Score: 175.87  E-value: 1.12e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56117818  38 VDEVWPNLFIGDAATANNRFELWKLGITHVLNAAHKGLYcqggPDFYGSSVSYLGVPAHDLPDFDISAYFSSAADFIHRA 117
Cdd:cd00127   2 LSEITPGLYLGSYPAASDKELLKKLGITHVLNVAKEVPN----ENLFLSDFNYLYVPILDLPSQDISKYFDEAVDFIDDA 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56117818 118 LNTpGAKVLVHCVVGVSRSATLVLAYLMLHQRLSLRQAVITVRQHR-WVFPNRGFLHQLCRLD 179
Cdd:cd00127  78 REK-GGKVLVHCLAGVSRSATLVIAYLMKTLGLSLREAYEFVKSRRpIISPNAGFMRQLKEYE 139
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
40-176 1.72e-36

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551  Cd Length: 138  Bit Score: 126.63  E-value: 1.72e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56117818     40 EVWPNLFIGDAATANNRFELWKLGITHVLNAAhKGLYCQGGPDFYgssvsYLGVPAHDLPDFDISAYFSSAADFIHRALN 119
Cdd:smart00195   3 EILPHLYLGSYSDALNLALLKKLGITHVINVT-NEVPNYNGSDFT-----YLGVPIDDNTETKISPYFPEAVEFIEDAES 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 56117818    120 TpGAKVLVHCVVGVSRSATLVLAYLMLHQRLSLRQAVITVRQHRWVF-PNRGFLHQLC 176
Cdd:smart00195  77 K-GGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIIsPNFGFLRQLI 133
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
45-176 5.52e-32

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 307089  Cd Length: 127  Bit Score: 114.28  E-value: 5.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56117818    45 LFIGDAATANNRFeLWKLGITHVLNaahkglyCQGGPDFYGSSVSYLGVPAHDLPDFDISAYFSSAADFIHRALNTpGAK 124
Cdd:pfam00782   1 LYLGSKPTASDAF-LSKLGITAVIN-------VTREVDLYNSGILYLRIPVEDNHETNISKYLEEAVEFIDDARQK-GGK 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 56117818   125 VLVHCVVGVSRSATLVLAYLMLHQRLSLRQAVITVRQHR-WVFPNRGFLHQLC 176
Cdd:pfam00782  72 VLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRpGISPNFGFKRQLI 124
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
87-163 9.35e-15

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 225297  Cd Length: 180  Bit Score: 69.02  E-value: 9.35e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56117818  87 SVSYLGVPAHDLPDFdisAYFSSAADFIHRALNTpGAKVLVHCVVGVSRSATLVLAYLMLHQRLSLRQAVITVRQHR 163
Cdd:COG2453  74 QVLHLPILDGTVPDL---EDLDKIVDFIEEALSK-GKKVVVHCQGGIGRSGTVIAAYLMLYGGLSLADEAIAVKRRR 146
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
96-163 4.77e-07

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469  Cd Length: 105  Bit Score: 46.20  E-value: 4.77e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56117818     96 HDLPDFDISAYFSSAADFIH-----RALNTPGAKVLVHCVVGVSRSATLVLAYLMLHQ------RLSLRQAVITVRQHR 163
Cdd:smart00012   8 TGWPDHGVPESPDSILELLRavkknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQleaeagEVDIFDTVKELRSQR 86
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
96-163 4.77e-07

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649  Cd Length: 105  Bit Score: 46.20  E-value: 4.77e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56117818     96 HDLPDFDISAYFSSAADFIH-----RALNTPGAKVLVHCVVGVSRSATLVLAYLMLHQ------RLSLRQAVITVRQHR 163
Cdd:smart00404   8 TGWPDHGVPESPDSILELLRavkknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQleaeagEVDIFDTVKELRSQR 86
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
99-164 6.11e-06

Protein-tyrosine phosphatase;


Pssm-ID: 306584  Cd Length: 233  Bit Score: 44.92  E-value: 6.11e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56117818    99 PDFDISAYFSSAADFIHRALN---TPGAKVLVHCVVGVSRSATLVLAYLMLHQ-----RLSLRQAVITVRQHRW 164
Cdd:pfam00102 142 PDHGVPESPNSLLDLLRKVRKssdPRSGPIVVHCSAGIGRTGTFIAIDILLQQleaegEVDIFQIVKELRSQRP 215
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
99-163 2.16e-05

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550  Cd Length: 259  Bit Score: 43.42  E-value: 2.16e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56117818     99 PDFDISAYFSSAADFIHRALNTPGAK---VLVHCVVGVSRSATLVLAYLMLHQ-----RLSLRQAVITVRQHR 163
Cdd:smart00194 168 PDHGVPESPESILDLIRAVRKSQSTStgpIVVHCSAGVGRTGTFIAIDILLQQleagkEVDIFEIVKELRSQR 240
PTPc cd00047
Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; ...
90-164 3.10e-05

Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG. Characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 238006  Cd Length: 231  Bit Score: 42.96  E-value: 3.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56117818  90 YLGVPAHDLPDfdisayfsSAADFIH-----RALNTPGAK--VLVHCVVGVSRSATLVLAYLMLHQ-----RLSLRQAVI 157
Cdd:cd00047 135 YTGWPDHGVPE--------SPDSLLDllrkvRKSQQQPGSgpIVVHCSAGVGRTGTFIAIDILLQRleaegVVDIFQTVK 206

                ....*..
gi 56117818 158 TVRQHRW 164
Cdd:cd00047 207 ELRSQRP 213
PRK12361 PRK12361
hypothetical protein; Provisional
43-163 4.42e-05

hypothetical protein; Provisional


Pssm-ID: 183473  Cd Length: 547  Bit Score: 43.07  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56117818   43 PNLFIGDAATANNRFELWKLGITHVLN--AAHKGLycqgGPDFYGSSVSYLGVPA--HDLPDfdiSAYFSSAADFIHRAL 118
Cdd:PRK12361 100 ENLYLGCRLFPADLEKLKSNKITAILDvtAEFDGL----DWSLTEEDIDYLNIPIldHSVPT---LAQLNQAINWIHRQV 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 56117818  119 NTpGAKVLVHCVVGVSRSATLVLAYLMLHQR-LSLRQAVITVRQHR 163
Cdd:PRK12361 173 RA-NKSVVVHCALGRGRSVLVLAAYLLCKDPdLTVEEVLQQIKQIR 217
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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