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Conserved domains on  [gi|2560044518|gb|WKA00730|]
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hypothetical protein VitviT2T_019064 [Vitis vinifera]

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 ...
 92-239 1.23e-82

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: 244.80  E-value: 1.23e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  92 MNYTLITDHLIVGSQPQKPEDVDHLKQEeNVAYILNLQQDKDVEYWEVDLPSIIKRCKELEIRHMRRPARDFDPDSLRSG 171
Cdd:cd14526     1 LNYSRILPNLIVGSCPQNPEDVDRLKKE-GVTAVLNLQTDSDMEYWGVDIDSIRKACKESGIRYVRLPIRDFDTEDLRQK 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2560044518 172 LPKAVSSLEWAISEGkGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPCGPSKQAIRG 239
Cdd:cd14526    80 LPQAVALLYRLLKNG-GTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPDEEAIRG 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 ...
 92-239 1.23e-82

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: 244.80  E-value: 1.23e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  92 MNYTLITDHLIVGSQPQKPEDVDHLKQEeNVAYILNLQQDKDVEYWEVDLPSIIKRCKELEIRHMRRPARDFDPDSLRSG 171
Cdd:cd14526     1 LNYSRILPNLIVGSCPQNPEDVDRLKKE-GVTAVLNLQTDSDMEYWGVDIDSIRKACKESGIRYVRLPIRDFDTEDLRQK 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2560044518 172 LPKAVSSLEWAISEGkGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPCGPSKQAIRG 239
Cdd:cd14526    80 LPQAVALLYRLLKNG-GTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPDEEAIRG 146
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
97-247 1.73e-16

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 74.24  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  97 ITDHLIVGSQpqKPEDVDHLKQEENVAYILNLqqdkdVEYWEVDLPSiikrCKELEIRHMRRPARDFDPDSLRSgLPKAV 176
Cdd:COG2453     3 IIPGLLAGGP--LPGGGEADLKREGIDAVVSL-----TEEEELLLGL----LEEAGLEYLHLPIPDFGAPDDEQ-LQEAV 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2560044518 177 SSLEWAISEGKgKVYVHCTAGLGRAPAVAIAYMFWfCGMDLNTAYDTLTSKRPCGPSKQAIRGATYDLAKN 247
Cdd:COG2453    71 DFIDEALREGK-KVLVHCRGGIGRTGTVAAAYLVL-LGLSAEEALARVRAARPGAVETPAQRAFLERFAKR 139
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
95-230 3.66e-16

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 73.47  E-value: 3.66e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518   95 TLITDHLIVGSQP--QKPEdvdhLKQEENVAYILNLQQdkdveywEVDLPsiikrcKELEIRHMRRPARDFDPDSLRSGL 172
Cdd:smart00195   2 SEILPHLYLGSYSdaLNLA----LLKKLGITHVINVTN-------EVPNY------NGSDFTYLGVPIDDNTETKISPYF 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2560044518  173 PKAVSSLEWAISEGkGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPC 230
Cdd:smart00195  65 PEAVEFIEDAESKG-GKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPI 121
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 101-230 1.72e-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: 71.14  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 101 LIVGSqpqKPEDVDHLKQEENVAYILNLQQDKDveywevdlpsiikrCKELEIRHMRRPARDFDPDSLRSGLPKAVSSLE 180
Cdd:pfam00782   1 LYLGS---KPTASDAFLSKLGITAVINVTREVD--------------LYNSGILYLRIPVEDNHETNISKYLEEAVEFID 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2560044518 181 WAISEGkGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPC 230
Cdd:pfam00782  64 DARQKG-GKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPG 112
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 182-216 8.14e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 36.83  E-value: 8.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2560044518 182 AISEGKGKVYVHCTAGLGRAPAVAIAYMFWFcGMD 216
Cdd:PTZ00393  165 NVIKNNRAVAVHCVAGLGRAPVLASIVLIEF-GMD 198
 
Name Accession Description Interval E-value
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 92-239 1.23e-82

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: 244.80  E-value: 1.23e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  92 MNYTLITDHLIVGSQPQKPEDVDHLKQEeNVAYILNLQQDKDVEYWEVDLPSIIKRCKELEIRHMRRPARDFDPDSLRSG 171
Cdd:cd14526     1 LNYSRILPNLIVGSCPQNPEDVDRLKKE-GVTAVLNLQTDSDMEYWGVDIDSIRKACKESGIRYVRLPIRDFDTEDLRQK 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2560044518 172 LPKAVSSLEWAISEGkGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPCGPSKQAIRG 239
Cdd:cd14526    80 LPQAVALLYRLLKNG-GTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPDEEAIRG 146
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 95-230 3.30e-23

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: 92.22  E-value: 3.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  95 TLITDHLIVGSQPQKpEDVDHLKqEENVAYILNLQQDKDVEYwevdlpsiikrcKELEIRHMRRPARDFDPDSLRSGLPK 174
Cdd:cd14498     2 SEILPGLYLGSLDAA-QDKELLK-KLGITHILNVAGEPPPNK------------FPDGIKYLRIPIEDSPDEDILSHFEE 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2560044518 175 AVSSLEWAISEGkGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPC 230
Cdd:cd14498    68 AIEFIEEALKKG-GKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRPI 122
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
97-247 1.73e-16

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 74.24  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  97 ITDHLIVGSQpqKPEDVDHLKQEENVAYILNLqqdkdVEYWEVDLPSiikrCKELEIRHMRRPARDFDPDSLRSgLPKAV 176
Cdd:COG2453     3 IIPGLLAGGP--LPGGGEADLKREGIDAVVSL-----TEEEELLLGL----LEEAGLEYLHLPIPDFGAPDDEQ-LQEAV 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2560044518 177 SSLEWAISEGKgKVYVHCTAGLGRAPAVAIAYMFWfCGMDLNTAYDTLTSKRPCGPSKQAIRGATYDLAKN 247
Cdd:COG2453    71 DFIDEALREGK-KVLVHCRGGIGRTGTVAAAYLVL-LGLSAEEALARVRAARPGAVETPAQRAFLERFAKR 139
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
95-230 3.66e-16

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 73.47  E-value: 3.66e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518   95 TLITDHLIVGSQP--QKPEdvdhLKQEENVAYILNLQQdkdveywEVDLPsiikrcKELEIRHMRRPARDFDPDSLRSGL 172
Cdd:smart00195   2 SEILPHLYLGSYSdaLNLA----LLKKLGITHVINVTN-------EVPNY------NGSDFTYLGVPIDDNTETKISPYF 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2560044518  173 PKAVSSLEWAISEGkGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPC 230
Cdd:smart00195  65 PEAVEFIEDAESKG-GKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPI 121
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 101-230 1.72e-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: 71.14  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 101 LIVGSqpqKPEDVDHLKQEENVAYILNLQQDKDveywevdlpsiikrCKELEIRHMRRPARDFDPDSLRSGLPKAVSSLE 180
Cdd:pfam00782   1 LYLGS---KPTASDAFLSKLGITAVINVTREVD--------------LYNSGILYLRIPVEDNHETNISKYLEEAVEFID 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2560044518 181 WAISEGkGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPC 230
Cdd:pfam00782  64 DARQKG-GKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPG 112
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 95-229 1.42e-14

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: 68.98  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  95 TLITDHLIVGSQpqkpEDV--DHLKQEENVAYILNLQQdkdveywEVDLPSIIKrckelEIRHMRRPARDFDPDSLRSGL 172
Cdd:cd14568     2 TRILPHLYLGSQ----RDVldKDLMQRNGISYVLNVSN-------TCPKPDFIP-----DSHFLRIPVNDSYCEKLLPWL 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2560044518 173 PKAVSSLEWAISEGKGkVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRP 229
Cdd:cd14568    66 DKAVEFIEKARASNKR-VLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRP 121
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 94-229 1.29e-13

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: 66.90  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  94 YTLITDHLIVGSQPQKPEDvDHLKQEENVAYILNLQQdkdvEYwevDLPSIIKRCKE---LEIRHMRRPARDFDPDSLRS 170
Cdd:cd14524     2 YDRIDDTVILGALPFRSMT-VALVAKENVRGVITMNE----EY---ETRFFCNSKEEwkaLGVEQLRLPTVDFTGVPSLE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2560044518 171 GLPKAVSSLEWAISEGKgKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRP 229
Cdd:cd14524    74 DLEKGVDFILKHREKGK-SVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRP 131
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 95-229 4.15e-13

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: 65.20  E-value: 4.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  95 TLITDHLIVGSQpQKPEDVDHLkQEENVAYILNLQqdkdveywevdlPSIIKRCKELEIRHMRRPARDFDPDSLRSGLPK 174
Cdd:cd14512     2 TRILPNLYLGSQ-RDSLNLELM-QQLGIGYVLNVS------------NTCPNPDFIGLFHYKRIPVNDSFCQNISPWFDE 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2560044518 175 AVSSLEWAISEGKGkVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRP 229
Cdd:cd14512    68 AIEFIEEAKASNGG-VLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRP 121
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 97-229 2.20e-11

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: 60.41  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  97 ITDHLIVGSQpQKPEDVDHLKqEENVAYILNLQQDkdveywevdLPSIIKRCKEleIRHMRRPARDFDPDSLRSGLPKAV 176
Cdd:cd14566     4 ILPFLYLGNA-KDSANIDLLK-KYNIKYILNVTPN---------LPNTFEEDGG--FKYLQIPIDDHWSQNLSAFFPEAI 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2560044518 177 SSLEWAISEGKGkVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRP 229
Cdd:cd14566    71 SFIDEARSKKCG-VLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKRKS 122
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 95-229 2.39e-11

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: 60.53  E-value: 2.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  95 TLITDHLIVGSQpQKPEDVDHLkQEENVAYILNLQqdkdveyweVDLPSIIKrcKELEIRHMRRPARDFDPDSLRSGLPK 174
Cdd:cd14567     2 TPILPFLYLGNE-RDAQDIDTL-QRLNIGYVLNVT---------THLPLYHE--GKGGFRYKRLPATDSNKQNLRQYFEE 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2560044518 175 AVSSLEWAISEGKGkVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRP 229
Cdd:cd14567    69 AFEFIEEAHQSGKG-VLVHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKRP 122
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 149-230 4.39e-10

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: 56.63  E-value: 4.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 149 KELEIRHMRRPARDFDPDSLRSGLPKAVSSLEWAISEGkGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKR 228
Cdd:cd14565    41 FEDHFQYKSIPVEDSHNADISSWFEEAIGFIDKVKASG-GRVLVHCQAGISRSATICLAYLMTTRRVRLNEAFDYVKQRR 119


                  ..
gi 2560044518 229 PC 230
Cdd:cd14565   120 SV 121
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 159-232 6.52e-10

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: 57.08  E-value: 6.52e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2560044518 159 PARDFDPDSLRSGLPKAVSSLEWAISEGKGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPCGP 232
Cdd:cd14579    80 KANDTQHFNLSAYFEEAADFIDKALAQKNGRVLVHCREGYSRSPTLVIAYLMLRQKMDVKSALSTVRQKREIGP 153
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 182-233 1.29e-07

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: 49.90  E-value: 1.29e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2560044518 182 AISEGKGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPCGPS 233
Cdd:cd14515    83 ALSDPGGKVLVHCVEGVSRSATLVLAYLMIYQNMTLEEAIRTVRKKREIRPN 134
DSP_DUSP7 cd14643
dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual ...
 121-228 3.75e-07

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: 48.86  E-value: 3.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 121 NVAYILNLQQDkdveywevdLPSIIKRCKELEIRHMrrPARDFDPDSLRSGLPKAVSSLEWAISEGKGkVYVHCTAGLGR 200
Cdd:cd14643    31 GIKYILNVTPN---------LPNMFEHDGEFKYKQI--PISDHWSQNLSQFFPEAISFIDEARSKKCG-ILVHCLAGISR 98

                          90       100
                  ....*....|....*....|....*...
gi 2560044518 201 APAVAIAYMFWFCGMDLNTAYDTLTSKR 228
Cdd:cd14643    99 SVTVTVAYLMQKLNLSLNDAYDFVKRKK 126
DSP_DUSP9 cd14644
dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual ...
 97-228 4.24e-07

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: 48.46  E-value: 4.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  97 ITDHLIVGSQpQKPEDVDHLKQEeNVAYILNLQQDkdveywevdLPSIIKRCKELEIRHMrrPARDFDPDSLRSGLPKAV 176
Cdd:cd14644     6 ILPNLYLGSA-RDSANLETLAKL-GIRYILNVTPN---------LPNFFEKNGDFHYKQI--PISDHWSQNLSQFFPEAI 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2560044518 177 SSLEWAISEGKGkVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKR 228
Cdd:cd14644    73 EFIDEALSQNCG-VLVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDLVKRKK 123
DSP_fungal_SDP1-like cd14521
dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, ...
 171-229 5.42e-07

dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, and similar proteins; This family is composed of fungal dual specificity protein phosphatases (DUSPs) including Saccharomyces cerevisiae SDP1 and MSG5, and Schizosaccharomyces pombe Pmp1. function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. SDP1 is oxidative stress-induced and dephosphorylates MAPK substrates such as SLT2. MSG5 dephosphorylates the Fus3 and Slt2 MAPKs operating in the mating and cell wall integrity (CWI) pathways, respectively. Pmp1 is responsible for dephosphorylating the CWI MAPK Pmk1. These phosphatases bind to their target MAPKs through a conserved IYT motif located outside of the dual specificity phosphatase domain.


Pssm-ID: 350371 [Multi-domain]  Cd Length: 155  Bit Score: 48.47  E-value: 5.42e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2560044518 171 GLPKAVSSLEWAISEGKgKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRP 229
Cdd:cd14521    79 DLPKLTSIIEDATQSGK-KVLIHCQCGVSRSASLIIAYIMKKLGLSLNDAYDLLKSRSP 136
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 188-230 1.35e-06

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


Pssm-ID: 350364 [Multi-domain]  Cd Length: 133  Bit Score: 46.78  E-value: 1.35e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2560044518 188 GKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPC 230
Cdd:cd14514    78 GRTLVHCVAGVSRSATLCLAYLMKYEGMTLREAYKHVKAARPI 120
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 95-229 1.53e-06

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


Pssm-ID: 350494 [Multi-domain]  Cd Length: 145  Bit Score: 46.94  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  95 TLITDHLIVGSQpqkpEDV--DHLKQEENVAYILNLQQdkdveywEVDLPSIIKrckelEIRHMRRPARDFDPDSLRSGL 172
Cdd:cd14646     4 TRILPHLYLGCQ----RDVlnKELMQQNGIGYVLNASN-------TCPKPDFIP-----ESHFLRVPVNDSFCEKILPWL 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2560044518 173 PKAVSSLEWAiSEGKGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRP 229
Cdd:cd14646    68 DKSVDFIEKA-KASNGRVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRP 123
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 183-230 1.66e-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: 46.58  E-value: 1.66e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2560044518 183 ISEGK---GKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPC 230
Cdd:cd14523    72 IDEAKsqdGVVLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNARPS 122
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 152-229 1.85e-06

dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity protein phosphatase 18 (DUSP18), dual specificity protein phosphatase 21 (DUSP21), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP18, also called low molecular weight dual specificity phosphatase 20 (LMW-DSP20), is a catalytically active phosphatase with a preference for phosphotyrosine over phosphoserine/threonine oligopeptides in vitro. In vivo, it has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP21 is also called low molecular weight dual specificity phosphatase 21 (LMW-DSP21). Its gene has been identified as a potential therapeutic target in human hepatocellular carcinoma. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane.


Pssm-ID: 350421 [Multi-domain]  Cd Length: 158  Bit Score: 46.71  E-value: 1.85e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2560044518 152 EIRHMRRPARDfDPDSLRSGLPKAVSSLEWAISEGKGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRP 229
Cdd:cd14573    45 GIEYLHVPVAD-SPDTRLRDYFDPIADKIHTVEARGGRTLLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTWVKSCRP 121
DSP_DUSP6 cd14642
dual specificity phosphatase domain of dual specificity protein phosphatase 6; Dual ...
 118-228 2.74e-06

dual specificity phosphatase domain of dual specificity protein phosphatase 6; Dual specificity protein phosphatase 6 (DUSP6), also called mitogen-activated protein kinase (MAPK) phosphatase 3 (MKP-3) or dual specificity protein phosphatase PYST1, 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. DUSP6/MKP-3 plays an important role in obesity-related hyperglycemia by promoting hepatic glucose output. MKP-3 deficiency attenuates body weight gain induced by a high-fat diet, protects mice from developing obesity-related hepatosteatosis, and reduces adiposity, possibly by repressing adipocyte differentiation. It also contributes to p53-controlled cellular senescence. 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: 350490 [Multi-domain]  Cd Length: 143  Bit Score: 46.22  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 118 QEENVAYILNLQQDkdveywevdLPSIIKRCKELEIRHMrrPARDFDPDSLRSGLPKAVSslewAISEGKGK---VYVHC 194
Cdd:cd14642    25 EEFGIKYILNVTPN---------LPNLFENAGEFKYKQI--PISDHWSQNLSQFFPEAIS----FIDEARGKncgVLVHC 89

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2560044518 195 TAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKR 228
Cdd:cd14642    90 LAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKK 123
DSP_DUSP8 cd14645
dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual ...
 95-229 4.74e-06

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: 45.39  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  95 TLITDHLIVGSQpqkpEDV--DHLKQEENVAYILNLQQdkdveywEVDLPSIIKrckelEIRHMRRPARDFDPDSLRSGL 172
Cdd:cd14645    13 TRILPHLYLGSQ----KDVlnKDLMAQNGITYVLNASN-------SCPKPDFIC-----ESHFMRIPVNDNYCEKLLPWL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2560044518 173 PKAVSSLEWAiSEGKGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRP 229
Cdd:cd14645    77 DKSIEFIDKA-KVSNCRVIVHCLAGISRSATIAIAYIMKTMGLSSDDAYRFVKDRRP 132
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 91-229 5.66e-06

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: 46.19  E-value: 5.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  91 GMNYTLITDHLIVGSQPQKP--EDVDHLKQ--EENVAYILNLQQD-------KDVEYwEVDLPSIIKRCKELEIRHMRRP 159
Cdd:cd14506     5 GLYSSWITDDILAMARPSTEliDKYGIIEQfkEKGIKTVINLQEPgehascgPGLEP-ESGFSYLPEAFMRAGIYFYNFG 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2560044518 160 ARDFDPDSLRSGLpKAVSSLEWAISEGkGKVYVHCTAGLGRApAVAIA-YMFWFCGMDLNTAYDTLTSKRP 229
Cdd:cd14506    84 WKDYGVPSLTTIL-DIVKVMAFALQEG-GKVAVHCHAGLGRT-GVLIAcYLVYALRMSADQAIRLVRSKRP 151
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
 153-230 1.66e-05

dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar proteins; Dual specificity protein phosphatase 12 (DUSP12), also called YVH1, 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. DUSP12 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 targets p38 MAPK to regulate macrophage response to bacterial infection. It also ameliorates cardiac hypertrophy in response to pressure overload through c-Jun N-terminal kinase (JNK) inhibition. DUSP12 has been identified as a modulator of cell cycle progression, a function independent of phosphatase activity and mediated by its C-terminal zinc-binding domain.


Pssm-ID: 350370 [Multi-domain]  Cd Length: 144  Bit Score: 43.78  E-value: 1.66e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2560044518 153 IRHMRRPARDFDPDSLRSGLPKAVSSLEWAISEGKgkVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPC 230
Cdd:cd14520    47 LVRKFVPALDEESTDLLSRLDECLDFIDEGRAEGA--VLVHCHAGVSRSAAVVTAYLMKTEQLSFEEALASLRECKPD 122
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 105-209 3.51e-05

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: 42.65  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 105 SQPQKPEDVDHLkQEENVAYILNLQQDKDVEYWEvdlpsiikRCKELEIRHMrrPARDFDPDSLRSgLPKAVSSLEWAIS 184
Cdd:cd14504    13 AFPRLPEHYAYL-NENGIRHVVTLTEEPPPEHSD--------TCPGLRYHHI--PIEDYTPPTLEQ-IDEFLDIVEEANA 80

                          90       100
                  ....*....|....*....|....*
gi 2560044518 185 EGKGkVYVHCTAGLGRAPAVAIAYM 209
Cdd:cd14504    81 KNEA-VLVHCLAGKGRTGTMLACYL 104
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 142-229 5.80e-05

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: 41.88  E-value: 5.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 142 PSIIKRCKELEIRHMRRPARDF--------DPDSLRsglpKAVSSLEWAISEGkGKVYVHCTAGLGRAPAVAIAYMFWFC 213
Cdd:cd14527    28 PAVLDLTAELPRPRKRQAYRCVplldlvapTPEQLE----RAVAWIEELRAQG-GPVLVHCALGYGRSATVVAAWLLAYG 102

                          90
                  ....*....|....*..
gi 2560044518 214 GM-DLNTAYDTLTSKRP 229
Cdd:cd14527   103 RAkSVAEAEALIRAARP 119
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
 148-228 1.38e-04

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: 41.00  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 148 CKELEIRHMRRPARDFDPDSLRSGLPKAVSSLEWaISEGKGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSK 227
Cdd:cd14641    43 YFEGQFQYKSIPVEDSHMADISAWFQEAIDFIDS-VKNSGGRVLVHCQAGISRSATICLAYLIQSQRVRLDEAFDFVKQR 121


                  .
gi 2560044518 228 R 228
Cdd:cd14641   122 R 122
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 190-228 2.04e-04

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 40.67  E-value: 2.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2560044518 190 VYVHCTAGLGRAPA-VAIAYMfwFCGMDLNTAYDTLTSKR 228
Cdd:cd14500    98 IAVHCVAGLGRAPVlVAIALI--ELGMKPEDAVEFIRKKR 135
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 159-228 2.93e-04

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: 40.28  E-value: 2.93e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 159 PARDFDPDSLRSGLPKAVSSLEWAISEGkGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKR 228
Cdd:cd14639    51 PVEDSHTADISSHFQEAIDFIDCVRRAG-GKVLVHCEAGISRSPTICMAYLMKTKRFRLEEAFDYIKQRR 119
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 95-230 3.51e-04

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: 40.07  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518  95 TLITDHLIVGSQpQKPEDVDHLkQEENVAYILNLQQdkdveywEVD--LPSIIKRCKeleIRHMRRPARDFDPDslrsgl 172
Cdd:cd14513     2 SKIFDHLYLGSE-WNASNLEEL-QNNGVKYILNVTR-------EIDnfFPGRFTYHN---IRVWDEESTNLLPY------ 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2560044518 173 pkavssleWA-----ISEGK---GKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPC 230
Cdd:cd14513    64 --------WNetyrfIKEARrkgSKVLVHCKMGVSRSASTVIAYAMKEYGWSLEQALEHVKERRSC 121
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
 116-232 3.60e-04

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


Pssm-ID: 350368 [Multi-domain]  Cd Length: 153  Bit Score: 39.99  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 116 LKQEENVAYILNLqqdkdVEYwevDLPSIIKRCKEleirHMRRPARDFDPDSLRSGLPKAVSSLEWAISEG--------- 186
Cdd:cd14518    21 LLKAENITHILSV-----IPG---DVPEEYFKGYE----HKQIEIDDVEDENILQHFPETNRFIDSALFGNgkdedeekk 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2560044518 187 -KGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRP-CGP 232
Cdd:cd14518    89 hGGAVLVHCAMGKSRSVTVVIAYLMYKYNLSVSQALHAVRRKRPiAEP 136
DSP_fungal_PPS1 cd14516
dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; ...
 166-221 3.63e-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: 3.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2560044518 166 DSLRSGLPKAVSSLEWAISEGkGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAY 221
Cdd:cd14516    96 DSLLPQLTDALDFIQKARLLG-GKTLVHCRVGVSRSATVVIAEVMKHLRMSLVDAY 150
DUSP28 cd14574
dual specificity protein phosphatase 28; Dual specificity protein phosphatase 28 (DUSP28), ...
 153-229 6.12e-04

dual specificity protein phosphatase 28; Dual specificity protein phosphatase 28 (DUSP28), also called VHP, 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 that 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 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells. DUSP28 has an exceptionally low phosphatase activity due to the presence of bulky residues in the active site pocket resulting in low accessibility.


Pssm-ID: 350422 [Multi-domain]  Cd Length: 140  Bit Score: 39.38  E-value: 6.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2560044518 153 IRHMRRPARDfDP-DSLRSGLPKAVSSLEWAISEGkGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRP 229
Cdd:cd14574    45 VSTLRVPVFD-DPaEDLYRHFEQCADAIEAAVRRG-GKCLVYCKNGRSRSAAVCIAYLMKHRGLSLQDAFQVVKAARP 120
DSP_iDUSP27 cd14576
dual specificity phosphatase-like domain of inactive dual specificity protein phosphatase 27; ...
 151-233 7.72e-04

dual specificity phosphatase-like domain of inactive dual specificity protein phosphatase 27; Inactive dual specificity protein phosphatase 27 (DUSP27) may play a role in myofiber maturation. It is a pseudophosphatase containing a substitution of the active site cysteine into a serine. It is a large protein of more than 1000 amino acids in length with an N-terminal dual specificity phosphatase-like domain.


Pssm-ID: 350424  Cd Length: 159  Bit Score: 39.08  E-value: 7.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 151 LEIRHMRRPARDFDPDSLRSGLPKAVSSLEWAISEGKGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPC 230
Cdd:cd14576    59 MNIQYMGIEVDDFPDVDISKHFRKGAEFLDEALLTYRGKVLVSSEMGISRSAVLVAAYLMIFHNMTIMEALMTLRKKRAI 138


                  ...
gi 2560044518 231 GPS 233
Cdd:cd14576   139 YPN 141
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 186-230 7.74e-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: 38.88  E-value: 7.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2560044518 186 GKGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPC 230
Cdd:cd14519    76 NGGNVLVHCLAGVSRSVTIVAAYLMTVTDLGWRDALKAVRAARPC 120
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 112-230 9.54e-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: 38.85  E-value: 9.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 112 DVDHLKQEeNVAYILNLQQDKDVEYwevdlpsiIKRCKELEIRHMRRPARDFDPDSLRSGLPKAVSSLEWAISEGkGKVY 191
Cdd:cd14522    24 KLEVLLKH-GITHIVCVRQNIEANF--------IKPNFPDHFRYLVLDVADNPTENIIRHFPTVKEFIDDCLQTG-GKVL 93

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2560044518 192 VHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPC 230
Cdd:cd14522    94 VHGNAGISRSAALVIAYIMETYGLSYRDAFAYVQQRRFC 132
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
 183-229 1.25e-03

dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), also called mitogen-activated protein kinase (MAPK) phosphatase 6 (MKP-6) or MKP-1-like protein tyrosine phosphatase (MKP-L), 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. DUSP14 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. DUSP14 dephosphorylates JNK, ERK, and p38 in vitro. It also 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.


Pssm-ID: 350420 [Multi-domain]  Cd Length: 150  Bit Score: 38.31  E-value: 1.25e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2560044518 183 ISEGKGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRP 229
Cdd:cd14572    81 VGRKHGATLVHCAAGVSRSATLCIAYLMKYHRVSLLEAYNWVKARRP 127
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 187-229 1.28e-03

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: 38.28  E-value: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2560044518 187 KGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRP 229
Cdd:cd18534    73 KARVLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRP 115
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
 182-234 1.74e-03

dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 isoform A (DUSP13A), also called branching-enzyme interacting DSP or muscle-restricted DSP (MDSP), 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. DUSP13A 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. DUSP13A also functions as a regulator of apoptosis signal-regulating kinase 1 (ASK1), a MAPK kinase kinase, by interacting with its N-terminal domain and inducing ASK1-mediated apoptosis through the activation of caspase-3. This function is independent of phosphatase activity.


Pssm-ID: 350428 [Multi-domain]  Cd Length: 145  Bit Score: 37.81  E-value: 1.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2560044518 182 AISEGKGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPCGPSK 234
Cdd:cd14580    80 ALNTPGAKVLVHCAVGVSRSATLVLAYLMIYHQLSLVQAIKTVKERRWIFPNR 132
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 185-243 1.96e-03

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: 37.33  E-value: 1.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2560044518 185 EGKGKVYVHCTAGLGRAPAVAIAYMfwfCGMDLNTAYDTLTSKRPCGPSKQAIRGATYD 243
Cdd:cd14494    54 KPGEPVLVHCKAGVGRTGTLVACYL---VLLGGMSAEEAVRIVRLIRPGGIPQTIEQLD 109
DUSP26 cd14578
dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), ...
 121-238 2.47e-03

dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), also called mitogen-activated protein kinase (MAPK) phosphatase 8 (MKP-8) or low-molecular-mass dual-specificity phosphatase 4 (LDP-4), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP26 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is a brain phosphatase highly overexpressed in neuroblastoma and has also been identified as a p53 phosphatase, dephosphorylating phospho-Ser20 and phospho-Ser37 in the p53 transactivation domain.


Pssm-ID: 350426 [Multi-domain]  Cd Length: 144  Bit Score: 37.51  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 121 NVAYILNLQQDK---DVEYWEvdlpsiikrckELEIRHMRRPARDFDPDSLRSGLPKAVSSLEWAISEGKGKVYVHCTAG 197
Cdd:cd14578    26 GITHILNASHSKwrgGAEYYE-----------GLNIRYLGIEAHDSPAFDMSIHFYPAADFIHRALSQPGGKILVHCAVG 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2560044518 198 LGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPCGPSKQAIR 238
Cdd:cd14578    95 VSRSATLVLAYLMIHHHMTLVEAIKTVKDHRGIIPNRGFLR 135
DUSP13B cd14577
dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 ...
 182-233 3.69e-03

dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 isoform B (DUSP13B), also called testis- and skeletal-muscle-specific DSP (TMDP) or dual specificity phosphatase SKRP4, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP13B is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP13B inactivates MAPK activation in the order of selectivity, JNK = p38 > ERK in cells. It may play a role in protection from external stress during spermatogenesis.


Pssm-ID: 350425 [Multi-domain]  Cd Length: 163  Bit Score: 37.47  E-value: 3.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2560044518 182 AISEGKGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKRPCGPS 233
Cdd:cd14577    98 ALSSPNGRVLVHCAMGISRSATLVLAFLMICEDLTLVDAIQTVRAHRDICPN 149
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
 159-228 5.70e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual specificity protein phosphatase 4 (DUSP4), also called mitogen-activated protein kinase (MAPK) phosphatase 2 (MKP-2), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP4 regulates either ERK or c-JUN N-terminal kinase (JNK), depending on the cell type. It dephosphorylates nuclear JNK and induces apoptosis in diffuse large B cell lymphoma (DLBCL) cells. It acts as a negative regulator of macrophage M1 activation and inhibits inflammation during macrophage-adipocyte interaction. It has been linked to different aspects of cancer: it may have a role in the development of ovarian cancers, oesophagogastric rib metastasis, and pancreatic tumours; it may also be a candidate tumor suppressor gene, with its deletion implicated in breast cancer, prostate cancer, and gliomas. DUSP4/MKP-2 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350488 [Multi-domain]  Cd Length: 141  Bit Score: 36.55  E-value: 5.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 159 PARDFDPDSLRSGLPKAVSSLEwAISEGKGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKR 228
Cdd:cd14640    51 PVEDNHKADISSWFMEAIEYID-SVKDCNGRVLVHCQAGISRSATICLAYLMMKKRVRLEEAFEFVKQRR 119
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 190-228 7.65e-03

protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), also known as protein-tyrosine phosphatase of regenerating liver 2 (PRL-2), stimulates progression from G1 into S phase during mitosis and promotes tumors. It regulates tumor cell migration and invasion through an ERK-dependent signaling pathway. Its overexpression correlates with breast tumor formation and progression. PRL-2 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350512 [Multi-domain]  Cd Length: 155  Bit Score: 36.13  E-value: 7.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2560044518 190 VYVHCTAGLGRAPaVAIAYMFWFCGMDLNTAYDTLTSKR 228
Cdd:cd18536    97 VAVHCVAGLGRAP-VLVALALIECGMKYEDAVQFIRQKR 134
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 182-216 8.14e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 36.83  E-value: 8.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2560044518 182 AISEGKGKVYVHCTAGLGRAPAVAIAYMFWFcGMD 216
Cdd:PTZ00393  165 NVIKNNRAVAVHCVAGLGRAPVLASIVLIEF-GMD 198
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 187-207 8.29e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 36.15  E-value: 8.29e-03
                          10        20
                  ....*....|....*....|..
gi 2560044518 187 KGKVYVHCTAGLGRAPA-VAIA 207
Cdd:PTZ00242   98 PETIAVHCVAGLGRAPIlVALA 119
DSP_DUSP1 cd14638
dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual ...
 159-228 8.78e-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: 8.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2560044518 159 PARDFDPDSLRSGLPKAVSSLEwAISEGKGKVYVHCTAGLGRAPAVAIAYMFWFCGMDLNTAYDTLTSKR 228
Cdd:cd14638    51 PVEDNHKADISSWFNEAIDFID-SVKNAGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRR 119
 
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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