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Conserved domains on  [gi|66346728|ref|NP_001018051|]
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laforin isoform b [Homo sapiens]

Protein Classification

CBM20_laforin and DSP_laforin-like domain-containing protein( domain architecture ID 12944636)

CBM20_laforin and DSP_laforin-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 155-309 2.70e-76

dual specificity phosphatase domain of laforin and similar domains; This family is composed of glucan phosphatases including vertebrate dual specificity protein phosphatase laforin, also called lafora PTPase (LAFPTPase), and plant starch excess4 (SEX4). Laforin is a glycogen phosphatase; its gene is mutated in Lafora progressive myoclonus epilepsy or Lafora disease (LD), a fatal autosomal recessive neurodegenerative disorder characterized by the presence of progressive neurological deterioration, myoclonus, and epilepsy. One characteristic of LD is the accumulation of insoluble glucans. Laforin prevents LD by at least two mechanisms: by preventing hyperphosphorylation of glycogen by dephosphorylating it, allowing proper glycogen formation, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with malin. Laforin contains an N-terminal CBM20 (carbohydrate-binding module, family 20) domain and a C-terminal catalytic dual specificity phosphatase (DSP) domain. Plant SEX4 regulate starch metabolism by selectively dephosphorylating glucose moieties within starch glucan chains. It contains an N-terminal catalytic DSP domain and a C-terminal Early (E) set domain.


:

Pssm-ID: 350375 [Multi-domain]  Cd Length: 146  Bit Score: 230.16  E-value: 2.70e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 155 MHYSRILPNIWLGSCPRQVEHVTIKLKHelGITAVMNFQTEWDIvqnssgcnrYPEPMTPDTMIKLYREEGLAYIWMPTP 234
Cdd:cd14526   1 LNYSRILPNLIVGSCPQNPEDVDRLKKE--GVTAVLNLQTDSDM---------EYWGVDIDSIRKACKESGIRYVRLPIR 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66346728 235 DMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAvYIDEEA 309
Cdd:cd14526  70 DFDTEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPC-GPDEEA 143
CBM20_laforin cd05806
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 1-129 4.12e-57

Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Laforin, encoded by the EPM2A gene, is a dual-specificity phosphatase that dephosphorylates complex carbohydrates. Mutations in the gene encoding laforin result in Lafora disease, a fatal autosomal recessive neurodegenerative disorder characterized by the presence of intracellular deposits of insoluble, abnormally branched, glycogen-like polymers, known as Lafora bodies, in neurons, muscle, liver, and other tissues. The molecular basis for the formation of these Lafora bodies is unknown. Laforin is one of the only phosphatases that contains a carbohydrate-binding module. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


:

Pssm-ID: 99881  Cd Length: 112  Bit Score: 180.02  E-value: 4.12e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728   1 MRFRFGVVVPPAvaGARPELLVVGSRPELGRWEPRGAVRLRPAGTAagdgaLALQEPGLWLGEVELaaeeaaqdgAEPGR 80
Cdd:cd05806   1 MLFRFGVVLTFA--DRDTELLVLGSRPELGSWDPQRAVPMRPARKA-----LSPQEPSLWLGEVEL---------SEPGS 64

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 66346728  81 VDTFWYKFLKREPGgELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHW 129
Cdd:cd05806  65 EDTFWYKFLKREAG-ALIWEGNGPHHDRCCVYDSSNLVDGVYCLPVGHW 112
 
Name Accession Description Interval E-value
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 155-309 2.70e-76

dual specificity phosphatase domain of laforin and similar domains; This family is composed of glucan phosphatases including vertebrate dual specificity protein phosphatase laforin, also called lafora PTPase (LAFPTPase), and plant starch excess4 (SEX4). Laforin is a glycogen phosphatase; its gene is mutated in Lafora progressive myoclonus epilepsy or Lafora disease (LD), a fatal autosomal recessive neurodegenerative disorder characterized by the presence of progressive neurological deterioration, myoclonus, and epilepsy. One characteristic of LD is the accumulation of insoluble glucans. Laforin prevents LD by at least two mechanisms: by preventing hyperphosphorylation of glycogen by dephosphorylating it, allowing proper glycogen formation, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with malin. Laforin contains an N-terminal CBM20 (carbohydrate-binding module, family 20) domain and a C-terminal catalytic dual specificity phosphatase (DSP) domain. Plant SEX4 regulate starch metabolism by selectively dephosphorylating glucose moieties within starch glucan chains. It contains an N-terminal catalytic DSP domain and a C-terminal Early (E) set domain.


Pssm-ID: 350375 [Multi-domain]  Cd Length: 146  Bit Score: 230.16  E-value: 2.70e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 155 MHYSRILPNIWLGSCPRQVEHVTIKLKHelGITAVMNFQTEWDIvqnssgcnrYPEPMTPDTMIKLYREEGLAYIWMPTP 234
Cdd:cd14526   1 LNYSRILPNLIVGSCPQNPEDVDRLKKE--GVTAVLNLQTDSDM---------EYWGVDIDSIRKACKESGIRYVRLPIR 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66346728 235 DMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAvYIDEEA 309
Cdd:cd14526  70 DFDTEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPC-GPDEEA 143
CBM20_laforin cd05806
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 1-129 4.12e-57

Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Laforin, encoded by the EPM2A gene, is a dual-specificity phosphatase that dephosphorylates complex carbohydrates. Mutations in the gene encoding laforin result in Lafora disease, a fatal autosomal recessive neurodegenerative disorder characterized by the presence of intracellular deposits of insoluble, abnormally branched, glycogen-like polymers, known as Lafora bodies, in neurons, muscle, liver, and other tissues. The molecular basis for the formation of these Lafora bodies is unknown. Laforin is one of the only phosphatases that contains a carbohydrate-binding module. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99881  Cd Length: 112  Bit Score: 180.02  E-value: 4.12e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728   1 MRFRFGVVVPPAvaGARPELLVVGSRPELGRWEPRGAVRLRPAGTAagdgaLALQEPGLWLGEVELaaeeaaqdgAEPGR 80
Cdd:cd05806   1 MLFRFGVVLTFA--DRDTELLVLGSRPELGSWDPQRAVPMRPARKA-----LSPQEPSLWLGEVEL---------SEPGS 64

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 66346728  81 VDTFWYKFLKREPGgELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHW 129
Cdd:cd05806  65 EDTFWYKFLKREAG-ALIWEGNGPHHDRCCVYDSSNLVDGVYCLPVGHW 112
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
158-304 4.27e-19

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 81.95  E-value: 4.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728    158 SRILPNIWLGSCPRqveHVTIKLKHELGITAVMNFQTEwdivqnssgcnrypepmtpdtmIKLYREEGLAYIWMPTPDMS 237
Cdd:smart00195   2 SEILPHLYLGSYSD---ALNLALLKKLGITHVINVTNE----------------------VPNYNGSDFTYLGVPIDDNT 56

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66346728    238 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVY 304
Cdd:smart00195  57 ETKISPYFPEAVEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIIS 123
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 164-303 9.40e-15

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: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 69.60  E-value: 9.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728   164 IWLGSCPRQVEHVTIKLkhelGITAVMNFQTEwdivqnssgCNRYPEpmtpdtmiklyreeGLAYIWMPTPDMSTEGRVQ 243
Cdd:pfam00782   1 LYLGSKPTASDAFLSKL----GITAVINVTRE---------VDLYNS--------------GILYLRIPVEDNHETNISK 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728   244 MLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 303
Cdd:pfam00782  54 YLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGI 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
164-281 1.67e-13

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 66.53  E-value: 1.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 164 IWLGSCPRQVEHVTiklkHELGITAVMNFQTEWDIVqnssgcnrypepmtpdtmIKLYREEGLAYIWMPTPDMSTEgRVQ 243
Cdd:COG2453   8 LAGGPLPGGGEADL----KREGIDAVVSLTEEEELL------------------LGLLEEAGLEYLHLPIPDFGAP-DDE 64

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 66346728 244 MLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWL 281
Cdd:COG2453  65 QLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYL 102
CBM_2 smart01065
Starch binding domain;
4-106 7.30e-10

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 55.05  E-value: 7.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728      4 RFGVVVPPAVAGARpeLLVVGSRPELGRWEPRGAVRLRPAGTAAGD--GALALQEPGlwlgevelaaeeaaqdgaepgrv 81
Cdd:smart01065   4 TFKVRNGYTQPGES--VYVVGSVPELGNWNPKKAVPLSPDTDGYPLwkGTVSLPPAG----------------------- 58

                           90       100
                   ....*....|....*....|....*
gi 66346728     82 DTFWYKFLKREPGGELSWEGNGPHH 106
Cdd:smart01065  59 TTIEYKYVKVDEDGSVTWESGPNRR 83
CBM_20 pfam00686
Starch binding domain;
19-106 4.39e-07

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 47.28  E-value: 4.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728    19 ELLVVGSRPELGRWEPRGAVRLRPAGTAAGDgalalqepgLWLgevelaaeeaaqdgaepGRVD-----TFWYKFLKREP 93
Cdd:pfam00686  16 SVYIVGSIPELGNWNPKKAIALSASEYSSYP---------LWS-----------------GTVSlpagtTIEYKYIKVDS 69

                          90
                  ....*....|...
gi 66346728    94 GGELSWEgNGPHH 106
Cdd:pfam00686  70 DGSVTWE-SGPNR 81
 
Name Accession Description Interval E-value
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 155-309 2.70e-76

dual specificity phosphatase domain of laforin and similar domains; This family is composed of glucan phosphatases including vertebrate dual specificity protein phosphatase laforin, also called lafora PTPase (LAFPTPase), and plant starch excess4 (SEX4). Laforin is a glycogen phosphatase; its gene is mutated in Lafora progressive myoclonus epilepsy or Lafora disease (LD), a fatal autosomal recessive neurodegenerative disorder characterized by the presence of progressive neurological deterioration, myoclonus, and epilepsy. One characteristic of LD is the accumulation of insoluble glucans. Laforin prevents LD by at least two mechanisms: by preventing hyperphosphorylation of glycogen by dephosphorylating it, allowing proper glycogen formation, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with malin. Laforin contains an N-terminal CBM20 (carbohydrate-binding module, family 20) domain and a C-terminal catalytic dual specificity phosphatase (DSP) domain. Plant SEX4 regulate starch metabolism by selectively dephosphorylating glucose moieties within starch glucan chains. It contains an N-terminal catalytic DSP domain and a C-terminal Early (E) set domain.


Pssm-ID: 350375 [Multi-domain]  Cd Length: 146  Bit Score: 230.16  E-value: 2.70e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 155 MHYSRILPNIWLGSCPRQVEHVTIKLKHelGITAVMNFQTEWDIvqnssgcnrYPEPMTPDTMIKLYREEGLAYIWMPTP 234
Cdd:cd14526   1 LNYSRILPNLIVGSCPQNPEDVDRLKKE--GVTAVLNLQTDSDM---------EYWGVDIDSIRKACKESGIRYVRLPIR 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66346728 235 DMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAvYIDEEA 309
Cdd:cd14526  70 DFDTEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPC-GPDEEA 143
CBM20_laforin cd05806
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 1-129 4.12e-57

Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Laforin, encoded by the EPM2A gene, is a dual-specificity phosphatase that dephosphorylates complex carbohydrates. Mutations in the gene encoding laforin result in Lafora disease, a fatal autosomal recessive neurodegenerative disorder characterized by the presence of intracellular deposits of insoluble, abnormally branched, glycogen-like polymers, known as Lafora bodies, in neurons, muscle, liver, and other tissues. The molecular basis for the formation of these Lafora bodies is unknown. Laforin is one of the only phosphatases that contains a carbohydrate-binding module. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99881  Cd Length: 112  Bit Score: 180.02  E-value: 4.12e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728   1 MRFRFGVVVPPAvaGARPELLVVGSRPELGRWEPRGAVRLRPAGTAagdgaLALQEPGLWLGEVELaaeeaaqdgAEPGR 80
Cdd:cd05806   1 MLFRFGVVLTFA--DRDTELLVLGSRPELGSWDPQRAVPMRPARKA-----LSPQEPSLWLGEVEL---------SEPGS 64

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 66346728  81 VDTFWYKFLKREPGgELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHW 129
Cdd:cd05806  65 EDTFWYKFLKREAG-ALIWEGNGPHHDRCCVYDSSNLVDGVYCLPVGHW 112
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 158-307 2.79e-19

dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase.


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 82.21  E-value: 2.79e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 158 SRILPNIWLGSCpRQVEHVTIkLKhELGITAVMNFQTEwdivqnssgcnrypepmtpdtMIKLYREEGLAYIWMPTPDMS 237
Cdd:cd14498   2 SEILPGLYLGSL-DAAQDKEL-LK-KLGITHILNVAGE---------------------PPPNKFPDGIKYLRIPIEDSP 57

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 238 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDE 307
Cdd:cd14498  58 DEDILSHFEEAIEFIEEALKKGGKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRPIISPNP 127
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
158-304 4.27e-19

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 81.95  E-value: 4.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728    158 SRILPNIWLGSCPRqveHVTIKLKHELGITAVMNFQTEwdivqnssgcnrypepmtpdtmIKLYREEGLAYIWMPTPDMS 237
Cdd:smart00195   2 SEILPHLYLGSYSD---ALNLALLKKLGITHVINVTNE----------------------VPNYNGSDFTYLGVPIDDNT 56

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66346728    238 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVY 304
Cdd:smart00195  57 ETKISPYFPEAVEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIIS 123
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 156-303 2.62e-15

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 71.91  E-value: 2.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 156 HYSRILPNIWLGSCPrqVEHVTIKLKHELGITAVMNfqtewdivqnssgCNRYPEPMTPDTMIKLYREEGLAYIWMPTPD 235
Cdd:cd14524   1 WYDRIDDTVILGALP--FRSMTVALVAKENVRGVIT-------------MNEEYETRFFCNSKEEWKALGVEQLRLPTVD 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66346728 236 MSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 303
Cdd:cd14524  66 FTGVPSLEDLEKGVDFILKHREKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRPHI 133
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 164-303 9.40e-15

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: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 69.60  E-value: 9.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728   164 IWLGSCPRQVEHVTIKLkhelGITAVMNFQTEwdivqnssgCNRYPEpmtpdtmiklyreeGLAYIWMPTPDMSTEGRVQ 243
Cdd:pfam00782   1 LYLGSKPTASDAFLSKL----GITAVINVTRE---------VDLYNS--------------GILYLRIPVEDNHETNISK 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728   244 MLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 303
Cdd:pfam00782  54 YLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGI 113
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 19-119 2.97e-14

The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 119437  Cd Length: 96  Bit Score: 67.32  E-value: 2.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728  19 ELLVVGSRPELGRWEPRGAVRLRPAGtaagdgalalqEPGLWLGevelaaeeaaQDGAEPGRVDTFWYKFLKREPGGELS 98
Cdd:cd05467  15 SVYVVGSHPELGNWDPAKALRLNTSN-----------SYPLWTG----------EIPLPAPEGQVIEYKYVIVDDDGNVQ 73

                        90       100
                ....*....|....*....|.
gi 66346728  99 WEGNGPHHDRCCTYNENNLVD 119
Cdd:cd05467  74 WESGSNRVLTVPSTSSLIVVD 94
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
164-281 1.67e-13

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 66.53  E-value: 1.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 164 IWLGSCPRQVEHVTiklkHELGITAVMNFQTEWDIVqnssgcnrypepmtpdtmIKLYREEGLAYIWMPTPDMSTEgRVQ 243
Cdd:COG2453   8 LAGGPLPGGGEADL----KREGIDAVVSLTEEEELL------------------LGLLEEAGLEYLHLPIPDFGAP-DDE 64

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 66346728 244 MLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWL 281
Cdd:COG2453  65 QLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYL 102
CBM_2 smart01065
Starch binding domain;
4-106 7.30e-10

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 55.05  E-value: 7.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728      4 RFGVVVPPAVAGARpeLLVVGSRPELGRWEPRGAVRLRPAGTAAGD--GALALQEPGlwlgevelaaeeaaqdgaepgrv 81
Cdd:smart01065   4 TFKVRNGYTQPGES--VYVVGSVPELGNWNPKKAVPLSPDTDGYPLwkGTVSLPPAG----------------------- 58

                           90       100
                   ....*....|....*....|....*
gi 66346728     82 DTFWYKFLKREPGGELSWEGNGPHH 106
Cdd:smart01065  59 TTIEYKYVKVDEDGSVTWESGPNRR 83
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 158-303 8.59e-08

dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class III MKPs consist of DUSP8, DUSP10/MKP-5 and DUSP16/MKP-7, and are JNK/p38-selective phosphatases, which are found in both the cell nucleus and cytoplasm. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350416 [Multi-domain]  Cd Length: 140  Bit Score: 50.49  E-value: 8.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 158 SRILPNIWLGScprQVEHVTIKLKHELGITAVMNFqtewdivqnSSGCNRYPepMTPDTmiklyreeglAYIWMPTPDMS 237
Cdd:cd14568   2 TRILPHLYLGS---QRDVLDKDLMQRNGISYVLNV---------SNTCPKPD--FIPDS----------HFLRIPVNDSY 57

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66346728 238 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 303
Cdd:cd14568  58 CEKLLPWLDKAVEFIEKARASNKRVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRPTI 123
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 157-303 3.15e-07

dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is composed of dual specificity protein phosphatase 14 (DUSP14, also known as MKP-6), 18 (DUSP18), 21 (DUSP21), 28 (DUSP28), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses. DUSP18 has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane. DUSP28 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells.


Pssm-ID: 350364 [Multi-domain]  Cd Length: 133  Bit Score: 48.70  E-value: 3.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 157 YSRILPNIWLGSCprqvEHVTIKLKHELGITAVMNFQTEwdivqnssgcnrYPEPMTPdtmiklyreeGLAYIWMPTPDM 236
Cdd:cd14514   1 ISQITPHLFLSGA----SAATPPLLLSRGITCIINATTE------------LPDPSYP----------GIEYLRVPVEDS 54

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66346728 237 STEgrvQMLP--QAVC-LLHALLEKGHIVYVHCNAGVGRStAAVCgwLQYVM---GWNLRKVQYFLMAKRPAV 303
Cdd:cd14514  55 PHA---DLSPhfDEVAdKIHQVKRRGGRTLVHCVAGVSRS-ATLC--LAYLMkyeGMTLREAYKHVKAARPII 121
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 157-281 3.41e-07

unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily is composed of uncharacterized bacterial and plant dual-specificity protein phosphatases. DUSPs function as a protein-serine/threonine phosphatases (EC 3.1.3.16) and a protein-tyrosine-phosphatases (EC 3.1.3.48).


Pssm-ID: 350376 [Multi-domain]  Cd Length: 136  Bit Score: 48.81  E-value: 3.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 157 YSRILPNIWLGSCPRQVEHVTiklkhelGITAVMnfqtewDIvqnssgCNRYPepmtpdtmiklYREEGLAYIWMPTPDM 236
Cdd:cd14527   5 YDEVLPGLYLGRWPSADELPP-------GVPAVL------DL------TAELP-----------RPRKRQAYRCVPLLDL 54

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 66346728 237 sTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWL 281
Cdd:cd14527  55 -VAPTPEQLERAVAWIEELRAQGGPVLVHCALGYGRSATVVAAWL 98
CBM_20 pfam00686
Starch binding domain;
19-106 4.39e-07

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 47.28  E-value: 4.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728    19 ELLVVGSRPELGRWEPRGAVRLRPAGTAAGDgalalqepgLWLgevelaaeeaaqdgaepGRVD-----TFWYKFLKREP 93
Cdd:pfam00686  16 SVYIVGSIPELGNWNPKKAIALSASEYSSYP---------LWS-----------------GTVSlpagtTIEYKYIKVDS 69

                          90
                  ....*....|...
gi 66346728    94 GGELSWEgNGPHH 106
Cdd:pfam00686  70 DGSVTWE-SGPNR 81
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 160-303 4.70e-07

dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual specificity protein phosphatase 19 (DUSP19), also called low molecular weight dual specificity phosphatase 3 (LMW-DSP3) or stress-activated protein kinase (SAPK) pathway-regulating phosphatase 1 (SKRP1), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP19 interacts with the MAPK kinase MKK7, a JNK activator, and inactivates the JNK MAPK pathway.


Pssm-ID: 350373 [Multi-domain]  Cd Length: 137  Bit Score: 48.12  E-value: 4.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 160 ILPNIWLGSCPRQVEHVTIKlKHElgITAVMNFQtewdivqnSSGCNRYPEPMT---------PDTMIKLYREEGLAYIw 230
Cdd:cd14523   5 IKPWLLLSSQDVAHDLETLK-KHK--VTHILNVA--------YGVENAFPDDFTyktisildlPETDITSYFPECFEFI- 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66346728 231 mptpdmsTEGRVQmlpqavcllhallekGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 303
Cdd:cd14523  73 -------DEAKSQ---------------DGVVLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNARPSI 123
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 19-101 2.13e-06

Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99883  Cd Length: 95  Bit Score: 45.43  E-value: 2.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728  19 ELLVVGSRPELGRWEPRGAVRLRPAGTAAGDGALALqepglwlgevelaaeeaaqdgaePGRVdTFWYKFLKREPGGELS 98
Cdd:cd05808  16 NVYVVGNVPELGNWSPANAVALSAATYPVWSGTVDL-----------------------PAGT-AIEYKYIKKDGSGTVT 71


                ...
gi 66346728  99 WEG 101
Cdd:cd05808  72 WES 74
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 159-303 3.33e-06

dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs, which are involved in gene regulation, cell proliferation, programmed cell death and stress responses, as an important feedback control mechanism that limits MAPK cascades. MKPs, also referred to as typical DUSPs, function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III).


Pssm-ID: 350362 [Multi-domain]  Cd Length: 136  Bit Score: 45.94  E-value: 3.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 159 RILPNIWLGSCpRQVEHvtIKLKHELGITAVMNFQTewdivqnssgcnrypepmtpdTMIKLYREEGLAYIWMPTPDMST 238
Cdd:cd14512   3 RILPNLYLGSQ-RDSLN--LELMQQLGIGYVLNVSN---------------------TCPNPDFIGLFHYKRIPVNDSFC 58

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66346728 239 EGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 303
Cdd:cd14512  59 QNISPWFDEAIEFIEEAKASNGGVLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRPTI 123
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
 160-285 7.12e-06

dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual specificity protein phosphatase 2 (DUSP2), also called dual specificity protein phosphatase PAC-1, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (MKPs), it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP2 can preferentially dephosphorylate ERK1/2 and p38, but not JNK in vitro. It is predominantly expressed in hematopoietic tissues with high T-cell content, such as thymus, spleen, lymph nodes, peripheral blood and other organs such as the brain and liver. It has a critical and positive role in inflammatory responses. DUSP2 mRNA and protein are significantly reduced in most solid cancers including breast, colon, lung, ovary, kidney and prostate, and the suppression of DUSP2 is associated with tumorigenesis and malignancy. DUSP2 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350489 [Multi-domain]  Cd Length: 144  Bit Score: 45.24  E-value: 7.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 160 ILPNIWLGSCPRQVEHVTIKlkhELGITAVMNFqtewdivqnSSGCnrypepmtPDtmiklYREEGLAYIWMPTPDMSTE 239
Cdd:cd14641   7 ILPFLFLGSAHHSSRRETLE---SLGITAVLNV---------SSSC--------PN-----YFEGQFQYKSIPVEDSHMA 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 66346728 240 GRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRStAAVCgwLQYVM 285
Cdd:cd14641  62 DISAWFQEAIDFIDSVKNSGGRVLVHCQAGISRS-ATIC--LAYLI 104
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 159-303 1.71e-05

dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class II MKPs consist of DUSP6/MKP-3, DUSP7/MKP-X and DUSP9/MKP-4, and are ERK-selective cytoplasmic MKPs. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350414 [Multi-domain]  Cd Length: 137  Bit Score: 43.85  E-value: 1.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 159 RILPNIWLGScprqVEHVT-IKLKHELGITAVMNfqtewdivqnssgcnrypepMTPDTMIKLYREEGLAYIWMPTPDMS 237
Cdd:cd14566   3 EILPFLYLGN----AKDSAnIDLLKKYNIKYILN--------------------VTPNLPNTFEEDGGFKYLQIPIDDHW 58

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66346728 238 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 303
Cdd:cd14566  59 SQNLSAFFPEAISFIDEARSKKCGVLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKRKSNI 124
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 160-285 1.80e-05

dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class I MKPs consist of DUSP1/MKP-1, DUSP2 (PAC1), DUSP4/MKP-2 and DUSP5. They are all mitogen- and stress-inducible nuclear MKPs. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350413 [Multi-domain]  Cd Length: 138  Bit Score: 43.92  E-value: 1.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 160 ILPNIWLGSCprqvEHVTIK-LKHELGITAVMNFqtewdivqnSSGCNRYPEPMtpdtmiklyreegLAYIWMPTPDMST 238
Cdd:cd14565   4 ILPFLYLGSA----YHASRReVLKALGITAVLNV---------SRNCPNHFEDH-------------FQYKSIPVEDSHN 57

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 66346728 239 EGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRStAAVCgwLQYVM 285
Cdd:cd14565  58 ADISSWFEEAIGFIDKVKASGGRVLVHCQAGISRS-ATIC--LAYLM 101
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 213-303 3.78e-05

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 42.34  E-value: 3.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 213 TPDTMIKLYREEGLAYIWMPTPDMSTEgrvqmlpqAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKV 292
Cdd:cd14494  18 PLEADSRFLKQLGVTTIVDLTLAMVDR--------FLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEA 89

                        90
                ....*....|.
gi 66346728 293 QYFLMAKRPAV 303
Cdd:cd14494  90 VRIVRLIRPGG 100
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 160-285 5.10e-05

dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; Serine/threonine/tyrosine-interacting protein (STYX), also called protein tyrosine phosphatase-like protein, is a catalytically inactive member of the protein tyrosine phosphatase family that plays an integral role in regulating pathways by competing with active phosphatases for binding to MAPKs. It acts as a nuclear anchor for MAPKs, affecting their nucleocytoplasmic shuttling.


Pssm-ID: 350372 [Multi-domain]  Cd Length: 151  Bit Score: 42.70  E-value: 5.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 160 ILPNIWLGSCPRQVEHvtiKLKH--ELGITAVMNfqtewdIVQNSSGcnRYPEPMTPDtmiklyreeGLAYIWMPTPDMS 237
Cdd:cd14522   8 ILPGLYLGPYSAAMKS---KLEVllKHGITHIVC------VRQNIEA--NFIKPNFPD---------HFRYLVLDVADNP 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 66346728 238 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVcgwLQYVM 285
Cdd:cd14522  68 TENIIRHFPTVKEFIDDCLQTGGKVLVHGNAGISRSAALV---IAYIM 112
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 247-312 5.63e-05

dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is composed of Arabidopsis thaliana INDOLE-3-BUTYRIC ACID (IBA) RESPONSE 5 (IBR5) and similar plant proteins. IBR5 protein is also called SKP1-interacting partner 33. The IBR5 gene encodes a dual-specificity phosphatase (DUSP) which acts as a positive regulator of plant responses to auxin and abscisic acid. DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. IBR5 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs. It has been shown to target MPK12, which is a negative regulator of auxin signaling.


Pssm-ID: 350510 [Multi-domain]  Cd Length: 130  Bit Score: 42.14  E-value: 5.63e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66346728 247 QAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDEEAASQ 312
Cdd:cd18534  61 EAVDFIEQCRKDKARVLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRPSINLSPAVAKQ 126
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 158-303 6.63e-05

dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual specificity protein phosphatase 16 (DUSP16), also called mitogen-activated protein kinase (MAPK) phosphatase 7 (MKP-7), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP16/MKP-7 plays an essential role in perinatal survival and selectively controls the differentiation and cytokine production of myeloid cells. It is acetylated by Mycobacterium tuberculosis Eis protein, which leads to the inhibition of JNK-dependent autophagy, phagosome maturation, and ROS generation, and thus, initiating suppression of host immune responses. DUSP16/MKP-7 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350494 [Multi-domain]  Cd Length: 145  Bit Score: 42.32  E-value: 6.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 158 SRILPNIWLGsCPRQVEHVTIKLKHELGItavmnfqtewdiVQNSSgcNRYPEP-MTPDTMiklyreeglaYIWMPTPDM 236
Cdd:cd14646   4 TRILPHLYLG-CQRDVLNKELMQQNGIGY------------VLNAS--NTCPKPdFIPESH----------FLRVPVNDS 58

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66346728 237 STEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 303
Cdd:cd14646  59 FCEKILPWLDKSVDFIEKAKASNGRVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPTI 125
DUSP22 cd14581
dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), ...
 224-287 7.71e-05

dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), also called JNK-stimulatory phosphatase-1 (JSP-1), low molecular weight dual specificity phosphatase 2 (LMW-DSP2), mitogen-activated protein kinase phosphatase x (MKP-x) or VHR-related MKPx (VHX), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP22 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP22 negatively regulates the estrogen receptor-alpha-mediated signaling pathway and the IL6-leukemia inhibitory factor (LIF)-STAT3-mediated signaling pathway. It also regulates cell death by acting as a scaffold protein for the ASK1-MKK7-JNK signal transduction pathway independently of its phosphatase activity.


Pssm-ID: 350429 [Multi-domain]  Cd Length: 149  Bit Score: 42.09  E-value: 7.71e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66346728 224 EGLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYV--MGW 287
Cdd:cd14581  45 EGMTYLCIPAADSPSQNLTQHFKESIKFIHECRLRGEGCLVHCLAGVSRSVTLVVAYIMTVtdFGW 110
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 182-301 1.89e-04

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 41.95  E-value: 1.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 182 HELGITAVMNFQTEWDIVQNSSGCNR-----YPEpmtpdtmiKLYREEGLAYIWMPTPDMSTEGRVQMLpQAVCLLHALL 256
Cdd:cd14506  36 KEKGIKTVINLQEPGEHASCGPGLEPesgfsYLP--------EAFMRAGIYFYNFGWKDYGVPSLTTIL-DIVKVMAFAL 106

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 66346728 257 EKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRP 301
Cdd:cd14506 107 QEGGKVAVHCHAGLGRTGVLIACYLVYALRMSADQAIRLVRSKRP 151
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 180-278 2.08e-04

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 41.09  E-value: 2.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 180 LKHElGITAVMNFQTEWDIVQNssGCNRYPEpmtpdtmikLYREEGLAYIWMPTPDMST---EGRVQMLPQAvclLHALL 256
Cdd:cd14505  39 LKDQ-GVDDVVTLCTDGELEEL--GVPDLLE---------QYQQAGITWHHLPIPDGGVpsdIAQWQELLEE---LLSAL 103

                        90       100
                ....*....|....*....|...
gi 66346728 257 EKGHIVYVHCNAGVGRS-TAAVC 278
Cdd:cd14505 104 ENGKKVLIHCKGGLGRTgLIAAC 126
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 158-303 2.44e-04

dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual specificity protein phosphatase 10 (DUSP10), also called mitogen-activated protein kinase (MAPK) phosphatase 5 (MKP-5), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP10/MKP-5 coordinates skeletal muscle regeneration by negatively regulating mitochondria-mediated apoptosis. It is also an important regulator of intestinal epithelial barrier function and a suppressor of colon tumorigenesis. DUSP10/MKP-5 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350415 [Multi-domain]  Cd Length: 152  Bit Score: 40.89  E-value: 2.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 158 SRILPNIWLGScprQVEHVTIKLKHELGITAVMNfqtewdiVQNSSGCNRYPEPmtpdtmiklyreeGLAYIWMPTPDMS 237
Cdd:cd14567   2 TPILPFLYLGN---ERDAQDIDTLQRLNIGYVLN-------VTTHLPLYHEGKG-------------GFRYKRLPATDSN 58

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66346728 238 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 303
Cdd:cd14567  59 KQNLRQYFEEAFEFIEEAHQSGKGVLVHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKRPII 124
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
 158-303 5.54e-04

dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein phosphatase slingshot homolog 3 (SSH3), also called SSH-like protein 3, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. The Xenopus homolog (xSSH) is involved in the gastrulation movement. Mouse SSH3 dephosphorylates actin-depolymerizing factor (ADF) and cofilin but is dispensable for development. There are at least two human SSH3 isoforms reported: hSSH-3L (long) and hSSH-3. As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. In addition, hSSH-3L contains a C-terminal tail while hSSH-3 does not.


Pssm-ID: 350419 [Multi-domain]  Cd Length: 144  Bit Score: 39.46  E-value: 5.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 158 SRILPNIWLGScprQVEHVTIKLKHELGITAVMNFQTEWDivqnssgcNRYPEPMTPDTmIKLYREEG--LAYIWMPTPD 235
Cdd:cd14571   5 SRIFPYLYLGS---EWNAANLEELQRNRVSHILNVTREID--------NFFPERFTYMN-IRVYDEEAtqLLPHWKETHR 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66346728 236 MSTEGRVQmlpqavcllhallekGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 303
Cdd:cd14571  73 FIEAARAQ---------------GTRVLVHCKMGVSRSASTVIAYAMKQYGWTLEQALRHVRERRPIV 125
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 224-301 5.57e-04

dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and similar proteins; Dual specificity protein phosphatase 22 (DUSP22, also known as VHX) and 15 (DUSP15, also known as VHY) function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). They are atypical DUSPs; they contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. The both contain N-terminal myristoylation recognition sequences and myristoylation regulates their subcellular location. DUSP22 negatively regulates the estrogen receptor-alpha-mediated signaling pathway and the IL6-leukemia inhibitory factor (LIF)-STAT3-mediated signaling pathway. DUSP15 has been identified as a regulator of oligodendrocyte differentiation. DUSP22 is a single domain protein containing only the catalytic dual specificity phosphatase domain while DUSP15 contains a short C-terminal tail.


Pssm-ID: 350369 [Multi-domain]  Cd Length: 136  Bit Score: 39.27  E-value: 5.57e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66346728 224 EGLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRP 301
Cdd:cd14519  42 EDIKYLCIPAADTPEQNISQHFRECINFIHEARLNGGNVLVHCLAGVSRSVTIVAAYLMTVTDLGWRDALKAVRAARP 119
DSP_DUSP15 cd14582
dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual ...
 209-301 1.46e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual specificity protein phosphatase 15 (DUSP15), also called Vaccinia virus VH1-related dual-specific protein phosphatase Y (VHY) or VH1-related member Y, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). DUSP15 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is highly expressed in the testis and is located in the plasma membrane in a myristoylation-dependent manner. It may be involved in the regulation of meiotic signal transduction in testis cells. It is also expressed in the brain and has been identified as a regulator of oligodendrocyte differentiation. DUSP15 contains an N-terminal catalytic dual specificity phosphatase domain and a short C-terminal tail.


Pssm-ID: 350430 [Multi-domain]  Cd Length: 146  Bit Score: 38.39  E-value: 1.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 209 PEPMTPDtmiklyreegLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWN 288
Cdd:cd14582  41 PQPLLQD----------ITYLRIPLPDTPEAPIKKHFKECISFIHQCRLNGGNCLVHCLAGISRSTTIVVAYVMAVTELS 110

                        90
                ....*....|...
gi 66346728 289 LRKVQYFLMAKRP 301
Cdd:cd14582 111 WQEVLEAIRAVRP 123
DSP_DUSP9 cd14644
dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual ...
 159-300 2.61e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual specificity protein phosphatase 9 (DUSP9), also called mitogen-activated protein kinase (MAPK) phosphatase 4 (MKP-4), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class II subfamily and is an ERK-selective cytoplasmic MKP. DUSP9 is a mediator of bone morphogenetic protein (BMP) signaling to control the appropriate ERK activity critical for the determination of embryonic stem cell fate. Down-regulation of DUSP9 expression has been linked to severe pre-eclamptic placenta as well as cancers such as hepatocellular carcinoma. DUSP9 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350492 [Multi-domain]  Cd Length: 145  Bit Score: 37.67  E-value: 2.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 159 RILPNIWLGsCPRQVEHVTIKLKheLGITAVMNfqtewdivqnssgcnrypepMTPDtMIKLYREEG-LAYIWMPTPDMS 237
Cdd:cd14644   5 QILPNLYLG-SARDSANLETLAK--LGIRYILN--------------------VTPN-LPNFFEKNGdFHYKQIPISDHW 60

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66346728 238 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKR 300
Cdd:cd14644  61 SQNLSQFFPEAIEFIDEALSQNCGVLVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDLVKRKK 123
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 158-303 2.61e-03

dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) family of dual specificity protein phosphatases is composed of Drosophila slingshot phosphatase and its vertebrate homologs: SSH1, SSH2 and SSH3. Its members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. In Drosophila, loss of ssh gene function causes prominent elevation in the levels of P-cofilin and filamentous actin and disorganized epidermal cell morphogenesis, including bifurcation phenotypes of bristles and wing hairs. SSH family phosphatases contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. In addition, many members contain a C-terminal tail. The SSH-N domain plays critical roles in P-cofilin recognition, F-actin-mediated activation, and subcellular localization of SSHs.


Pssm-ID: 350363 [Multi-domain]  Cd Length: 139  Bit Score: 37.37  E-value: 2.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 158 SRILPNIWLGScprqvEHVTIKLKhEL---GITAVMNFQTEWDivqnssgcNRYPEPMTPDTmIKLYREEG---LAYiWM 231
Cdd:cd14513   2 SKIFDHLYLGS-----EWNASNLE-ELqnnGVKYILNVTREID--------NFFPGRFTYHN-IRVWDEEStnlLPY-WN 65

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66346728 232 PTPDMSTEGRvqmlpqavcllhallEKGHIVYVHCNAGVGRSTAAVcgwLQYVM---GWNLRKVQYFLMAKRPAV 303
Cdd:cd14513  66 ETYRFIKEAR---------------RKGSKVLVHCKMGVSRSASTV---IAYAMkeyGWSLEQALEHVKERRSCI 122
DSP_DUSP1 cd14638
dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual ...
 160-293 3.75e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual specificity protein phosphatase 1 (DUSP1), also called mitogen-activated protein kinase (MAPK) phosphatase 1 (MKP-1), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. Human MKP-1 dephosphorylates MAPK1/ERK2, regulating its activity during the meiotic cell cycle. Although initially MKP-1 was considered to be ERK-specific, it has been shown that MKP-1 also dephosphorylates both JNK and p38 MAPKs. DUSP1/MKP-1 is involved in various functions, including proliferation, differentiation, and apoptosis in normal cells. It is a central regulator of a variety of functions in the immune, metabolic, cardiovascular, and nervous systems. It contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350486 [Multi-domain]  Cd Length: 151  Bit Score: 37.35  E-value: 3.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 160 ILPNIWLGScprqVEHVTIK-LKHELGITAVMNFqtewdivqnSSGCnrypepmtPDtmiklYREEGLAYIWMPTPDMST 238
Cdd:cd14638   4 ILPFLYLGS----AYHASRKdMLDTLGITALINV---------SANC--------PN-----HFEGHYQYKSIPVEDNHK 57

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66346728 239 EGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRStAAVCgwLQYVMGWNLRKVQ 293
Cdd:cd14638  58 ADISSWFNEAIDFIDSVKNAGGRVFVHCQAGISRS-ATIC--LAYLMRTNRVKLD 109
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 160-285 4.29e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual specificity protein phosphatase 5 (DUSP5) functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (MKPs), it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP5 preferentially dephosphorylates extracellular signal-regulated kinase (ERK), and is involved in ERK signaling and ERK-dependent inflammatory gene expression in adipocytes. It also plays a role in regulating pressure-dependent myogenic cerebral arterial constriction, which is crucial for the maintenance of constant cerebral blood flow to the brain. DUSP5 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350487 [Multi-domain]  Cd Length: 138  Bit Score: 36.82  E-value: 4.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 160 ILPNIWLGScprqVEHVT-IKLKHELGITAVMNfqtewdIVQNSSGCNRypepmtpdtmiklyreEGLAYIWMPTPDMST 238
Cdd:cd14639   4 ILPFLYLGS----AYHASkCEFLANLHITALLN------VSRRSSEACK----------------GQYHYKWIPVEDSHT 57

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 66346728 239 EGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRStAAVCgwLQYVM 285
Cdd:cd14639  58 ADISSHFQEAIDFIDCVRRAGGKVLVHCEAGISRS-PTIC--MAYLM 101
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 156-281 4.49e-03

dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also called vaccinia H1-related phosphatase (VHR), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP3 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It favors bisphosphorylated substrates over monophosphorylated ones, and prefers pTyr peptides over pSer/pThr peptides. Reported physiological substrates includes MAPKs ERK1/2, JNK, and p38, as well as STAT5, EGFR, and ErbB2. DUSP3 has been linked to breast and prostate cancer, and may also play a role in thrombosis.


Pssm-ID: 350427 [Multi-domain]  Cd Length: 168  Bit Score: 37.44  E-value: 4.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 156 HYSRILPNIWLGScpRQVEHVTIKLKHeLGITAVMNfqtewdivqnSSGCNRYpepMTPDTMIKLYREEGLAYIWMPTPD 235
Cdd:cd14579  20 HCNEVYPRIYVGN--ASVAQNIMRLQR-LGITHVLN----------AAEGKSF---MHVNTNAEFYEDTGITYHGIKAND 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 66346728 236 MSTEGRVQMLPQAVCLLH-ALLEKGHIVYVHCNAGVGRSTAAVCGWL 281
Cdd:cd14579  84 TQHFNLSAYFEEAADFIDkALAQKNGRVLVHCREGYSRSPTLVIAYL 130
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 179-285 5.47e-03

dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is composed of dual specificity protein phosphatase 3 (DUSP3, also known as VHR), 13B (DUSP13B, also known as TMDP), 26 (DUSP26, also known as MPK8), 13A (DUSP13A, also known as MDSP), dual specificity phosphatase and pro isomerase domain containing 1 (DUPD1), and inactive DUSP27. In general, DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Members of this family are atypical DUSPs; they contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Inactive DUSP27 contains a dual specificity phosphatase-like domain with the active site cysteine substituted to serine.


Pssm-ID: 350365 [Multi-domain]  Cd Length: 148  Bit Score: 36.81  E-value: 5.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 179 KLKhELGITAVMNfqtewdIVQNSSGcnrypepMTPDTMIKLYREEGLAYIWMPTPDMSTEGRVQMLPQAVCLLH-ALLE 257
Cdd:cd14515  21 KLK-KLGITHVLN------AAEGKKN-------GEVNTNAKFYKGSGIIYLGIPASDLPTFDISQYFDEAADFIDkALSD 86

                        90       100
                ....*....|....*....|....*...
gi 66346728 258 KGHIVYVHCNAGVGRSTAAVcgwLQYVM 285
Cdd:cd14515  87 PGGKVLVHCVEGVSRSATLV---LAYLM 111
DSP_DUSP7 cd14643
dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual ...
 159-300 5.95e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual specificity protein phosphatase 7 (DUSP7), also called mitogen-activated protein kinase (MAPK) phosphatase X (MKP-X) or dual specificity protein phosphatase PYST2, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class II subfamily and is an ERK-selective cytoplasmic MKP. DUSP7 has been shown as an essential regulator of multiple steps in oocyte meiosis. Due to alternative promoter usage, the PYST2 gene gives rise to two isoforms, PYST2-S and PYST2-L. PYST2-L is over-expressed in leukocytes derived from AML and ALL patients as well as in some solid tumors and lymphoblastoid cell lines; it plays a role in cell-crowding. It contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350491 [Multi-domain]  Cd Length: 149  Bit Score: 36.54  E-value: 5.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 159 RILPNIWLGsCPRQVEHVTIKLKHelGITAVMNfqtewdivqnssgcnrypepMTPDtMIKLYREEG-LAYIWMPTPDMS 237
Cdd:cd14643   8 QILPYLYLG-CAKDSTNLDVLGKY--GIKYILN--------------------VTPN-LPNMFEHDGeFKYKQIPISDHW 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66346728 238 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKR 300
Cdd:cd14643  64 SQNLSQFFPEAISFIDEARSKKCGILVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDFVKRKK 126
DSP_DUSP8 cd14645
dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual ...
 158-303 6.67e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual specificity protein phosphatase 8 (DUSP8), also called DUSP hVH-5 or M3/6, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP8 controls basal and acute stress-induced ERK1/2 signaling in adult cardiac myocytes, which impacts contractility, ventricular remodeling, and disease susceptibility. It also plays a role in decreasing ureteric branching morphogenesis by inhibiting p38MAPK. DUSP8 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350493 [Multi-domain]  Cd Length: 151  Bit Score: 36.53  E-value: 6.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 158 SRILPNIWLGScprQVEHVTIKLKHELGITAVMNfqtewdivqNSSGCNRyPEPMTPDTMIKLYREEGLAYIWMPTPDMS 237
Cdd:cd14645  13 TRILPHLYLGS---QKDVLNKDLMAQNGITYVLN---------ASNSCPK-PDFICESHFMRIPVNDNYCEKLLPWLDKS 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728 238 TEgrvqmlpqavcllhaLLEKGHI----VYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 303
Cdd:cd14645  80 IE---------------FIDKAKVsncrVIVHCLAGISRSATIAIAYIMKTMGLSSDDAYRFVKDRRPSI 134
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 219-272 6.69e-03

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 36.49  E-value: 6.69e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 66346728 219 KLYREEGLAYIWMPTPDMSTEGRVQMLpQAVCLLHALLEKGHIVYVHCNAGVGR 272
Cdd:cd14504  43 HSDTCPGLRYHHIPIEDYTPPTLEQID-EFLDIVEEANAKNEAVLVHCLAGKGR 95
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 22-102 6.73e-03

Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99886 [Multi-domain]  Cd Length: 106  Bit Score: 35.71  E-value: 6.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66346728  22 VVGSRPELGRWEPRGAVRLRPAGTAAGDgalalqePgLWLGEVELAaeeaaqdgaePGrvDTFWYKFLKREPGGELSWEG 101
Cdd:cd05811  25 IVGSIPQLGNWDTSSAVALSASQYTSSN-------P-LWSVTIPLP----------AG--TSFEYKFIRKESDGSVTWES 84


                .
gi 66346728 102 N 102
Cdd:cd05811  85 D 85
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 239-271 8.23e-03

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 37.38  E-value: 8.23e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 66346728 239 EGRVQMLPQAVcllHALLEKGHIVYVHCNAGVG 271
Cdd:cd05305  13 ENRVALTPAGV---AELVAAGHEVLVEKGAGLG 42
 
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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