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Conserved domains on  [gi|194332787|ref|NP_001123695|]
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laforin [Xenopus tropicalis]

Protein Classification

laforin family CBM20 domain-containing protein( domain architecture ID 12944636)

laforin family CBM20 (family 20 carbohydrate-binding module) domain-containing protein may play a regulatory role in starch metabolism or glycogen metabolism; similar to Homo sapiens laforin isoform c

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 ...
 137-294 4.30e-80

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: 239.41  E-value: 4.30e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 137 MHFSRILPNIWLGSCPRQREHVTVKMKHelGVTAVLNFQTEWDViqnssgcnnYPEPMSPETMFRLYKEAGITYIWIPTP 216
Cdd:cd14526    1 LNYSRILPNLIVGSCPQNPEDVDRLKKE--GVTAVLNLQTDSDM---------EYWGVDIDSIRKACKESGIRYVRLPIR 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194332787 217 DMSTEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAvYIDEEAMIN 294
Cdd:cd14526   70 DFDTEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPC-GPDEEAIRG 146
CBM20_laforin cd05806
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 1-111 6.85e-73

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: 220.08  E-value: 6.85e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787   1 MLFRFGVIITLNHSDNELLVLGSRKEMGSWDPQYAVPMKPTRCPLSTTEPSFWVGEVLLEEPYT-DTFWFKFIKKESGAL 79
Cdd:cd05806    1 MLFRFGVVLTFADRDTELLVLGSRPELGSWDPQRAVPMRPARKALSPQEPSLWLGEVELSEPGSeDTFWYKFLKREAGAL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 194332787  80 IWEGNGPHHDRCCVFNESNIVDGVYCHPVGHW 111
Cdd:cd05806   81 IWEGNGPHHDRCCVYDSSNLVDGVYCLPVGHW 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 ...
 137-294 4.30e-80

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: 239.41  E-value: 4.30e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 137 MHFSRILPNIWLGSCPRQREHVTVKMKHelGVTAVLNFQTEWDViqnssgcnnYPEPMSPETMFRLYKEAGITYIWIPTP 216
Cdd:cd14526    1 LNYSRILPNLIVGSCPQNPEDVDRLKKE--GVTAVLNLQTDSDM---------EYWGVDIDSIRKACKESGIRYVRLPIR 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194332787 217 DMSTEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAvYIDEEAMIN 294
Cdd:cd14526   70 DFDTEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPC-GPDEEAIRG 146
CBM20_laforin cd05806
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 1-111 6.85e-73

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: 220.08  E-value: 6.85e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787   1 MLFRFGVIITLNHSDNELLVLGSRKEMGSWDPQYAVPMKPTRCPLSTTEPSFWVGEVLLEEPYT-DTFWFKFIKKESGAL 79
Cdd:cd05806    1 MLFRFGVVLTFADRDTELLVLGSRPELGSWDPQRAVPMRPARKALSPQEPSLWLGEVELSEPGSeDTFWYKFLKREAGAL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 194332787  80 IWEGNGPHHDRCCVFNESNIVDGVYCHPVGHW 111
Cdd:cd05806   81 IWEGNGPHHDRCCVYDSSNLVDGVYCLPVGHW 112
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
140-286 7.96e-20

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 83.87  E-value: 7.96e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787   140 SRILPNIWLGSCPRqreHVTVKMKHELGVTAVLNFQTEwdviqnssgcnnypepmspetmFRLYKEAGITYIWIPTPDMS 219
Cdd:smart00195   2 SEILPHLYLGSYSD---ALNLALLKKLGITHVINVTNE----------------------VPNYNGSDFTYLGVPIDDNT 56

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194332787   220 TEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAVY 286
Cdd:smart00195  57 ETKISPYFPEAVEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIIS 123
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
140-303 9.76e-18

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 78.09  E-value: 9.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 140 SRILPN-IWLGSCPRQREHVTVkmkhELGVTAVLNFQTEWdviqnssgcnnypepmspETMFRLYKEAGITYIWIPTPDM 218
Cdd:COG2453    1 SWIIPGlLAGGPLPGGGEADLK----REGIDAVVSLTEEE------------------ELLLGLLEEAGLEYLHLPIPDF 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 219 STEgRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYvIGWSLRK-VQYFLASRRPAVYIDeeaminAQE 297
Cdd:COG2453   59 GAP-DDEQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYLVL-LGLSAEEaLARVRAARPGAVETP------AQR 130


                 ....*.
gi 194332787 298 DFHKKF 303
Cdd:COG2453  131 AFLERF 136
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 146-285 3.16e-17

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: 76.53  E-value: 3.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787  146 IWLGSCPrqreHVTVKMKHELGVTAVLNFQTEwdviqnssgCNNYPEpmspetmfrlykeaGITYIWIPTPDMSTEGRIR 225
Cdd:pfam00782   1 LYLGSKP----TASDAFLSKLGITAVINVTRE---------VDLYNS--------------GILYLRIPVEDNHETNISK 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787  226 MLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:pfam00782  54 YLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGI 113
CBM_2 smart01065
Starch binding domain;
4-88 1.58e-11

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 59.67  E-value: 1.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787     4 RFGVIITLNHSDNELLVLGSRKEMGSWDPQYAVPMKPTrcplSTTEPSfWVGEVLLeEPYTDTFWFKFIKK-ESGALIWE 82
Cdd:smart01065   4 TFKVRNGYTQPGESVYVVGSVPELGNWNPKKAVPLSPD----TDGYPL-WKGTVSL-PPAGTTIEYKYVKVdEDGSVTWE 77


                   ....*.
gi 194332787    83 GNGPHH 88
Cdd:smart01065  78 SGPNRR 83
CBM_20 pfam00686
Starch binding domain;
7-88 7.78e-10

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 54.99  E-value: 7.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787    7 VIITLN-----HSDNELLVLGSRKEMGSWDPQYAVPMKPTRCplsTTEPsFWVGEVLLeEPYTdTFWFKFIKKES-GALI 80
Cdd:pfam00686   1 VSVTFNvnattQYGQSVYIVGSIPELGNWNPKKAIALSASEY---SSYP-LWSGTVSL-PAGT-TIEYKYIKVDSdGSVT 74


                  ....*...
gi 194332787   81 WEgNGPHH 88
Cdd:pfam00686  75 WE-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 ...
 137-294 4.30e-80

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: 239.41  E-value: 4.30e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 137 MHFSRILPNIWLGSCPRQREHVTVKMKHelGVTAVLNFQTEWDViqnssgcnnYPEPMSPETMFRLYKEAGITYIWIPTP 216
Cdd:cd14526    1 LNYSRILPNLIVGSCPQNPEDVDRLKKE--GVTAVLNLQTDSDM---------EYWGVDIDSIRKACKESGIRYVRLPIR 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194332787 217 DMSTEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAvYIDEEAMIN 294
Cdd:cd14526   70 DFDTEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPC-GPDEEAIRG 146
CBM20_laforin cd05806
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 1-111 6.85e-73

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: 220.08  E-value: 6.85e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787   1 MLFRFGVIITLNHSDNELLVLGSRKEMGSWDPQYAVPMKPTRCPLSTTEPSFWVGEVLLEEPYT-DTFWFKFIKKESGAL 79
Cdd:cd05806    1 MLFRFGVVLTFADRDTELLVLGSRPELGSWDPQRAVPMRPARKALSPQEPSLWLGEVELSEPGSeDTFWYKFLKREAGAL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 194332787  80 IWEGNGPHHDRCCVFNESNIVDGVYCHPVGHW 111
Cdd:cd05806   81 IWEGNGPHHDRCCVYDSSNLVDGVYCLPVGHW 112
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 140-289 4.95e-22

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: 89.53  E-value: 4.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 140 SRILPNIWLGSCP--RQREHVtvkmkHELGVTAVLNfqtewdviqnssgCNNYPEPmspetmfrLYKEAGITYIWIPTPD 217
Cdd:cd14498    2 SEILPGLYLGSLDaaQDKELL-----KKLGITHILN-------------VAGEPPP--------NKFPDGIKYLRIPIED 55

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194332787 218 MSTEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAVYIDE 289
Cdd:cd14498   56 SPDEDILSHFEEAIEFIEEALKKGGKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRPIISPNP 127
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
140-286 7.96e-20

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 83.87  E-value: 7.96e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787   140 SRILPNIWLGSCPRqreHVTVKMKHELGVTAVLNFQTEwdviqnssgcnnypepmspetmFRLYKEAGITYIWIPTPDMS 219
Cdd:smart00195   2 SEILPHLYLGSYSD---ALNLALLKKLGITHVINVTNE----------------------VPNYNGSDFTYLGVPIDDNT 56

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194332787   220 TEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAVY 286
Cdd:smart00195  57 ETKISPYFPEAVEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIIS 123
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
140-303 9.76e-18

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 78.09  E-value: 9.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 140 SRILPN-IWLGSCPRQREHVTVkmkhELGVTAVLNFQTEWdviqnssgcnnypepmspETMFRLYKEAGITYIWIPTPDM 218
Cdd:COG2453    1 SWIIPGlLAGGPLPGGGEADLK----REGIDAVVSLTEEE------------------ELLLGLLEEAGLEYLHLPIPDF 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 219 STEgRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYvIGWSLRK-VQYFLASRRPAVYIDeeaminAQE 297
Cdd:COG2453   59 GAP-DDEQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYLVL-LGLSAEEaLARVRAARPGAVETP------AQR 130


                 ....*.
gi 194332787 298 DFHKKF 303
Cdd:COG2453  131 AFLERF 136
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 146-285 3.16e-17

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: 76.53  E-value: 3.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787  146 IWLGSCPrqreHVTVKMKHELGVTAVLNFQTEwdviqnssgCNNYPEpmspetmfrlykeaGITYIWIPTPDMSTEGRIR 225
Cdd:pfam00782   1 LYLGSKP----TASDAFLSKLGITAVINVTRE---------VDLYNS--------------GILYLRIPVEDNHETNISK 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787  226 MLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:pfam00782  54 YLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGI 113
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 138-302 3.33e-16

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: 74.22  E-value: 3.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 138 HFSRILPNIWLGSCPrQREHvTVKMKHELGVTAVLNFQTEWdviQNSSGCNNYPEpmspetmfrlYKEAGITYIWIPTPD 217
Cdd:cd14524    1 WYDRIDDTVILGALP-FRSM-TVALVAKENVRGVITMNEEY---ETRFFCNSKEE----------WKALGVEQLRLPTVD 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 218 MSTEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAVYIDEEAMINAQE 297
Cdd:cd14524   66 FTGVPSLEDLEKGVDFILKHREKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRPHILLRLSQREVLEE 145


                 ....*
gi 194332787 298 dFHKK 302
Cdd:cd14524  146 -FYRK 149
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 4-101 1.35e-15

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: 71.17  E-value: 1.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787   4 RFGVIITLNHSDNeLLVLGSRKEMGSWDPQYAVPMKPtrcplSTTEPsFWVGEVLLEEPYTDTFWFKFIKKES-GALIWE 82
Cdd:cd05467    3 RFQVRCTTQFGQS-VYVVGSHPELGNWDPAKALRLNT-----SNSYP-LWTGEIPLPAPEGQVIEYKYVIVDDdGNVQWE 75

                         90
                 ....*....|....*....
gi 194332787  83 GNGPHHDRCCVFNESNIVD 101
Cdd:cd05467   76 SGSNRVLTVPSTSSLIVVD 94
CBM_2 smart01065
Starch binding domain;
4-88 1.58e-11

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 59.67  E-value: 1.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787     4 RFGVIITLNHSDNELLVLGSRKEMGSWDPQYAVPMKPTrcplSTTEPSfWVGEVLLeEPYTDTFWFKFIKK-ESGALIWE 82
Cdd:smart01065   4 TFKVRNGYTQPGESVYVVGSVPELGNWNPKKAVPLSPD----TDGYPL-WKGTVSL-PPAGTTIEYKYVKVdEDGSVTWE 77


                   ....*.
gi 194332787    83 GNGPHH 88
Cdd:smart01065  78 SGPNRR 83
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 140-285 7.22e-10

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: 56.27  E-value: 7.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 140 SRILPNIWLGScprQREHVTVKMKHELGVTAVLNFqtewdviqnSSGCnnyPEP-MSPETMFRLykeagityiwIPTPDM 218
Cdd:cd14568    2 TRILPHLYLGS---QRDVLDKDLMQRNGISYVLNV---------SNTC---PKPdFIPDSHFLR----------IPVNDS 56

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194332787 219 STEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:cd14568   57 YCEKLLPWLDKAVEFIEKARASNKRVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRPTI 123
CBM_20 pfam00686
Starch binding domain;
7-88 7.78e-10

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 54.99  E-value: 7.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787    7 VIITLN-----HSDNELLVLGSRKEMGSWDPQYAVPMKPTRCplsTTEPsFWVGEVLLeEPYTdTFWFKFIKKES-GALI 80
Cdd:pfam00686   1 VSVTFNvnattQYGQSVYIVGSIPELGNWNPKKAIALSASEY---SSYP-LWSGTVSL-PAGT-TIEYKYIKVDSdGSVT 74


                  ....*...
gi 194332787   81 WEgNGPHH 88
Cdd:pfam00686  75 WE-SGPNR 81
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 141-285 3.69e-09

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: 54.41  E-value: 3.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 141 RILPNIWLGSCprqREHVTVKMKHELGVTAVLNFQtewdviqnssgcNNYPEPmspetmfrlYKEAGITYIWIPTPDMST 220
Cdd:cd14512    3 RILPNLYLGSQ---RDSLNLELMQQLGIGYVLNVS------------NTCPNP---------DFIGLFHYKRIPVNDSFC 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194332787 221 EGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:cd14512   59 QNISPWFDEAIEFIEEAKASNGGVLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRPTI 123
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 142-285 1.48e-08

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: 52.77  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 142 ILPNIWLGSCprqrEHVTVK-MKHELGVTAVLNFqtewdviqnSSGCNNYPEPMspetmfrlykeagITYIWIPTPDMST 220
Cdd:cd14565    4 ILPFLYLGSA----YHASRReVLKALGITAVLNV---------SRNCPNHFEDH-------------FQYKSIPVEDSHN 57

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194332787 221 EGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRStAAVC-GFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:cd14565   58 ADISSWFEEAIGFIDKVKASGGRVLVHCQAGISRS-ATIClAYLMTTRRVRLNEAFDYVKQRRSVI 122
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 139-299 6.50e-08

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: 50.74  E-value: 6.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 139 FSRILPNIWLGSCPRQREHVTvkmkhelGVTAVLnfqtewDViqnssgCNNYPEPMSPETmfrlykeagitYIWIPTPDM 218
Cdd:cd14527    5 YDEVLPGLYLGRWPSADELPP-------GVPAVL------DL------TAELPRPRKRQA-----------YRCVPLLDL 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 219 S--TEGRIRmlpQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMY---VIGWS--LRKVQyflaSRRPAVYIdEEA 291
Cdd:cd14527   55 VapTPEQLE---RAVAWIEELRAQGGPVLVHCALGYGRSATVVAAWLLAygrAKSVAeaEALIR----AARPQVVL-NPA 126


                 ....*...
gi 194332787 292 MINAQEDF 299
Cdd:cd14527  127 QRKALEAW 134
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 164-300 1.59e-07

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: 50.81  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 164 HELGVTAVLNFQTEWDviQNSSGCNNYPE---PMSPETmfrlYKEAGITYIWIPTPDMSTEGRIRMLPQAVYLLFGLLEn 240
Cdd:cd14506   36 KEKGIKTVINLQEPGE--HASCGPGLEPEsgfSYLPEA----FMRAGIYFYNFGWKDYGVPSLTTILDIVKVMAFALQE- 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 241 GHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAVyIDEEAMINAQEDFH 300
Cdd:cd14506  109 GGKVAVHCHAGLGRTGVLIACYLVYALRMSADQAIRLVRSKRPNS-IQTRGQVLCVREFA 167
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 244-285 1.70e-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: 49.66  E-value: 1.70e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 194332787 244 VYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:cd14523   82 VLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNARPSI 123
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 167-271 2.84e-07

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: 49.57  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 167 GVTAVLNFQTEWDViqNSSGCNNYPEpmspetmfrLYKEAGITYIWIPTPDMSTEGRIRMLPQAVYLLFGLLENGHTVYV 246
Cdd:cd14505   43 GVDDVVTLCTDGEL--EELGVPDLLE---------QYQQAGITWHHLPIPDGGVPSDIAQWQELLEELLSALENGKKVLI 111

                         90       100
                 ....*....|....*....|....*.
gi 194332787 247 HCNAGVGRS-TAAVCgfLMYVIGWSL 271
Cdd:cd14505  112 HCKGGLGRTgLIAAC--LLLELGDTL 135
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 142-282 3.27e-07

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: 48.87  E-value: 3.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 142 ILPNIWLGScprqrehVTVKMKHEL------GVTAVLNfqtewdVIQNSSGcnNYPEPMSPEtmfrlykeaGITYIWIPT 215
Cdd:cd14522    8 ILPGLYLGP-------YSAAMKSKLevllkhGITHIVC------VRQNIEA--NFIKPNFPD---------HFRYLVLDV 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194332787 216 PDMSTEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRR 282
Cdd:cd14522   64 ADNPTENIIRHFPTVKEFIDDCLQTGGKVLVHGNAGISRSAALVIAYIMETYGLSYRDAFAYVQQRR 130
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 139-285 1.23e-06

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: 46.78  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 139 FSRILPNIWLGSCprqrEHVTVKMKHELGVTAVLNFQTEwdviqnsSGCNNYPepmspetmfrlykeaGITYIWIPTPDM 218
Cdd:cd14514    1 ISQITPHLFLSGA----SAATPPLLLSRGITCIINATTE-------LPDPSYP---------------GIEYLRVPVEDS 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194332787 219 STEgriRMLP---------QAVYllfgllENGHTVYVHCNAGVGRStAAVCgfLMYVI---GWSLRKVQYFLASRRPAV 285
Cdd:cd14514   55 PHA---DLSPhfdevadkiHQVK------RRGGRTLVHCVAGVSRS-ATLC--LAYLMkyeGMTLREAYKHVKAARPII 121
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 141-285 1.60e-06

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: 46.93  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 141 RILPNIWLGsCPRQREHVTVKMKHelGVTAVLNfqtewdVIQNSsgcnnypepmsPETmfrLYKEAGITYIWIPTPDMST 220
Cdd:cd14566    3 EILPFLYLG-NAKDSANIDLLKKY--NIKYILN------VTPNL-----------PNT---FEEDGGFKYLQIPIDDHWS 59

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194332787 221 EGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:cd14566   60 QNLSAFFPEAISFIDEARSKKCGVLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKRKSNI 124
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
 142-282 1.77e-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: 46.78  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 142 ILPNIWLGSCPRQREHVTVKmkhELGVTAVLNFqtewdviqnSSGCNNYPEpmspeTMFRlykeagitYIWIPTPDMSTE 221
Cdd:cd14641    7 ILPFLFLGSAHHSSRRETLE---SLGITAVLNV---------SSSCPNYFE-----GQFQ--------YKSIPVEDSHMA 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194332787 222 GRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRR 282
Cdd:cd14641   62 DISAWFQEAIDFIDSVKNSGGRVLVHCQAGISRSATICLAYLIQSQRVRLDEAFDFVKQRR 122
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 5-84 2.30e-06

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: 45.73  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787   5 FGVIITLNHSDNELLVlGSRKEMGSWDPQYAVPMKPTRcpLSTTEPsFWVGEVLLeePYTDTFWFKFIKKES-GALIWEG 83
Cdd:cd05811   11 FNERVTTSYGENIKIV-GSIPQLGNWDTSSAVALSASQ--YTSSNP-LWSVTIPL--PAGTSFEYKFIRKESdGSVTWES 84


                 .
gi 194332787  84 N 84
Cdd:cd05811   85 D 85
DSP_DUSP15 cd14582
dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual ...
 208-283 3.79e-06

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: 46.10  E-value: 3.79e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194332787 208 ITYIWIPTPDMSTEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRP 283
Cdd:cd14582   48 ITYLRIPLPDTPEAPIKKHFKECISFIHQCRLNGGNCLVHCLAGISRSTTIVVAYVMAVTELSWQEVLEAIRAVRP 123
DUSP22 cd14581
dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), ...
 140-269 4.25e-06

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: 45.94  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 140 SRILPNIWLGSC--PRQREHVtvkmkHELGVTAVLnfqtewdviqnsSGCNNyPEPMSpetmfrlykeAGITYIWIPTPD 217
Cdd:cd14581    5 NKVLPGLYLGNFkdARDREQL-----SKNNITHIL------------SVHDS-ARPML----------EGMTYLCIPAAD 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 194332787 218 MSTEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYV--IGW 269
Cdd:cd14581   57 SPSQNLTQHFKESIKFIHECRLRGEGCLVHCLAGVSRSVTLVVAYIMTVtdFGW 110
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 140-285 4.85e-06

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: 45.40  E-value: 4.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 140 SRILPNIWLGScprQREHVTVKMKHELGVTAVLNfqtewdviqnssGCNNYPEP-MSPETMFrlykeagityIWIPTPDM 218
Cdd:cd14646    4 TRILPHLYLGC---QRDVLNKELMQQNGIGYVLN------------ASNTCPKPdFIPESHF----------LRVPVNDS 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194332787 219 STEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:cd14646   59 FCEKILPWLDKSVDFIEKAKASNGRVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPTI 125
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 13-88 8.46e-06

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 2. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal CBM20 domains. Included in this group are PDE2-like proteins from Dictyostelium, Entamoeba, and Bacteroides. 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: 99890  Cd Length: 99  Bit Score: 43.85  E-value: 8.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787  13 HSDNELLVLGSRKEMGSWDPQYAVPMKPtrcplstTEPSFWVGEVLLEepyTDTFWF--KFI--KKESGALIWEgNGPHH 88
Cdd:cd05816   12 PKGQSVYVTGSSPELGNWDPQKALKLSD-------VGFPIWEADIDIS---KDSFPFeyKYIiaNKDSGVVSWE-NGPNR 80
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 17-83 1.13e-05

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: 43.12  E-value: 1.13e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194332787  17 ELLVLGSRKEMGSWDPQYAVPMKPtrcplsTTEPSfWVGEVLLeePYTDTFWFKFIKKE-SGALIWEG 83
Cdd:cd05808   16 NVYVVGNVPELGNWSPANAVALSA------ATYPV-WSGTVDL--PAGTAIEYKYIKKDgSGTVTWES 74
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 244-297 1.26e-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: 44.06  E-value: 1.26e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 194332787 244 VYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAVYIDEEAMINAQE 297
Cdd:cd18534   76 VLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRPSINLSPAVAKQLQE 129
DSP_DUSP8 cd14645
dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual ...
 140-285 1.29e-05

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: 44.62  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 140 SRILPNIWLGScprQREHVTVKMKHELGVTAVLNfqtewdviqNSSGCNNyPEPMSPETMFRlykeagityiwIPTPDMS 219
Cdd:cd14645   13 TRILPHLYLGS---QKDVLNKDLMAQNGITYVLN---------ASNSCPK-PDFICESHFMR-----------IPVNDNY 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194332787 220 TEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:cd14645   69 CEKLLPWLDKSIEFIDKAKVSNCRVIVHCLAGISRSATIAIAYIMKTMGLSSDDAYRFVKDRRPSI 134
DSP_DUSP9 cd14644
dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual ...
 141-304 1.39e-05

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: 44.22  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 141 RILPNIWLGSCprqREHVTVKMKHELGVTAVLNfqtewdviqnssgcnnypepMSPETMFRLYKEAGITYIWIPTPDMST 220
Cdd:cd14644    5 QILPNLYLGSA---RDSANLETLAKLGIRYILN--------------------VTPNLPNFFEKNGDFHYKQIPISDHWS 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 221 EGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVqYFLASRRPAVYIDEEAMINAQEDFH 300
Cdd:cd14644   62 QNLSQFFPEAIEFIDEALSQNCGVLVHCLAGISRSVTVTVAYLMQKLNLSLNDA-YDLVKRKKSNISPNFNFMGQLLDFE 140


                 ....
gi 194332787 301 KKFG 304
Cdd:cd14644  141 KSLG 144
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 140-285 1.51e-05

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: 44.36  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 140 SRILPNIWLGScprQREHVTVKMKHELGVTAVLNFQTEwdviqnssgcnnypepmspeTMFRLYKEAGITYIWIPTPDmS 219
Cdd:cd14567    2 TPILPFLYLGN---ERDAQDIDTLQRLNIGYVLNVTTH--------------------LPLYHEGKGGFRYKRLPATD-S 57

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 220 TEGRIRMLPQAVyllFGLLE----NGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:cd14567   58 NKQNLRQYFEEA---FEFIEeahqSGKGVLVHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKRPII 124
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 239-285 2.22e-05

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: 43.54  E-value: 2.22e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 194332787 239 ENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:cd14513   76 RKGSKVLVHCKMGVSRSASTVIAYAMKEYGWSLEQALEHVKERRSCI 122
DUSP26 cd14578
dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), ...
 202-264 2.32e-05

dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), also called mitogen-activated protein kinase (MAPK) phosphatase 8 (MKP-8) or low-molecular-mass dual-specificity phosphatase 4 (LDP-4), 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. DUSP26 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 a brain phosphatase highly overexpressed in neuroblastoma and has also been identified as a p53 phosphatase, dephosphorylating phospho-Ser20 and phospho-Ser37 in the p53 transactivation domain.


Pssm-ID: 350426 [Multi-domain]  Cd Length: 144  Bit Score: 43.67  E-value: 2.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194332787 202 LYKEAGITYIWI-----PTPDMStegrIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLM 264
Cdd:cd14578   44 YYEGLNIRYLGIeahdsPAFDMS----IHFYPAADFIHRALSQPGGKILVHCAVGVSRSATLVLAYLM 107
DUSP13B cd14577
dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 ...
 138-271 2.45e-05

dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 isoform B (DUSP13B), also called testis- and skeletal-muscle-specific DSP (TMDP) or dual specificity phosphatase SKRP4, 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. DUSP13B 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. DUSP13B inactivates MAPK activation in the order of selectivity, JNK = p38 > ERK in cells. It may play a role in protection from external stress during spermatogenesis.


Pssm-ID: 350425 [Multi-domain]  Cd Length: 163  Bit Score: 44.02  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 138 HFSRILPNIWLGSCPRQREHvtvKMKHELGVTAVLNfqtewdviqNSSGcnnypePMSPETMFRLYKEAGITYIWI---- 213
Cdd:cd14577   17 HVNEVWPNLYLGDAYAARDK---SVLIQLGITHIVN---------AASG------KFHVNTGPKFYRDMNIDYYGVeadd 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194332787 214 -PTPDMStegrIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSL 271
Cdd:cd14577   79 nPFFDLS----VYFYPVARFIRAALSSPNGRVLVHCAMGISRSATLVLAFLMICEDLTL 133
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
 140-285 2.46e-05

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: 43.70  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 140 SRILPNIWLGScprQREHVTVKMKHELGVTAVLNFQTEWDviqnssgcNNYPEPMSPETMfRLYKEAGITYI--WIPTPD 217
Cdd:cd14571    5 SRIFPYLYLGS---EWNAANLEELQRNRVSHILNVTREID--------NFFPERFTYMNI-RVYDEEATQLLphWKETHR 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194332787 218 MSTEGRirmlpqavyllfgllENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:cd14571   73 FIEAAR---------------AQGTRVLVHCKMGVSRSASTVIAYAMKQYGWTLEQALRHVRERRPIV 125
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 144-264 4.10e-05

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: 42.97  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 144 PNIWLGScprqrEHVTVKMKH--ELGVTAVLNfqtewdVIQNSSGCNNYPEPMSpetmfrlYKEAGITYIWIPTPDMSTE 221
Cdd:cd14515    6 PGIYIGD-----ESTAKNKAKlkKLGITHVLN------AAEGKKNGEVNTNAKF-------YKGSGIIYLGIPASDLPTF 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 194332787 222 gRIRML--PQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLM 264
Cdd:cd14515   68 -DISQYfdEAADFIDKALSDPGGKVLVHCVEGVSRSATLVLAYLM 111
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 193-285 1.26e-04

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: 40.80  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 193 PMSP-ETMFRLYKEAGITYIWIPTPDMsTEGRIRMLPQAvyllfglLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSL 271
Cdd:cd14494   15 PLSPlEADSRFLKQLGVTTIVDLTLAM-VDRFLEVLDQA-------EKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSA 86

                         90
                 ....*....|....
gi 194332787 272 RKVQYFLASRRPAV 285
Cdd:cd14494   87 EEAVRIVRLIRPGG 100
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 138-264 1.62e-04

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: 41.68  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 138 HFSRILPNIWLGSCPRQREhvtvKMK-HELGVTAVLNfqtewdviqnSSGCNNYpepMSPETMFRLYKEAGITYIWIPTP 216
Cdd:cd14579   20 HCNEVYPRIYVGNASVAQN----IMRlQRLGITHVLN----------AAEGKSF---MHVNTNAEFYEDTGITYHGIKAN 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 194332787 217 DMSTEGRIRMLPQAV-YLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLM 264
Cdd:cd14579   83 DTQHFNLSAYFEEAAdFIDKALAQKNGRVLVHCREGYSRSPTLVIAYLM 131
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
 140-265 2.09e-04

dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; This family is composed of Saccharomyces cerevisiae dual specificity protein phosphatase Yvh1 and similar fungal proteins. Yvh1 could function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It regulates cell growth, sporulation, and glycogen accumulation. It plays an important role in ribosome assembly. Yvh1 associates transiently with late pre-60S particles and is required for the release of the nucleolar/nuclear pre-60S factor Mrt4, which is necessary to construct a translation-competent 60S subunit and mature ribosome stalk. Yvh1 contains an N-terminal catalytic dual specificity phosphatase domain and a C-terminal tail.


Pssm-ID: 350368 [Multi-domain]  Cd Length: 153  Bit Score: 40.76  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 140 SRILPNIWLGSCPRQREHVTVKmkhELGVTAVLNfqtewdVIqnssgcnnyPEPMsPETMFRLYKeagitYIWIPTPDMS 219
Cdd:cd14518    2 SRILGGLYLGGIEPLNRNRLLK---AENITHILS------VI---------PGDV-PEEYFKGYE-----HKQIEIDDVE 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194332787 220 TEGRIRMLPQAV-YLLFGLLENGHT----------VYVHCNAGVGRSTAAVCGFLMY 265
Cdd:cd14518   58 DENILQHFPETNrFIDSALFGNGKDedeekkhggaVLVHCAMGKSRSVTVVIAYLMY 114
DSP_fungal_PPS1 cd14516
dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; ...
 140-287 7.19e-04

dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; This subfamily contains fungal proteins with similarity to dual specificity protein phosphatase PPS1 from Saccharomyces cerevisiae, which has a role in the DNA synthesis phase of the cell cycle. As a dual specificity protein phosphatase, PPS1 functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It contains a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350366 [Multi-domain]  Cd Length: 177  Bit Score: 39.56  E-value: 7.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 140 SRILPNIWLGS-----------------------CPRQREHVTVKMKHELGVTAVLNFqteWDVIQNSSGCNNYPEPMSP 196
Cdd:cd14516    8 SRILPHLYLGSlnhasnatlleslgithivsvgeSPSWFSNLKIKYIFDFSLQDLSNL---DSNSEGSLWAAEYKGLISV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 197 ETMFRLyKEAGItyiwiptpDMSTEGRIRMLP--QAVYLLfgllenGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKV 274
Cdd:cd14516   85 LYIHNL-KDDGI--------DSLLPQLTDALDfiQKARLL------GGKTLVHCRVGVSRSATVVIAEVMKHLRMSLVDA 149

                        170
                 ....*....|...
gi 194332787 275 QYFLASRRPAVYI 287
Cdd:cd14516  150 YLFVRVRRLNIII 162
DSP_slingshot_1 cd14570
dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein ...
 239-282 8.94e-04

dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein phosphatase slingshot homolog 1 (SSH1), also called SSH-like protein 1, 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. SSH1 links NOD1 signaling to actin remodeling, facilitating the changes that leads to NF-kappaB activation and innate immune responses. There are at least two human SSH1 isoforms reported: hSSH-1L (long) and hSSH-1S (short). 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. They also contain C-terminal tails, differing in the lengths of the tail.


Pssm-ID: 350418 [Multi-domain]  Cd Length: 144  Bit Score: 38.90  E-value: 8.94e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 194332787 239 ENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRR 282
Cdd:cd14570   79 KNHSKCLVHCKMGVSRSASTVIAYAMKEFGWSLEKAYNFVKQKR 122
DSP_DUSP1 cd14638
dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual ...
 142-285 9.68e-04

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: 38.89  E-value: 9.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 142 ILPNIWLGSCprqrEHVTVK-MKHELGVTAVLNFqtewdviqnSSGCNNYpepmspetmfrlyKEAGITYIWIPTPDMST 220
Cdd:cd14638    4 ILPFLYLGSA----YHASRKdMLDTLGITALINV---------SANCPNH-------------FEGHYQYKSIPVEDNHK 57

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194332787 221 EGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:cd14638   58 ADISSWFNEAIDFIDSVKNAGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSII 122
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 207-283 1.25e-03

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: 38.50  E-value: 1.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194332787 207 GITYIWIPTPDMSTEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRP 283
Cdd:cd14519   43 DIKYLCIPAADTPEQNISQHFRECINFIHEARLNGGNVLVHCLAGVSRSVTIVAAYLMTVTDLGWRDALKAVRAARP 119
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 211-262 1.89e-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: 39.31  E-value: 1.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 194332787 211 IWIPTPDMSTEGRIRMLPQAVYLLfglLENGHTVYVHCNAGVGrstaavCGF 262
Cdd:cd05305    3 IGIPKEIKNQENRVALTPAGVAEL---VAAGHEVLVEKGAGLG------SGF 45
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
 142-285 1.94e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual specificity protein phosphatase 4 (DUSP4), also called mitogen-activated protein kinase (MAPK) phosphatase 2 (MKP-2), 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. DUSP4 regulates either ERK or c-JUN N-terminal kinase (JNK), depending on the cell type. It dephosphorylates nuclear JNK and induces apoptosis in diffuse large B cell lymphoma (DLBCL) cells. It acts as a negative regulator of macrophage M1 activation and inhibits inflammation during macrophage-adipocyte interaction. It has been linked to different aspects of cancer: it may have a role in the development of ovarian cancers, oesophagogastric rib metastasis, and pancreatic tumours; it may also be a candidate tumor suppressor gene, with its deletion implicated in breast cancer, prostate cancer, and gliomas. DUSP4/MKP-2 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: 350488 [Multi-domain]  Cd Length: 141  Bit Score: 38.09  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 142 ILPNIWLGSCprqrEHVTVK-MKHELGVTAVLNFqtewdviqnSSGCNNYpepmspetmfrlyKEAGITYIWIPTPDMST 220
Cdd:cd14640    4 ILPFLYLGSA----YHAARRdMLDALGITALLNV---------SSDCPNH-------------FEGHYQYKCIPVEDNHK 57

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194332787 221 EGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:cd14640   58 ADISSWFMEAIEYIDSVKDCNGRVLVHCQAGISRSATICLAYLMMKKRVRLEEAFEFVKQRRSII 122
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
 20-87 2.29e-03

CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. 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: 99882 [Multi-domain]  Cd Length: 101  Bit Score: 36.77  E-value: 2.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194332787  20 VLGSRKEMGSWDPQYAV-PM-------KPTrcplsttepsfWVGEVLLeePYTDTFWFKFIKKES-GALIWEGNGPH 87
Cdd:cd05807   22 LVGNVHELGNWDPSKAIgPFfnqvvyqYPN-----------WYYDVSV--PAGTTIEFKFIKKNGdNTVTWESGSNH 85
CBM20_water_dikinase cd05818
Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 ...
 20-83 2.39e-03

Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in the chloroplast-encoded phosphoglucan water dikinase, one of two enzymes involved in the phosphorylation of plant starches. In addition to the CBM20 domain, phosphoglucan water dikinase contains a C-terminal pyruvate binding domain. 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: 99892  Cd Length: 92  Bit Score: 36.71  E-value: 2.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194332787  20 VLGSRKEMGSWDPQyavpmkptrCPLSTTEpSFWVGEvlLEEPYTDTFWFKF-IKKESGALIWEG 83
Cdd:cd05818   20 ILGSTKELGSWKKK---------VPMNWTE-NGWVCD--LELDGGELVEYKFvIVKRDGSVIWEG 72
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 210-285 4.73e-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: 4.73e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194332787 210 YIWIPTPDMSTEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRPAV 285
Cdd:cd14639   47 YKWIPVEDSHTADISSHFQEAIDFIDCVRRAGGKVLVHCEAGISRSPTICMAYLMKTKRFRLEEAFDYIKQRRSLI 122
DUPD1 cd14575
dual specificity phosphatase and pro isomerase domain containing 1; Dual specificity ...
 129-264 5.51e-03

dual specificity phosphatase and pro isomerase domain containing 1; Dual specificity phosphatase and pro isomerase domain containing 1 (DUPD1) was initially named as such because computational prediction appeared to encode a protein of 446 amino acids in length that included two catalytic domains: a proline isomerase and a dual specificity phosphatase (DUSP). However, it was subsequently shown that the true open reading frame only encompassed the DUSP domain and the gene product was therefore renamed DUSP27. This is distinct from inactive DUSP27. DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). DUPD1/DUSP27 has been shown to have catalytic activity with preference for phosphotyrosine over phosphothreonine and phosphoserine residues. It associates with the short form of the prolactin (PRL) receptor and plays a role in PRL-mediated MAPK inhibition in ovarian cells.


Pssm-ID: 350423 [Multi-domain]  Cd Length: 160  Bit Score: 37.11  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 129 FHFAGTQAMHFSRILPNIWLGSCPRQREHVTVKmkhELGVTAVLNF-QTEWDViqnSSGCNNYPEpmspeTMFRLYkeaG 207
Cdd:cd14575    1 FWKGGPKYTHVNEVWPGLYIGDEKTALDRYSLQ---KLGITHILNAaHGKWNV---DTGAEYYKD-----MTIHYY---G 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194332787 208 ITYIWIPTPDMStegrIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLM 264
Cdd:cd14575   67 VEADDLPTFNLS----QFFYSAAEFIHQALSDPHNKLLVHCVMGRSRSATLVLAYLM 119
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 207-283 6.13e-03

dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity protein phosphatase 18 (DUSP18), dual specificity protein phosphatase 21 (DUSP21), 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. DUSP18, also called low molecular weight dual specificity phosphatase 20 (LMW-DSP20), is a catalytically active phosphatase with a preference for phosphotyrosine over phosphoserine/threonine oligopeptides in vitro. In vivo, it has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP21 is also called low molecular weight dual specificity phosphatase 21 (LMW-DSP21). Its gene has been identified as a potential therapeutic target in human hepatocellular carcinoma. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane.


Pssm-ID: 350421 [Multi-domain]  Cd Length: 158  Bit Score: 36.69  E-value: 6.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194332787 207 GITYIWIPTPDmSTEGRIR-MLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRP 283
Cdd:cd14573   45 GIEYLHVPVAD-SPDTRLRdYFDPIADKIHTVEARGGRTLLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTWVKSCRP 121
DSP_STYXL1 cd14517
dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; ...
 202-273 8.33e-03

dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; Serine/threonine/tyrosine interacting like 1 (STYXL1), also known as DUSP24 and MK-STYX, is a catalytically inactive phosphatase with homology to the mitogen-activated protein kinase (MAPK) phosphatases (MKPs). STYXL1 plays a role in regulating pathways by competing with active phosphatases for binding to MAPKs. Similar to MKPs, STYXL1 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, however its C-terminal dual specificity phosphatase-like domain is a pseudophosphatase missing the catalytic cysteine.


Pssm-ID: 350367 [Multi-domain]  Cd Length: 155  Bit Score: 36.49  E-value: 8.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194332787 202 LYKEAGITYIWIPTPDMSTEGRIRMLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRK 273
Cdd:cd14517   51 LFKSGNDQVLHIPVEDSVEADLLSFFERACSFIDKHKNNGSRVLVFSTLGISRSVAVAIAYLMYHYKWSLKD 122
DSP_fungal_SDP1-like cd14521
dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, ...
 144-283 9.38e-03

dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, and similar proteins; This family is composed of fungal dual specificity protein phosphatases (DUSPs) including Saccharomyces cerevisiae SDP1 and MSG5, and Schizosaccharomyces pombe Pmp1. 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. SDP1 is oxidative stress-induced and dephosphorylates MAPK substrates such as SLT2. MSG5 dephosphorylates the Fus3 and Slt2 MAPKs operating in the mating and cell wall integrity (CWI) pathways, respectively. Pmp1 is responsible for dephosphorylating the CWI MAPK Pmk1. These phosphatases bind to their target MAPKs through a conserved IYT motif located outside of the dual specificity phosphatase domain.


Pssm-ID: 350371 [Multi-domain]  Cd Length: 155  Bit Score: 36.15  E-value: 9.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194332787 144 PNIWLGSCPRQREhvtvkmkhelgvtaVLNFqtewDVIQN-SSGCNNYPEPMSPETMFRLYKEAG-----ITYIWIP--- 214
Cdd:cd14521   11 PNIYLYSEPTLEE--------------ASSF----DVVINvAKEVKNPFLSDASLAEKEKTILPGqqvknPEYIHVPwdh 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194332787 215 TPDMSTEgrirmLPQAVYLLFGLLENGHTVYVHCNAGVGRSTAAVCGFLMYVIGWSLRKVQYFLASRRP 283
Cdd:cd14521   73 NSQIQKD-----LPKLTSIIEDATQSGKKVLIHCQCGVSRSASLIIAYIMKKLGLSLNDAYDLLKSRSP 136
 
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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