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Conserved domains on  [gi|1334928398|ref|NP_001346993|]
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laforin isoform d [Homo sapiens]

Protein Classification

DSP_laforin-like domain-containing protein( domain architecture ID 12998397)

DSP_laforin-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 17-174 1.13e-77

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: 228.62  E-value: 1.13e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  17 MHYSRILPNIWLGSCPRQVEHVTIKLKHelGITAVMNFQTEWDIvqnssgcnrYPEPMTPDTMIKLYREEGLAYIWMPTP 96
Cdd:cd14526     1 LNYSRILPNLIVGSCPQNPEDVDRLKKE--GVTAVLNLQTDSDM---------EYWGVDIDSIRKACKESGIRYVRLPIR 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1334928398  97 DMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAvYIDEEALAR 174
Cdd:cd14526    70 DFDTEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPC-GPDEEAIRG 146
 
Name Accession Description Interval E-value
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 17-174 1.13e-77

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: 228.62  E-value: 1.13e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  17 MHYSRILPNIWLGSCPRQVEHVTIKLKHelGITAVMNFQTEWDIvqnssgcnrYPEPMTPDTMIKLYREEGLAYIWMPTP 96
Cdd:cd14526     1 LNYSRILPNLIVGSCPQNPEDVDRLKKE--GVTAVLNLQTDSDM---------EYWGVDIDSIRKACKESGIRYVRLPIR 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1334928398  97 DMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAvYIDEEALAR 174
Cdd:cd14526    70 DFDTEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPC-GPDEEAIRG 146
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
20-166 4.37e-19

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 79.25  E-value: 4.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398   20 SRILPNIWLGSCPRqveHVTIKLKHELGITAVMNFQTEwdivqnssgcnrypepmtpdtmIKLYREEGLAYIWMPTPDMS 99
Cdd:smart00195   2 SEILPHLYLGSYSD---ALNLALLKKLGITHVINVTNE----------------------VPNYNGSDFTYLGVPIDDNT 56

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1334928398  100 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVY 166
Cdd:smart00195  57 ETKISPYFPEAVEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIIS 123
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
20-185 1.29e-16

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 72.70  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  20 SRILPN-IWLGSCPRQVEHVTiklkHELGITAVMNFQTEWDIVqnssgcnrypepmtpdtmIKLYREEGLAYIWMPTPDM 98
Cdd:COG2453     1 SWIIPGlLAGGPLPGGGEADL----KREGIDAVVSLTEEEELL------------------LGLLEEAGLEYLHLPIPDF 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  99 STEgRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLqyVM-GWN----LRKVQyflmAKRPAVyideeALA 173
Cdd:COG2453    59 GAP-DDEQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYL--VLlGLSaeeaLARVR----AARPGA-----VET 126

                         170
                  ....*....|..
gi 1334928398 174 RAQEDFFQKFGK 185
Cdd:COG2453   127 PAQRAFLERFAK 138
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 26-165 6.90e-15

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


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 67.67  E-value: 6.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  26 IWLGSCPRQVEHVTIKLkhelGITAVMNFQTEwdivqnssgCNRYPEpmtpdtmiklyreeGLAYIWMPTPDMSTEGRVQ 105
Cdd:pfam00782   1 LYLGSKPTASDAFLSKL----GITAVINVTRE---------VDLYNS--------------GILYLRIPVEDNHETNISK 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398 106 MLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 165
Cdd:pfam00782  54 YLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGI 113
 
Name Accession Description Interval E-value
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 17-174 1.13e-77

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: 228.62  E-value: 1.13e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  17 MHYSRILPNIWLGSCPRQVEHVTIKLKHelGITAVMNFQTEWDIvqnssgcnrYPEPMTPDTMIKLYREEGLAYIWMPTP 96
Cdd:cd14526     1 LNYSRILPNLIVGSCPQNPEDVDRLKKE--GVTAVLNLQTDSDM---------EYWGVDIDSIRKACKESGIRYVRLPIR 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1334928398  97 DMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAvYIDEEALAR 174
Cdd:cd14526    70 DFDTEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPC-GPDEEAIRG 146
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 20-169 1.52e-19

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


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 80.28  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  20 SRILPNIWLGSCpRQVEHVTIkLKhELGITAVMNFQTEwdivqnssgcnrypepmtpdtMIKLYREEGLAYIWMPTPDMS 99
Cdd:cd14498     2 SEILPGLYLGSL-DAAQDKEL-LK-KLGITHILNVAGE---------------------PPPNKFPDGIKYLRIPIEDSP 57

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398 100 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDE 169
Cdd:cd14498    58 DEDILSHFEEAIEFIEEALKKGGKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRPIISPNP 127
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
20-166 4.37e-19

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 79.25  E-value: 4.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398   20 SRILPNIWLGSCPRqveHVTIKLKHELGITAVMNFQTEwdivqnssgcnrypepmtpdtmIKLYREEGLAYIWMPTPDMS 99
Cdd:smart00195   2 SEILPHLYLGSYSD---ALNLALLKKLGITHVINVTNE----------------------VPNYNGSDFTYLGVPIDDNT 56

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1334928398  100 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVY 166
Cdd:smart00195  57 ETKISPYFPEAVEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIIS 123
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 18-183 1.27e-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: 73.06  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  18 HYSRILPNIWLGSCPrqVEHVTIKLKHELGITAVMNfqtewdivqnssgCNRYPEPMTPDTMIKLYREEGLAYIWMPTPD 97
Cdd:cd14524     1 WYDRIDDTVILGALP--FRSMTVALVAKENVRGVIT-------------MNEEYETRFFCNSKEEWKALGVEQLRLPTVD 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  98 MSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVyideeALARAQE 177
Cdd:cd14524    66 FTGVPSLEDLEKGVDFILKHREKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRPHI-----LLRLSQR 140


                  ....*.
gi 1334928398 178 DFFQKF 183
Cdd:cd14524   141 EVLEEF 146
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
20-185 1.29e-16

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 72.70  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  20 SRILPN-IWLGSCPRQVEHVTiklkHELGITAVMNFQTEWDIVqnssgcnrypepmtpdtmIKLYREEGLAYIWMPTPDM 98
Cdd:COG2453     1 SWIIPGlLAGGPLPGGGEADL----KREGIDAVVSLTEEEELL------------------LGLLEEAGLEYLHLPIPDF 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  99 STEgRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLqyVM-GWN----LRKVQyflmAKRPAVyideeALA 173
Cdd:COG2453    59 GAP-DDEQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYL--VLlGLSaeeaLARVR----AARPGA-----VET 126

                         170
                  ....*....|..
gi 1334928398 174 RAQEDFFQKFGK 185
Cdd:COG2453   127 PAQRAFLERFAK 138
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 26-165 6.90e-15

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


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 67.67  E-value: 6.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  26 IWLGSCPRQVEHVTIKLkhelGITAVMNFQTEwdivqnssgCNRYPEpmtpdtmiklyreeGLAYIWMPTPDMSTEGRVQ 105
Cdd:pfam00782   1 LYLGSKPTASDAFLSKL----GITAVINVTRE---------VDLYNS--------------GILYLRIPVEDNHETNISK 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398 106 MLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 165
Cdd:pfam00782  54 YLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGI 113
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 19-143 1.65e-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: 51.12  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  19 YSRILPNIWLGSCPRQVEHVTiklkhelGITAVMnfqtewDIvqnssgCNRYPepmtpdtmiklYREEGLAYIWMPTPDM 98
Cdd:cd14527     5 YDEVLPGLYLGRWPSADELPP-------GVPAVL------DL------TAELP-----------RPRKRQAYRCVPLLDL 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1334928398  99 sTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWL 143
Cdd:cd14527    55 -VAPTPEQLERAVAWIEELRAQGGPVLVHCALGYGRSATVVAAWL 98
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 20-165 2.78e-08

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


Pssm-ID: 350416 [Multi-domain]  Cd Length: 140  Bit Score: 50.49  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  20 SRILPNIWLGScprQVEHVTIKLKHELGITAVMNFqtewdivqnSSGCNRYPepMTPDTmiklyreeglAYIWMPTPDMS 99
Cdd:cd14568     2 TRILPHLYLGS---QRDVLDKDLMQRNGISYVLNV---------SNTCPKPD--FIPDS----------HFLRIPVNDSY 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1334928398 100 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 165
Cdd:cd14568    58 CEKLLPWLDKAVEFIEKARASNKRVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRPTI 123
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 19-165 3.57e-07

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


Pssm-ID: 350364 [Multi-domain]  Cd Length: 133  Bit Score: 47.16  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  19 YSRILPNIWLGSCprqvEHVTIKLKHELGITAVMNFQTEwdivqnssgcnrYPEPMTPdtmiklyreeGLAYIWMPTPDM 98
Cdd:cd14514     1 ISQITPHLFLSGA----SAATPPLLLSRGITCIINATTE------------LPDPSYP----------GIEYLRVPVEDS 54

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1334928398  99 STEgrvQMLP--QAVC-LLHALLEKGHIVYVHCNAGVGRStAAVCgwLQYVM---GWNLRKVQYFLMAKRPAV 165
Cdd:cd14514    55 PHA---DLSPhfDEVAdKIHQVKRRGGRTLVHCVAGVSRS-ATLC--LAYLMkyeGMTLREAYKHVKAARPII 121
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 22-165 3.72e-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: 47.35  E-value: 3.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  22 ILPNIWLGSCPRQVEHVTIKlKHElgITAVMNFQtewdivqnSSGCNRYPEPMT---------PDTMIKLYREEGLAYIw 92
Cdd:cd14523     5 IKPWLLLSSQDVAHDLETLK-KHK--VTHILNVA--------YGVENAFPDDFTyktisildlPETDITSYFPECFEFI- 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1334928398  93 mptpdmsTEGRVQmlpqavcllhallekGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 165
Cdd:cd14523    73 -------DEAKSQ---------------DGVVLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNARPSI 123
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 21-165 1.29e-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: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  21 RILPNIWLGSCpRQVEHvtIKLKHELGITAVMNFQTewdivqnssgcnrypepmtpdTMIKLYREEGLAYIWMPTPDMST 100
Cdd:cd14512     3 RILPNLYLGSQ-RDSLN--LELMQQLGIGYVLNVSN---------------------TCPNPDFIGLFHYKRIPVNDSFC 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1334928398 101 EGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 165
Cdd:cd14512    59 QNISPWFDEAIEFIEEAKASNGGVLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRPTI 123
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
 22-147 5.60e-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: 44.08  E-value: 5.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  22 ILPNIWLGSCPRQVEHVTIKlkhELGITAVMNFqtewdivqnSSGCnrypepmtPDtmiklYREEGLAYIWMPTPDMSTE 101
Cdd:cd14641     7 ILPFLFLGSAHHSSRRETLE---SLGITAVLNV---------SSSC--------PN-----YFEGQFQYKSIPVEDSHMA 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1334928398 102 GRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRStAAVCgwLQYVM 147
Cdd:cd14641    62 DISAWFQEAIDFIDSVKNSGGRVLVHCQAGISRS-ATIC--LAYLI 104
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 21-165 6.97e-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: 43.85  E-value: 6.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  21 RILPNIWLGScprqVEHVT-IKLKHELGITAVMNfqtewdivqnssgcnrypepMTPDTMIKLYREEGLAYIWMPTPDMS 99
Cdd:cd14566     3 EILPFLYLGN----AKDSAnIDLLKKYNIKYILN--------------------VTPNLPNTFEEDGGFKYLQIPIDDHW 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1334928398 100 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 165
Cdd:cd14566    59 SQNLSAFFPEAISFIDEARSKKCGVLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKRKSNI 124
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 22-147 8.74e-06

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


Pssm-ID: 350413 [Multi-domain]  Cd Length: 138  Bit Score: 43.53  E-value: 8.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  22 ILPNIWLGSCprqvEHVTIK-LKHELGITAVMNFqtewdivqnSSGCNRYPEPMtpdtmiklyreegLAYIWMPTPDMST 100
Cdd:cd14565     4 ILPFLYLGSA----YHASRReVLKALGITAVLNV---------SRNCPNHFEDH-------------FQYKSIPVEDSHN 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1334928398 101 EGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRStAAVCgwLQYVM 147
Cdd:cd14565    58 ADISSWFEEAIGFIDKVKASGGRVLVHCQAGISRS-ATIC--LAYLM 101
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 109-177 1.33e-05

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


Pssm-ID: 350510 [Multi-domain]  Cd Length: 130  Bit Score: 42.91  E-value: 1.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1334928398 109 QAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDEEALARAQE 177
Cdd:cd18534    61 EAVDFIEQCRKDKARVLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRPSINLSPAVAKQLQE 129
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 20-165 2.81e-05

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


Pssm-ID: 350494 [Multi-domain]  Cd Length: 145  Bit Score: 42.32  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  20 SRILPNIWLGsCPRQVEHVTIKLKHELGItavmnfqtewdiVQNSSgcNRYPEP-MTPDTMiklyreeglaYIWMPTPDM 98
Cdd:cd14646     4 TRILPHLYLG-CQRDVLNKELMQQNGIGY------------VLNAS--NTCPKPdFIPESH----------FLRVPVNDS 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1334928398  99 STEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 165
Cdd:cd14646    59 FCEKILPWLDKSVDFIEKAKASNGRVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPTI 125
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 75-165 4.85e-05

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 41.18  E-value: 4.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  75 TPDTMIKLYREEGLAYIWMPTPDMSTEgrvqmlpqAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKV 154
Cdd:cd14494    18 PLEADSRFLKQLGVTTIVDLTLAMVDR--------FLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEA 89

                          90
                  ....*....|.
gi 1334928398 155 QYFLMAKRPAV 165
Cdd:cd14494    90 VRIVRLIRPGG 100
DUSP22 cd14581
dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), ...
 86-149 4.85e-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: 41.71  E-value: 4.85e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1334928398  86 EGLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYV--MGW 149
Cdd:cd14581    45 EGMTYLCIPAADSPSQNLTQHFKESIKFIHECRLRGEGCLVHCLAGVSRSVTLVVAYIMTVtdFGW 110
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 42-140 4.90e-05

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 41.87  E-value: 4.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  42 LKHElGITAVMNFQTEWDIVQNssGCNRYPEpmtpdtmikLYREEGLAYIWMPTPDMST---EGRVQMLPQAvclLHALL 118
Cdd:cd14505    39 LKDQ-GVDDVVTLCTDGELEEL--GVPDLLE---------QYQQAGITWHHLPIPDGGVpsdIAQWQELLEE---LLSAL 103

                          90       100
                  ....*....|....*....|...
gi 1334928398 119 EKGHIVYVHCNAGVGRS-TAAVC 140
Cdd:cd14505   104 ENGKKVLIHCKGGLGRTgLIAAC 126
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 22-147 5.56e-05

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


Pssm-ID: 350372 [Multi-domain]  Cd Length: 151  Bit Score: 41.55  E-value: 5.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  22 ILPNIWLGSCPRQVEHvtiKLKH--ELGITAVMNfqtewdIVQNSSGcnRYPEPMTPDtmiklyreeGLAYIWMPTPDMS 99
Cdd:cd14522     8 ILPGLYLGPYSAAMKS---KLEVllKHGITHIVC------VRQNIEA--NFIKPNFPD---------HFRYLVLDVADNP 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1334928398 100 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVcgwLQYVM 147
Cdd:cd14522    68 TENIIRHFPTVKEFIDDCLQTGGKVLVHGNAGISRSAALV---IAYIM 112
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 44-163 1.24e-04

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 41.18  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  44 HELGITAVMNFQTEWDIVQNSSGCNR-----YPEpmtpdtmiKLYREEGLAYIWMPTPDMSTEGRVQMLpQAVCLLHALL 118
Cdd:cd14506    36 KEKGIKTVINLQEPGEHASCGPGLEPesgfsYLP--------EAFMRAGIYFYNFGWKDYGVPSLTTIL-DIVKVMAFAL 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1334928398 119 EKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRP 163
Cdd:cd14506   107 QEGGKVAVHCHAGLGRTGVLIACYLVYALRMSADQAIRLVRSKRP 151
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 20-165 2.17e-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: 39.73  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  20 SRILPNIWLGScprQVEHVTIKLKHELGITAVMNfqtewdiVQNSSGCNRYPEPmtpdtmiklyreeGLAYIWMPTPDMS 99
Cdd:cd14567     2 TPILPFLYLGN---ERDAQDIDTLQRLNIGYVLN-------VTTHLPLYHEGKG-------------GFRYKRLPATDSN 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1334928398 100 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 165
Cdd:cd14567    59 KQNLRQYFEEAFEFIEEAHQSGKGVLVHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKRPII 124
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
 20-165 4.70e-04

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


Pssm-ID: 350419 [Multi-domain]  Cd Length: 144  Bit Score: 38.69  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  20 SRILPNIWLGScprQVEHVTIKLKHELGITAVMNFQTEWDivqnssgcNRYPEPMTPDTmIKLYREEG--LAYIWMPTPD 97
Cdd:cd14571     5 SRIFPYLYLGS---EWNAANLEELQRNRVSHILNVTREID--------NFFPERFTYMN-IRVYDEEAtqLLPHWKETHR 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1334928398  98 MSTEGRVQmlpqavcllhallekGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 165
Cdd:cd14571    73 FIEAARAQ---------------GTRVLVHCKMGVSRSASTVIAYAMKQYGWTLEQALRHVRERRPIV 125
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 86-163 4.90e-04

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


Pssm-ID: 350369 [Multi-domain]  Cd Length: 136  Bit Score: 38.50  E-value: 4.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1334928398  86 EGLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRP 163
Cdd:cd14519    42 EDIKYLCIPAADTPEQNISQHFRECINFIHEARLNGGNVLVHCLAGVSRSVTIVAAYLMTVTDLGWRDALKAVRAARP 119
DSP_DUSP15 cd14582
dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual ...
 71-163 6.69e-04

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


Pssm-ID: 350430 [Multi-domain]  Cd Length: 146  Bit Score: 38.39  E-value: 6.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  71 PEPMTPDtmiklyreegLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWN 150
Cdd:cd14582    41 PQPLLQD----------ITYLRIPLPDTPEAPIKKHFKECISFIHQCRLNGGNCLVHCLAGISRSTTIVVAYVMAVTELS 110

                          90
                  ....*....|...
gi 1334928398 151 LRKVQYFLMAKRP 163
Cdd:cd14582   111 WQEVLEAIRAVRP 123
DSP_DUSP9 cd14644
dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual ...
 21-162 1.21e-03

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


Pssm-ID: 350492 [Multi-domain]  Cd Length: 145  Bit Score: 37.67  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  21 RILPNIWLGsCPRQVEHVTIKLKheLGITAVMNfqtewdivqnssgcnrypepMTPDtMIKLYREEG-LAYIWMPTPDMS 99
Cdd:cd14644     5 QILPNLYLG-SARDSANLETLAK--LGIRYILN--------------------VTPN-LPNFFEKNGdFHYKQIPISDHW 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1334928398 100 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKR 162
Cdd:cd14644    61 SQNLSQFFPEAIEFIDEALSQNCGVLVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDLVKRKK 123
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 101-133 2.56e-03

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


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 37.77  E-value: 2.56e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1334928398 101 EGRVQMLPQAVcllHALLEKGHIVYVHCNAGVG 133
Cdd:cd05305    13 ENRVALTPAGV---AELVAAGHEVLVEKGAGLG 42
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 18-143 2.75e-03

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


Pssm-ID: 350427 [Multi-domain]  Cd Length: 168  Bit Score: 37.05  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  18 HYSRILPNIWLGScpRQVEHVTIKLKHeLGITAVMNfqtewdivqnSSGCNRYpepMTPDTMIKLYREEGLAYIWMPTPD 97
Cdd:cd14579    20 HCNEVYPRIYVGN--ASVAQNIMRLQR-LGITHVLN----------AAEGKSF---MHVNTNAEFYEDTGITYHGIKAND 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1334928398  98 MSTEGRVQMLPQAVCLLH-ALLEKGHIVYVHCNAGVGRSTAAVCGWL 143
Cdd:cd14579    84 TQHFNLSAYFEEAADFIDkALAQKNGRVLVHCREGYSRSPTLVIAYL 130
DSP_DUSP7 cd14643
dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual ...
 21-162 2.79e-03

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


Pssm-ID: 350491 [Multi-domain]  Cd Length: 149  Bit Score: 36.54  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  21 RILPNIWLGsCPRQVEHVTIKLKHelGITAVMNfqtewdivqnssgcnrypepMTPDtMIKLYREEG-LAYIWMPTPDMS 99
Cdd:cd14643     8 QILPYLYLG-CAKDSTNLDVLGKY--GIKYILN--------------------VTPN-LPNMFEHDGeFKYKQIPISDHW 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1334928398 100 TEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKR 162
Cdd:cd14643    64 SQNLSQFFPEAISFIDEARSKKCGILVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDFVKRKK 126
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 20-165 2.94e-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: 36.60  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  20 SRILPNIWLGScprqvEHVTIKLKhEL---GITAVMNFQTEWDivqnssgcNRYPEPMTPDTmIKLYREEG---LAYiWM 93
Cdd:cd14513     2 SKIFDHLYLGS-----EWNASNLE-ELqnnGVKYILNVTREID--------NFFPGRFTYHN-IRVWDEEStnlLPY-WN 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1334928398  94 PTPDMSTEGRvqmlpqavcllhallEKGHIVYVHCNAGVGRSTAAVcgwLQYVM---GWNLRKVQYFLMAKRPAV 165
Cdd:cd14513    66 ETYRFIKEAR---------------RKGSKVLVHCKMGVSRSASTV---IAYAMkeyGWSLEQALEHVKERRSCI 122
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 81-134 3.11e-03

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 36.49  E-value: 3.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1334928398  81 KLYREEGLAYIWMPTPDMSTEGRVQMLpQAVCLLHALLEKGHIVYVHCNAGVGR 134
Cdd:cd14504    43 HSDTCPGLRYHHIPIEDYTPPTLEQID-EFLDIVEEANAKNEAVLVHCLAGKGR 95
DSP_DUSP8 cd14645
dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual ...
 20-165 3.12e-03

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


Pssm-ID: 350493 [Multi-domain]  Cd Length: 151  Bit Score: 36.53  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  20 SRILPNIWLGScprQVEHVTIKLKHELGITAVMNfqtewdivqNSSGCNRyPEPMTPDTMIKLYREEGLAYIWMPTPDMS 99
Cdd:cd14645    13 TRILPHLYLGS---QKDVLNKDLMAQNGITYVLN---------ASNSCPK-PDFICESHFMRIPVNDNYCEKLLPWLDKS 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398 100 TEgrvqmlpqavcllhaLLEKGHI----VYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAV 165
Cdd:cd14645    80 IE---------------FIDKAKVsncrVIVHCLAGISRSATIAIAYIMKTMGLSSDDAYRFVKDRRPSI 134
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 41-147 4.34e-03

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


Pssm-ID: 350365 [Multi-domain]  Cd Length: 148  Bit Score: 36.04  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  41 KLKhELGITAVMNfqtewdIVQNSSGcnrypepMTPDTMIKLYREEGLAYIWMPTPDMSTEGRVQMLPQAVCLLH-ALLE 119
Cdd:cd14515    21 KLK-KLGITHVLN------AAEGKKN-------GEVNTNAKFYKGSGIIYLGIPASDLPTFDISQYFDEAADFIDkALSD 86

                          90       100
                  ....*....|....*....|....*...
gi 1334928398 120 KGHIVYVHCNAGVGRSTAAVcgwLQYVM 147
Cdd:cd14515    87 PGGKVLVHCVEGVSRSATLV---LAYLM 111
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 22-147 4.36e-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: 36.05  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  22 ILPNIWLGScprqVEHVT-IKLKHELGITAVMNfqtewdIVQNSSGCNRypepmtpdtmiklyreEGLAYIWMPTPDMST 100
Cdd:cd14639     4 ILPFLYLGS----AYHASkCEFLANLHITALLN------VSRRSSEACK----------------GQYHYKWIPVEDSHT 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1334928398 101 EGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRStAAVCgwLQYVM 147
Cdd:cd14639    58 ADISSHFQEAIDFIDCVRRAGGKVLVHCEAGISRS-PTIC--MAYLM 101
DSP_DUSP1 cd14638
dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual ...
 22-155 4.51e-03

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


Pssm-ID: 350486 [Multi-domain]  Cd Length: 151  Bit Score: 36.20  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334928398  22 ILPNIWLGScprqVEHVTIK-LKHELGITAVMNFqtewdivqnSSGCnrypepmtPDtmiklYREEGLAYIWMPTPDMST 100
Cdd:cd14638     4 ILPFLYLGS----AYHASRKdMLDTLGITALINV---------SANC--------PN-----HFEGHYQYKSIPVEDNHK 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1334928398 101 EGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRStAAVCgwLQYVMGWNLRKVQ 155
Cdd:cd14638    58 ADISSWFNEAIDFIDSVKNAGGRVFVHCQAGISRS-ATIC--LAYLMRTNRVKLD 109
AlaDh_PNT_N pfam05222
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ...
 101-135 5.82e-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: 35.48  E-value: 5.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1334928398 101 EGRVQMLPQAVcllHALLEKGHIVYVHCNAGVGRS 135
Cdd:pfam05222  10 ERRVALTPAGV---KKLVKLGHEVLVESGAGLGAG 41
COG5350 COG5350
Predicted protein tyrosine phosphatase [General function prediction only];
120-138 9.31e-03

Predicted protein tyrosine phosphatase [General function prediction only];


Pssm-ID: 444131  Cd Length: 165  Bit Score: 35.22  E-value: 9.31e-03
                          10
                  ....*....|....*....
gi 1334928398 120 KGHIVyVHCNAGVGRSTAA 138
Cdd:COG5350    81 EAPLL-VHCHAGISRSTAA 98
 
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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