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Conserved domains on  [gi|116063575|ref|NP_034276|]
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laforin [Mus musculus]

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 ...
 154-311 4.38e-78

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: 235.17  E-value: 4.38e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 154 MHYSRILPNIWLGSCPRQLEHVTIKLKHelGVTAVMNFQTEWDIiqnssgcnrYPEPMTPDTMMKLYKEEGLSYIWMPTP 233
Cdd:cd14526    1 LNYSRILPNLIVGSCPQNPEDVDRLKKE--GVTAVLNLQTDSDM---------EYWGVDIDSIRKACKESGIRYVRLPIR 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116063575 234 DMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAvYIDEDALAQ 311
Cdd:cd14526   70 DFDTEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPC-GPDEEAIRG 146
CBM20_laforin cd05806
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 1-128 8.42e-54

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: 171.93  E-value: 8.42e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575   1 MLFRFGVVVPPAvaGARQELLLAGSRPELGRWEPHGAVRLRPAGTAAGAaalalQEPGLWLAEVELeayeeaggAEPGRV 80
Cdd:cd05806    1 MLFRFGVVLTFA--DRDTELLVLGSRPELGSWDPQRAVPMRPARKALSP-----QEPSLWLGEVEL--------SEPGSE 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 116063575  81 DTFWYKFLQREPGgELHWEGNGPHHDRCCTYNEDNLVDGVYCLPVGHW 128
Cdd:cd05806   66 DTFWYKFLKREAG-ALIWEGNGPHHDRCCVYDSSNLVDGVYCLPVGHW 112
 
Name Accession Description Interval E-value
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 154-311 4.38e-78

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: 235.17  E-value: 4.38e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 154 MHYSRILPNIWLGSCPRQLEHVTIKLKHelGVTAVMNFQTEWDIiqnssgcnrYPEPMTPDTMMKLYKEEGLSYIWMPTP 233
Cdd:cd14526    1 LNYSRILPNLIVGSCPQNPEDVDRLKKE--GVTAVLNLQTDSDM---------EYWGVDIDSIRKACKESGIRYVRLPIR 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116063575 234 DMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAvYIDEDALAQ 311
Cdd:cd14526   70 DFDTEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPC-GPDEEAIRG 146
CBM20_laforin cd05806
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 1-128 8.42e-54

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: 171.93  E-value: 8.42e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575   1 MLFRFGVVVPPAvaGARQELLLAGSRPELGRWEPHGAVRLRPAGTAAGAaalalQEPGLWLAEVELeayeeaggAEPGRV 80
Cdd:cd05806    1 MLFRFGVVLTFA--DRDTELLVLGSRPELGSWDPQRAVPMRPARKALSP-----QEPSLWLGEVEL--------SEPGSE 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 116063575  81 DTFWYKFLQREPGgELHWEGNGPHHDRCCTYNEDNLVDGVYCLPVGHW 128
Cdd:cd05806   66 DTFWYKFLKREAG-ALIWEGNGPHHDRCCVYDSSNLVDGVYCLPVGHW 112
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
157-303 3.50e-17

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 76.94  E-value: 3.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575   157 SRILPNIWLGSCPRqleHVTIKLKHELGVTAVMNFQTEwdiiqnssgcnrypepmtpdtmMKLYKEEGLSYIWMPTPDMS 236
Cdd:smart00195   2 SEILPHLYLGSYSD---ALNLALLKKLGITHVINVTNE----------------------VPNYNGSDFTYLGVPIDDNT 56

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116063575   237 TEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAVY 303
Cdd:smart00195  57 ETKISPYFPEAVEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIIS 123
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
163-322 2.52e-14

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 68.84  E-value: 2.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 163 IWLGSCPRqleHVTIKLKhELGVTAVMNFQTEWDIIqnssgcnrypepmtpdtmMKLYKEEGLSYIWMPTPDMSTEgRVQ 242
Cdd:COG2453    8 LAGGPLPG---GGEADLK-REGIDAVVSLTEEEELL------------------LGLLEEAGLEYLHLPIPDFGAP-DDE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 243 MLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYvIGWNLRKVQYFIMAKRPAVyidedALAQAQQDFSQKFGK 322
Cdd:COG2453   65 QLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYLVL-LGLSAEEALARVRAARPGA-----VETPAQRAFLERFAK 138
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 163-302 2.13e-13

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: 66.13  E-value: 2.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575  163 IWLGSCPRQLEHVTIKLkhelGVTAVMNFQTEwdiiqnssgCNRYPEpmtpdtmmklykeeGLSYIWMPTPDMSTEGRVQ 242
Cdd:pfam00782   1 LYLGSKPTASDAFLSKL----GITAVINVTRE---------VDLYNS--------------GILYLRIPVEDNHETNISK 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575  243 MLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAV 302
Cdd:pfam00782  54 YLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGI 113
CBM_2 smart01065
Starch binding domain;
4-105 1.74e-10

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 56.59  E-value: 1.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575     4 RFGVVVPPAVAGarQELLLAGSRPELGRWEPHGAVRLRPAGTAAgaaalalqepGLWLAEVELeayeeaggaePGRVDTF 83
Cdd:smart01065   4 TFKVRNGYTQPG--ESVYVVGSVPELGNWNPKKAVPLSPDTDGY----------PLWKGTVSL----------PPAGTTI 61

                           90       100
                   ....*....|....*....|..
gi 116063575    84 WYKFLQREPGGELHWEGNGPHH 105
Cdd:smart01065  62 EYKYVKVDEDGSVTWESGPNRR 83
CBM_20 pfam00686
Starch binding domain;
18-105 4.63e-09

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 53.06  E-value: 4.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575   18 QELLLAGSRPELGRWEPHGAVRLRPagtaagaaALALQEPgLWLAEVELEAYEeaggaepgrvdTFWYKFLQREPGGELH 97
Cdd:pfam00686  15 QSVYIVGSIPELGNWNPKKAIALSA--------SEYSSYP-LWSGTVSLPAGT-----------TIEYKYIKVDSDGSVT 74


                  ....*...
gi 116063575   98 WEgNGPHH 105
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 ...
 154-311 4.38e-78

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: 235.17  E-value: 4.38e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 154 MHYSRILPNIWLGSCPRQLEHVTIKLKHelGVTAVMNFQTEWDIiqnssgcnrYPEPMTPDTMMKLYKEEGLSYIWMPTP 233
Cdd:cd14526    1 LNYSRILPNLIVGSCPQNPEDVDRLKKE--GVTAVLNLQTDSDM---------EYWGVDIDSIRKACKESGIRYVRLPIR 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116063575 234 DMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAvYIDEDALAQ 311
Cdd:cd14526   70 DFDTEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPC-GPDEEAIRG 146
CBM20_laforin cd05806
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 1-128 8.42e-54

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: 171.93  E-value: 8.42e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575   1 MLFRFGVVVPPAvaGARQELLLAGSRPELGRWEPHGAVRLRPAGTAAGAaalalQEPGLWLAEVELeayeeaggAEPGRV 80
Cdd:cd05806    1 MLFRFGVVLTFA--DRDTELLVLGSRPELGSWDPQRAVPMRPARKALSP-----QEPSLWLGEVEL--------SEPGSE 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 116063575  81 DTFWYKFLQREPGgELHWEGNGPHHDRCCTYNEDNLVDGVYCLPVGHW 128
Cdd:cd05806   66 DTFWYKFLKREAG-ALIWEGNGPHHDRCCVYDSSNLVDGVYCLPVGHW 112
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 157-311 1.53e-18

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: 80.28  E-value: 1.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 157 SRILPNIWLGSCP--RQLEhvtiKLKhELGVTAVMNfqtewdiiqnssgCNRYPEPmtpdtmmkLYKEEGLSYIWMPTPD 234
Cdd:cd14498    2 SEILPGLYLGSLDaaQDKE----LLK-KLGITHILN-------------VAGEPPP--------NKFPDGIKYLRIPIED 55

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116063575 235 MSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAVYIDEDALAQ 311
Cdd:cd14498   56 SPDEDILSHFEEAIEFIEEALKKGGKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRPIISPNPGFLKQ 132
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 155-320 5.95e-18

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: 79.23  E-value: 5.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 155 HYSRILPNIWLGSCPrqLEHVTIKLKHELGVTAVMNfqtewdiiqnssgCNRYPEPMTPDTMMKLYKEEGLSYIWMPTPD 234
Cdd:cd14524    1 WYDRIDDTVILGALP--FRSMTVALVAKENVRGVIT-------------MNEEYETRFFCNSKEEWKALGVEQLRLPTVD 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 235 MSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAVyidedALAQAQQ 314
Cdd:cd14524   66 FTGVPSLEDLEKGVDFILKHREKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRPHI-----LLRLSQR 140


                 ....*.
gi 116063575 315 DFSQKF 320
Cdd:cd14524  141 EVLEEF 146
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
157-303 3.50e-17

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 76.94  E-value: 3.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575   157 SRILPNIWLGSCPRqleHVTIKLKHELGVTAVMNFQTEwdiiqnssgcnrypepmtpdtmMKLYKEEGLSYIWMPTPDMS 236
Cdd:smart00195   2 SEILPHLYLGSYSD---ALNLALLKKLGITHVINVTNE----------------------VPNYNGSDFTYLGVPIDDNT 56

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116063575   237 TEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAVY 303
Cdd:smart00195  57 ETKISPYFPEAVEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIIS 123
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 18-118 1.86e-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: 70.79  E-value: 1.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575  18 QELLLAGSRPELGRWEPHGAVRLRPagtaagaaalaLQEPGLWLAEVELEAYEEaggaepgrvDTFWYKFLQREPGGELH 97
Cdd:cd05467   14 QSVYVVGSHPELGNWDPAKALRLNT-----------SNSYPLWTGEIPLPAPEG---------QVIEYKYVIVDDDGNVQ 73

                         90       100
                 ....*....|....*....|.
gi 116063575  98 WEGNGPHHDRCCTYNEDNLVD 118
Cdd:cd05467   74 WESGSNRVLTVPSTSSLIVVD 94
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
163-322 2.52e-14

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 68.84  E-value: 2.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 163 IWLGSCPRqleHVTIKLKhELGVTAVMNFQTEWDIIqnssgcnrypepmtpdtmMKLYKEEGLSYIWMPTPDMSTEgRVQ 242
Cdd:COG2453    8 LAGGPLPG---GGEADLK-REGIDAVVSLTEEEELL------------------LGLLEEAGLEYLHLPIPDFGAP-DDE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 243 MLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYvIGWNLRKVQYFIMAKRPAVyidedALAQAQQDFSQKFGK 322
Cdd:COG2453   65 QLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYLVL-LGLSAEEALARVRAARPGA-----VETPAQRAFLERFAK 138
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 163-302 2.13e-13

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: 66.13  E-value: 2.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575  163 IWLGSCPRQLEHVTIKLkhelGVTAVMNFQTEwdiiqnssgCNRYPEpmtpdtmmklykeeGLSYIWMPTPDMSTEGRVQ 242
Cdd:pfam00782   1 LYLGSKPTASDAFLSKL----GITAVINVTRE---------VDLYNS--------------GILYLRIPVEDNHETNISK 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575  243 MLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAV 302
Cdd:pfam00782  54 YLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGI 113
CBM_2 smart01065
Starch binding domain;
4-105 1.74e-10

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 56.59  E-value: 1.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575     4 RFGVVVPPAVAGarQELLLAGSRPELGRWEPHGAVRLRPAGTAAgaaalalqepGLWLAEVELeayeeaggaePGRVDTF 83
Cdd:smart01065   4 TFKVRNGYTQPG--ESVYVVGSVPELGNWNPKKAVPLSPDTDGY----------PLWKGTVSL----------PPAGTTI 61

                           90       100
                   ....*....|....*....|..
gi 116063575    84 WYKFLQREPGGELHWEGNGPHH 105
Cdd:smart01065  62 EYKYVKVDEDGSVTWESGPNRR 83
CBM_20 pfam00686
Starch binding domain;
18-105 4.63e-09

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 53.06  E-value: 4.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575   18 QELLLAGSRPELGRWEPHGAVRLRPagtaagaaALALQEPgLWLAEVELEAYEeaggaepgrvdTFWYKFLQREPGGELH 97
Cdd:pfam00686  15 QSVYIVGSIPELGNWNPKKAIALSA--------SEYSSYP-LWSGTVSLPAGT-----------TIEYKYIKVDSDGSVT 74


                  ....*...
gi 116063575   98 WEgNGPHH 105
Cdd:pfam00686  75 WE-SGPNR 81
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 156-314 7.68e-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: 7.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 156 YSRILPNIWLGSCPRQLEHVTiklkhelGVTAVMNFQTEWDiiqnssgCNRYPepmtpdtmmklykeegLSYIWMPTPDM 235
Cdd:cd14527    5 YDEVLPGLYLGRWPSADELPP-------GVPAVLDLTAELP-------RPRKR----------------QAYRCVPLLDL 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 236 sTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWL-HYVIGWNLRKVQYFIMAKRPAVYIDE---DALAQ 311
Cdd:cd14527   55 -VAPTPEQLERAVAWIEELRAQGGPVLVHCALGYGRSATVVAAWLlAYGRAKSVAEAEALIRAARPQVVLNPaqrKALEA 133


                 ...
gi 116063575 312 AQQ 314
Cdd:cd14527  134 WSG 136
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 156-302 1.00e-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: 47.16  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 156 YSRILPNIWLGScprqLEHVTIKLKHELGVTAVMNFQTEwdiiqnssgcnrYPEPMTPdtmmklykeeGLSYIWMPTPDM 235
Cdd:cd14514    1 ISQITPHLFLSG----ASAATPPLLLSRGITCIINATTE------------LPDPSYP----------GIEYLRVPVEDS 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116063575 236 STEgrvQMLP--QAVC-LLHALLENGHTVYVHCNAGVGRStAAVCgwLHYVI---GWNLRKVQYFIMAKRPAV 302
Cdd:cd14514   55 PHA---DLSPhfDEVAdKIHQVKRRGGRTLVHCVAGVSRS-ATLC--LAYLMkyeGMTLREAYKHVKAARPII 121
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 157-302 2.13e-06

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: 46.64  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 157 SRILPNIWLGScprQLEHVTIKLKHELGVTAVMNFqtewdiiqnSSGCNRYPepMTPDTmmklykeeglSYIWMPTPDMS 236
Cdd:cd14568    2 TRILPHLYLGS---QRDVLDKDLMQRNGISYVLNV---------SNTCPKPD--FIPDS----------HFLRIPVNDSY 57

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116063575 237 TEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAV 302
Cdd:cd14568   58 CEKLLPWLDKAVEFIEKARASNKRVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRPTI 123
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 158-302 3.38e-06

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


Pssm-ID: 350362 [Multi-domain]  Cd Length: 136  Bit Score: 45.94  E-value: 3.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 158 RILPNIWLGSCPRQLEhvtIKLKHELGVTAVMNFQTewdiiqnssgcnrypepmtpdTMMKLYKEEGLSYIWMPTPDMST 237
Cdd:cd14512    3 RILPNLYLGSQRDSLN---LELMQQLGIGYVLNVSN---------------------TCPNPDFIGLFHYKRIPVNDSFC 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116063575 238 EGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAV 302
Cdd:cd14512   59 QNISPWFDEAIEFIEEAKASNGGVLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRPTI 123
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 214-277 3.41e-06

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: 46.49  E-value: 3.41e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116063575 214 DTMMKLYKEEGLSYIWMPTPDMST---EGRVQMLPQAvclLHALLENGHTVYVHCNAGVGRS-TAAVC 277
Cdd:cd14505   62 PDLLEQYQQAGITWHHLPIPDGGVpsdIAQWQELLEE---LLSALENGKKVLIHCKGGLGRTgLIAAC 126
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 159-302 7.60e-06

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: 45.04  E-value: 7.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 159 ILPNIWLGSCPRQLEHVTIKlKHElgVTAVMNFQtewdiiqnSSGCNRYPEPMT---------PDTMMKLYKEEGLSYIw 229
Cdd:cd14523    5 IKPWLLLSSQDVAHDLETLK-KHK--VTHILNVA--------YGVENAFPDDFTyktisildlPETDITSYFPECFEFI- 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116063575 230 mptpdmsTEGRVQmlpqavcllhalleNGhTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAV 302
Cdd:cd14523   73 -------DEAKSQ--------------DG-VVLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNARPSI 123
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
 159-284 1.02e-05

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: 44.85  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 159 ILPNIWLGSCPRQLEHVTIKlkhELGVTAVMNFqtewdiiqnSSGCnrypepmtPDtmmklYKEEGLSYIWMPTPDMSTE 238
Cdd:cd14641    7 ILPFLFLGSAHHSSRRETLE---SLGITAVLNV---------SSSC--------PN-----YFEGQFQYKSIPVEDSHMA 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 116063575 239 GRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRStAAVCgwLHYVI 284
Cdd:cd14641   62 DISAWFQEAIDFIDSVKNSGGRVLVHCQAGISRS-ATIC--LAYLI 104
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 246-314 2.82e-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: 43.29  E-value: 2.82e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116063575 246 QAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAVYIDEDALAQAQQ 314
Cdd:cd18534   61 EAVDFIEQCRKDKARVLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRPSINLSPAVAKQLQE 129
DSP_DUSP15 cd14582
dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual ...
 208-300 3.72e-05

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: 43.02  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 208 PEPMTPDtmmklykeegLSYIWMPTPDMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWN 287
Cdd:cd14582   41 PQPLLQD----------ITYLRIPLPDTPEAPIKKHFKECISFIHQCRLNGGNCLVHCLAGISRSTTIVVAYVMAVTELS 110

                         90
                 ....*....|...
gi 116063575 288 LRKVQYFIMAKRP 300
Cdd:cd14582  111 WQEVLEAIRAVRP 123
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 223-300 3.99e-05

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: 42.74  E-value: 3.99e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116063575 223 EGLSYIWMPTPDMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRP 300
Cdd:cd14519   42 EDIKYLCIPAADTPEQNISQHFRECINFIHEARLNGGNVLVHCLAGVSRSVTIVAAYLMTVTDLGWRDALKAVRAARP 119
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 159-318 5.52e-05

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


Pssm-ID: 350413 [Multi-domain]  Cd Length: 138  Bit Score: 42.37  E-value: 5.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 159 ILPNIWLGSCprqlEHVTIK-LKHELGVTAVMNFqtewdiiqnSSGCnryPEpmtpdtmmklYKEEGLSYIWMPTPDMST 237
Cdd:cd14565    4 ILPFLYLGSA----YHASRReVLKALGITAVLNV---------SRNC---PN----------HFEDHFQYKSIPVEDSHN 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 238 EGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRStAAVCgwLHYVI---GWNLRKVQYFIMAKRPAVYIDEDALAQAQQ 314
Cdd:cd14565   58 ADISSWFEEAIGFIDKVKASGGRVLVHCQAGISRS-ATIC--LAYLMttrRVRLNEAFDYVKQRRSVISPNFNFMGQLLQ 134


                 ....
gi 116063575 315 DFSQ 318
Cdd:cd14565  135 YESQ 138
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
 157-313 7.00e-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: 42.16  E-value: 7.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 157 SRILPNIWLGScprQLEHVTIKLKHELGVTAVMNFQTEWDiiqnssgcNRYPEPMTPDTMmKLYKEEGLSYI--WMPTPD 234
Cdd:cd14571    5 SRIFPYLYLGS---EWNAANLEELQRNRVSHILNVTREID--------NFFPERFTYMNI-RVYDEEATQLLphWKETHR 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116063575 235 MSTEGRVQmlpqavcllhallenGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAVYIDEDALAQAQ 313
Cdd:cd14571   73 FIEAARAQ---------------GTRVLVHCKMGVSRSASTVIAYAMKQYGWTLEQALRHVRERRPIVQPNPGFLRQLQ 136
DUSP22 cd14581
dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), ...
 223-286 8.06e-05

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


Pssm-ID: 350429 [Multi-domain]  Cd Length: 149  Bit Score: 42.09  E-value: 8.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116063575 223 EGLSYIWMPTPDMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYV--IGW 286
Cdd:cd14581   45 EGMTYLCIPAADSPSQNLTQHFKESIKFIHECRLRGEGCLVHCLAGVSRSVTLVVAYIMTVtdFGW 110
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 181-300 8.56e-05

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: 43.11  E-value: 8.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 181 HELGVTAVMNFQTEWDIIQNSSGCNR-----YPepmtPDTMMklykEEGLSYIWMPTPDMSTEGRVQMLPQAVCLLHALL 255
Cdd:cd14506   36 KEKGIKTVINLQEPGEHASCGPGLEPesgfsYL----PEAFM----RAGIYFYNFGWKDYGVPSLTTILDIVKVMAFALQ 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 116063575 256 EnGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRP 300
Cdd:cd14506  108 E-GGKVAVHCHAGLGRTGVLIACYLVYALRMSADQAIRLVRSKRP 151
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 18-100 1.13e-04

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: 40.43  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575  18 QELLLAGSRPELGRWEPHGAVRLRPagtaagaaalalQEPGLWLAEVELEAyeeaggaepgrvDT-FWYKFLQREPGGEL 96
Cdd:cd05808   15 QNVYVVGNVPELGNWSPANAVALSA------------ATYPVWSGTVDLPA------------GTaIEYKYIKKDGSGTV 70


                 ....
gi 116063575  97 HWEG 100
Cdd:cd05808   71 TWES 74
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 157-319 1.18e-04

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: 41.55  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 157 SRILPNIWLGsCPRQLEHVTIKLKHELGVtavmnfqtewdIIQNSSGCnryPEP-MTPDTmmklykeeglSYIWMPTPDM 235
Cdd:cd14646    4 TRILPHLYLG-CQRDVLNKELMQQNGIGY-----------VLNASNTC---PKPdFIPES----------HFLRVPVNDS 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 236 STEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAVYIDEDALAQAqQD 315
Cdd:cd14646   59 FCEKILPWLDKSVDFIEKAKASNGRVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPTISPNFNFLGQL-LD 137


                 ....
gi 116063575 316 FSQK 319
Cdd:cd14646  138 FEKK 141
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 212-302 1.19e-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: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 212 TPDTMMKLYKEEGLSYIWMPTPDMSTEgrvqmlpqAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKV 291
Cdd:cd14494   18 PLEADSRFLKQLGVTTIVDLTLAMVDR--------FLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEA 89

                         90
                 ....*....|.
gi 116063575 292 QYFIMAKRPAV 302
Cdd:cd14494   90 VRIVRLIRPGG 100
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 212-302 1.47e-04

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: 41.15  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 212 TPDTMMKLYKEEGLSYIWMPTPDMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKV 291
Cdd:cd14566   34 TPNLPNTFEEDGGFKYLQIPIDDHWSQNLSAFFPEAISFIDEARSKKCGVLVHCLAGISRSVTVTVAYLMQKLHLSLNDA 113

                         90
                 ....*....|.
gi 116063575 292 QYFIMAKRPAV 302
Cdd:cd14566  114 YDFVKKRKSNI 124
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 238-270 1.86e-04

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: 42.78  E-value: 1.86e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 116063575 238 EGRVQMLPQAVcllHALLENGHTVYVHCNAGVG 270
Cdd:cd05305   13 ENRVALTPAGV---AELVAAGHEVLVEKGAGLG 42
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 159-314 2.57e-04

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: 40.78  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 159 ILPNIWLGS----CPRQLEHVtiklkHELGVTAVMNfqtewdIIQNSSGcnRYPEPMTPDtmmklykeeGLSYIWMPTPD 234
Cdd:cd14522    8 ILPGLYLGPysaaMKSKLEVL-----LKHGITHIVC------VRQNIEA--NFIKPNFPD---------HFRYLVLDVAD 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 235 MSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVcgwLHYVIgwnlrkvQYFIMAKRpavyideDALAQAQQ 314
Cdd:cd14522   66 NPTENIIRHFPTVKEFIDDCLQTGGKVLVHGNAGISRSAALV---IAYIM-------ETYGLSYR-------DAFAYVQQ 128
DSP_fungal_PPS1 cd14516
dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; ...
 157-277 4.41e-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: 40.33  E-value: 4.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 157 SRILPNIWLGScprqLEHV-TIKLKHELGVTAV------------MNFQTEWDIiqnSSGCNRYPEPMTPDTMMKLYKEE 223
Cdd:cd14516    8 SRILPHLYLGS----LNHAsNATLLESLGITHIvsvgespswfsnLKIKYIFDF---SLQDLSNLDSNSEGSLWAAEYKG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 116063575 224 GLSYIWMptPDMSTEGRVQMLPQ-AVCL--LHALLENGHTVYVHCNAGVGRStAAVC 277
Cdd:cd14516   81 LISVLYI--HNLKDDGIDSLLPQlTDALdfIQKARLLGGKTLVHCRVGVSRS-ATVV 134
DSP_DUSP9 cd14644
dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual ...
 158-321 6.97e-04

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: 39.60  E-value: 6.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 158 RILPNIWLGSCPrqlEHVTIKLKHELGVTAVMNfqtewdiiqnssgcnrypepMTPDTMMKLYKEEGLSYIWMPTPDMST 237
Cdd:cd14644    5 QILPNLYLGSAR---DSANLETLAKLGIRYILN--------------------VTPNLPNFFEKNGDFHYKQIPISDHWS 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 238 EGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAVYIDEDALAQAqQDFS 317
Cdd:cd14644   62 QNLSQFFPEAIEFIDEALSQNCGVLVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDLVKRKKSNISPNFNFMGQL-LDFE 140


                 ....
gi 116063575 318 QKFG 321
Cdd:cd14644  141 KSLG 144
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 157-302 7.55e-04

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


Pssm-ID: 350415 [Multi-domain]  Cd Length: 152  Bit Score: 39.35  E-value: 7.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 157 SRILPNIWLGScprQLEHVTIKLKHELGVTAVMNfqtewdiiqnssgcnrypepMTPDTMMKLYKEEGLSYIWMPTPDMS 236
Cdd:cd14567    2 TPILPFLYLGN---ERDAQDIDTLQRLNIGYVLN--------------------VTTHLPLYHEGKGGFRYKRLPATDSN 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116063575 237 TEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAV 302
Cdd:cd14567   59 KQNLRQYFEEAFEFIEEAHQSGKGVLVHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKRPII 124
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 238-270 1.06e-03

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440450 [Multi-domain]  Cd Length: 372  Bit Score: 40.38  E-value: 1.06e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 116063575 238 EGRVQMLPQAVcllHALLENGHTVYVHCNAGVG 270
Cdd:COG0686   13 ENRVALTPAGV---RELVAAGHEVLVETGAGLG 42
AlaDh_PNT_N pfam05222
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ...
 238-272 1.26e-03

Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 461595 [Multi-domain]  Cd Length: 135  Bit Score: 38.56  E-value: 1.26e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 116063575  238 EGRVQMLPQAVcllHALLENGHTVYVHCNAGVGRS 272
Cdd:pfam05222  10 ERRVALTPAGV---KKLVKLGHEVLVESGAGLGAG 41
DSP_DUSP8 cd14645
dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual ...
 157-311 4.47e-03

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


Pssm-ID: 350493 [Multi-domain]  Cd Length: 151  Bit Score: 37.30  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575 157 SRILPNIWLGScprQLEHVTIKLKHELGVTAVMNfqtewdiiqNSSGCNRyPEPMTPDTMMKLykeeglsyiwmPTPDMS 236
Cdd:cd14645   13 TRILPHLYLGS---QKDVLNKDLMAQNGITYVLN---------ASNSCPK-PDFICESHFMRI-----------PVNDNY 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116063575 237 TEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAVYIDEDALAQ 311
Cdd:cd14645   69 CEKLLPWLDKSIEFIDKAKVSNCRVIVHCLAGISRSATIAIAYIMKTMGLSSDDAYRFVKDRRPSISPNFNFLGQ 143
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 18-101 4.92e-03

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


Pssm-ID: 99886 [Multi-domain]  Cd Length: 106  Bit Score: 36.10  E-value: 4.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063575  18 QELLLAGSRPELGRWEPHGAVRL--------RPagtaagaaalalqepgLWLAEVELeayeEAGgaepgrvDTFWYKFLQ 89
Cdd:cd05811   21 ENIKIVGSIPQLGNWDTSSAVALsasqytssNP----------------LWSVTIPL----PAG-------TSFEYKFIR 73

                         90
                 ....*....|..
gi 116063575  90 REPGGELHWEGN 101
Cdd:cd05811   74 KESDGSVTWESD 85
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 256-302 7.06e-03

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


Pssm-ID: 350363 [Multi-domain]  Cd Length: 139  Bit Score: 36.22  E-value: 7.06e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 116063575 256 ENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAV 302
Cdd:cd14513   76 RKGSKVLVHCKMGVSRSASTVIAYAMKEYGWSLEQALEHVKERRSCI 122
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 217-271 8.94e-03

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 36.10  E-value: 8.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 116063575 217 MKLYKEEGLSYIWMPTPDMSTEGRVQMLpQAVCLLHALLENGHTVYVHCNAGVGR 271
Cdd:cd14504   42 EHSDTCPGLRYHHIPIEDYTPPTLEQID-EFLDIVEEANAKNEAVLVHCLAGKGR 95
 
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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