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Conserved domains on  [gi|35902878|ref|NP_919361|]
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dual specificity protein phosphatase 6 [Danio rerio]

Protein Classification

dual specificity protein phosphatase family protein( domain architecture ID 12919527)

dual specificity protein phosphatase family protein such as dual specificity phosphatases, which dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues, as well as tyrosine-specific protein phosphatases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 206-342 1.62e-104

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: 303.86  E-value: 1.62e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14566   1 PVEILPFLYLGNAKDSANIDLLKKYNIKYILNVTPNLPNTFEEDGGFKYLQIPIDDHWSQNLSAFFPEAISFIDEARSKK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDF 342
Cdd:cd14566  81 CGVLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKRKSNISPNFNFMGQLLDF 137
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 17-147 4.69e-44

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


:

Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 148.97  E-value: 4.69e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878  17 SKTVEWLKEQLETRRDCLLVMDCRAQELYESSHVETAINVAIPSLMLRRLKKGNLPIKSLLSNGEDRERFARRcKTDTIV 96
Cdd:cd01446   1 TIDCAWLAALLREGGERLLLLDCRPFLEYSSSHIRGAVNVCCPTILRRRLQGGKILLQQLLSCPEDRDRLRRG-ESLAVV 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 35902878  97 LYDEYSREWNENID---GGSVLGLLLRRMkDEGYKAFYLEGGFSKFQTDFPAMC 147
Cdd:cd01446  80 VYDESSSDRERLREdstAESVLGKLLRKL-QEGCSVYLLKGGFEQFSSEFPELC 132
 
Name Accession Description Interval E-value
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 206-342 1.62e-104

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: 303.86  E-value: 1.62e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14566   1 PVEILPFLYLGNAKDSANIDLLKKYNIKYILNVTPNLPNTFEEDGGFKYLQIPIDDHWSQNLSAFFPEAISFIDEARSKK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDF 342
Cdd:cd14566  81 CGVLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKRKSNISPNFNFMGQLLDF 137
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
206-345 2.96e-64

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 201.36  E-value: 2.96e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878    206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFEnaGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:smart00195   1 PSEILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPNYNG--SDFTYLGVPIDDNTETKISPYFPEAVEFIEDAESKG 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878    286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERT 345
Cdd:smart00195  79 GKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLIEYERK 138
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 213-343 3.11e-51

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: 167.44  E-value: 3.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878   213 LYLGCAKDSTNLdILEEFGIKYILNVTPNLPNMFENageFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLKCGVLVHC 292
Cdd:pfam00782   1 LYLGSKPTASDA-FLSKLGITAVINVTREVDLYNSG---ILYLRIPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHC 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 35902878   293 LAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFE 343
Cdd:pfam00782  77 QAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISPNFGFKRQLLEYE 127
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 17-147 4.69e-44

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 148.97  E-value: 4.69e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878  17 SKTVEWLKEQLETRRDCLLVMDCRAQELYESSHVETAINVAIPSLMLRRLKKGNLPIKSLLSNGEDRERFARRcKTDTIV 96
Cdd:cd01446   1 TIDCAWLAALLREGGERLLLLDCRPFLEYSSSHIRGAVNVCCPTILRRRLQGGKILLQQLLSCPEDRDRLRRG-ESLAVV 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 35902878  97 LYDEYSREWNENID---GGSVLGLLLRRMkDEGYKAFYLEGGFSKFQTDFPAMC 147
Cdd:cd01446  80 VYDESSSDRERLREdstAESVLGKLLRKL-QEGCSVYLLKGGFEQFSSEFPELC 132
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
208-346 1.57e-20

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 86.56  E-value: 1.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGE--FKYKQIPISDHWSQNLSQFfPEAISFIDEARGLK 285
Cdd:COG2453   2 WIIPGLLAGGPLPGGGEADLKREGIDAVVSLTEEEELLLGLLEEagLEYLHLPIPDFGAPDDEQL-QEAVDFIDEALREG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMqKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 346
Cdd:COG2453  81 KKVLVHCRGGIGRTGTVAAAYLV-LLGLSAEEALARVRAARPGAVETPAQRAFLERFAKRL 140
PRK12361 PRK12361
hypothetical protein; Provisional
 208-333 7.56e-13

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 69.65  E-value: 7.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878  208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLP----NMFENagEFKYKQIPISDHWSQNLSQFFpEAISFIDEARG 283
Cdd:PRK12361  97 KIDENLYLGCRLFPADLEKLKSNKITAILDVTAEFDgldwSLTEE--DIDYLNIPILDHSVPTLAQLN-QAINWIHRQVR 173

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 35902878  284 LKCGVLVHCLAGISRSVTVTVAYLM-QKLNLSMNDAYDIVKMKKSNISPNF 333
Cdd:PRK12361 174 ANKSVVVHCALGRGRSVLVLAAYLLcKDPDLTVEEVLQQIKQIRKTARLNK 224
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 30-145 5.69e-11

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 58.62  E-value: 5.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878     30 RRDCLLVmDCRAQELYESSHVETAINVAIPSLMLRRLKKGNLPIKSLLsngedreRFARRCKTDTIVLYDEYSREWneni 109
Cdd:smart00450   2 DEKVVLL-DVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELL-------KRLGLDKDKPVVVYCRSGNRS---- 69

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 35902878    110 dggSVLGLLLRRMkdeGYK-AFYLEGGFSKFQTDFPA 145
Cdd:smart00450  70 ---AKAAWLLREL---GFKnVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 31-140 3.40e-10

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 56.34  E-value: 3.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878    31 RDCLLVMDCRAQELYESSHVETAINVAIPSLMLRRLKKGNLPiksllsngedrERFARRCKTDTIVLYDeysrewneniD 110
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELL-----------EKLLELLKDKPIVVYC----------N 61

                          90       100       110
                  ....*....|....*....|....*....|.
gi 35902878   111 GGSVLGLLLRRMKDEGY-KAFYLEGGFSKFQ 140
Cdd:pfam00581  62 SGNRAAAAAALLKALGYkNVYVLDGGFEAWK 92
 
Name Accession Description Interval E-value
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 206-342 1.62e-104

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: 303.86  E-value: 1.62e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14566   1 PVEILPFLYLGNAKDSANIDLLKKYNIKYILNVTPNLPNTFEEDGGFKYLQIPIDDHWSQNLSAFFPEAISFIDEARSKK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDF 342
Cdd:cd14566  81 CGVLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKRKSNISPNFNFMGQLLDF 137
DSP_DUSP7 cd14643
dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual ...
 202-349 2.29e-102

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: 298.86  E-value: 2.29e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 202 QPSFPVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEA 281
Cdd:cd14643   2 QPAFPVQILPYLYLGCAKDSTNLDVLGKYGIKYILNVTPNLPNMFEHDGEFKYKQIPISDHWSQNLSQFFPEAISFIDEA 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 35902878 282 RGLKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTLGLK 349
Cdd:cd14643  82 RSKKCGILVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDFVKRKKSNISPNFNFMGQLLDFERTLGLN 149
DSP_DUSP6 cd14642
dual specificity phosphatase domain of dual specificity protein phosphatase 6; Dual ...
 204-346 2.03e-97

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: 286.20  E-value: 2.03e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 204 SFPVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARG 283
Cdd:cd14642   1 SFPVEILPYLYLGCAKDSTNLDVLEEFGIKYILNVTPNLPNLFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 35902878 284 LKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 346
Cdd:cd14642  81 KNCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 143
DSP_DUSP9 cd14644
dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual ...
 204-348 7.73e-91

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: 269.56  E-value: 7.73e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 204 SFPVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARG 283
Cdd:cd14644   1 SFPVQILPNLYLGSARDSANLETLAKLGIRYILNVTPNLPNFFEKNGDFHYKQIPISDHWSQNLSQFFPEAIEFIDEALS 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 35902878 284 LKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTLGL 348
Cdd:cd14644  81 QNCGVLVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDLVKRKKSNISPNFNFMGQLLDFEKSLGL 145
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 206-342 3.25e-74

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: 226.60  E-value: 3.25e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENaGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14512   1 PTRILPNLYLGSQRDSLNLELMQQLGIGYVLNVSNTCPNPDFI-GLFHYKRIPVNDSFCQNISPWFDEAIEFIEEAKASN 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDF 342
Cdd:cd14512  80 GGVLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRPTISPNFNFMGQLLDF 136
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
206-345 2.96e-64

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 201.36  E-value: 2.96e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878    206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFEnaGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:smart00195   1 PSEILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPNYNG--SDFTYLGVPIDDNTETKISPYFPEAVEFIEDAESKG 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878    286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERT 345
Cdd:smart00195  79 GKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLIEYERK 138
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 206-343 3.99e-61

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: 193.37  E-value: 3.99e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFEnaGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14565   1 PVEILPFLYLGSAYHASRREVLKALGITAVLNVSRNCPNHFE--DHFQYKSIPVEDSHNADISSWFEEAIGFIDKVKASG 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFE 343
Cdd:cd14565  79 GRVLVHCQAGISRSATICLAYLMTTRRVRLNEAFDYVKQRRSVISPNFNFMGQLLQYE 136
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 206-346 2.70e-57

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: 183.39  E-value: 2.70e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPnMFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14568   1 PTRILPHLYLGSQRDVLDKDLMQRNGISYVLNVSNTCP-KPDFIPDSHFLRIPVNDSYCEKLLPWLDKAVEFIEKARASN 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 346
Cdd:cd14568  80 KRVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRPTISPNFNFLGQLLEFEKKL 140
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 206-341 1.69e-56

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: 181.20  E-value: 1.69e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGeFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14498   1 PSEILPGLYLGSLDAAQDKELLKKLGITHILNVAGEPPPNKFPDG-IKYLRIPIEDSPDEDILSHFEEAIEFIEEALKKG 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLD 341
Cdd:cd14498  80 GKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRPIISPNPGFLKQLKE 135
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 206-346 1.71e-56

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: 181.87  E-value: 1.71e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14567   1 LTPILPFLYLGNERDAQDIDTLQRLNIGYVLNVTTHLPLYHEGKGGFRYKRLPATDSNKQNLRQYFEEAFEFIEEAHQSG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 346
Cdd:cd14567  81 KGVLVHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKRPIISPNLNFMGQLLEFEEDL 141
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 213-343 3.11e-51

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: 167.44  E-value: 3.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878   213 LYLGCAKDSTNLdILEEFGIKYILNVTPNLPNMFENageFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLKCGVLVHC 292
Cdd:pfam00782   1 LYLGSKPTASDA-FLSKLGITAVINVTREVDLYNSG---ILYLRIPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHC 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 35902878   293 LAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFE 343
Cdd:pfam00782  77 QAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISPNFGFKRQLLEYE 127
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
 206-343 1.10e-45

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: 153.87  E-value: 1.10e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFEnaGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14641   4 PVEILPFLFLGSAHHSSRRETLESLGITAVLNVSSSCPNYFE--GQFQYKSIPVEDSHMADISAWFQEAIDFIDSVKNSG 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFE 343
Cdd:cd14641  82 GRVLVHCQAGISRSATICLAYLIQSQRVRLDEAFDFVKQRRGVISPNFSFMGQLLQFE 139
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
 206-343 1.82e-44

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: 150.57  E-value: 1.82e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFEnaGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14640   1 PVEILPFLYLGSAYHAARRDMLDALGITALLNVSSDCPNHFE--GHYQYKCIPVEDNHKADISSWFMEAIEYIDSVKDCN 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFE 343
Cdd:cd14640  79 GRVLVHCQAGISRSATICLAYLMMKKRVRLEEAFEFVKQRRSIISPNFSFMGQLLQFE 136
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 17-147 4.69e-44

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 148.97  E-value: 4.69e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878  17 SKTVEWLKEQLETRRDCLLVMDCRAQELYESSHVETAINVAIPSLMLRRLKKGNLPIKSLLSNGEDRERFARRcKTDTIV 96
Cdd:cd01446   1 TIDCAWLAALLREGGERLLLLDCRPFLEYSSSHIRGAVNVCCPTILRRRLQGGKILLQQLLSCPEDRDRLRRG-ESLAVV 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 35902878  97 LYDEYSREWNENID---GGSVLGLLLRRMkDEGYKAFYLEGGFSKFQTDFPAMC 147
Cdd:cd01446  80 VYDESSSDRERLREdstAESVLGKLLRKL-QEGCSVYLLKGGFEQFSSEFPELC 132
DSP_DUSP1 cd14638
dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual ...
 206-359 4.05e-42

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: 144.82  E-value: 4.05e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFEnaGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14638   1 PVEILPFLYLGSAYHASRKDMLDTLGITALINVSANCPNHFE--GHYQYKSIPVEDNHKADISSWFNEAIDFIDSVKNAG 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTLgLKSPCDNRVPAP 359
Cdd:cd14638  79 GRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQV-LAPSCSAEAGSP 151
DSP_DUSP8 cd14645
dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual ...
 202-346 5.43e-41

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: 141.69  E-value: 5.43e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 202 QPSFPV------EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMfENAGEFKYKQIPISDHWSQNLSQFFPEAI 275
Cdd:cd14645   2 QPCLPVanvgptRILPHLYLGSQKDVLNKDLMAQNGITYVLNASNSCPKP-DFICESHFMRIPVNDNYCEKLLPWLDKSI 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35902878 276 SFIDEARGLKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 346
Cdd:cd14645  81 EFIDKAKVSNCRVIVHCLAGISRSATIAIAYIMKTMGLSSDDAYRFVKDRRPSISPNFNFLGQLLEYEKSL 151
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 206-343 1.88e-38

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: 134.66  E-value: 1.88e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFEnaGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14639   1 PVEILPFLYLGSAYHASKCEFLANLHITALLNVSRRSSEACK--GQYHYKWIPVEDSHTADISSHFQEAIDFIDCVRRAG 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFE 343
Cdd:cd14639  79 GKVLVHCEAGISRSPTICMAYLMKTKRFRLEEAFDYIKQRRSLISPNFGFMGQLLQYE 136
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 206-346 1.74e-37

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: 132.46  E-value: 1.74e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMfENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14646   3 PTRILPHLYLGCQRDVLNKELMQQNGIGYVLNASNTCPKP-DFIPESHFLRVPVNDSFCEKILPWLDKSVDFIEKAKASN 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 346
Cdd:cd14646  82 GRVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPTISPNFNFLGQLLDFEKKI 142
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 207-343 9.57e-37

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: 130.17  E-value: 9.57e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 207 VEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENagEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLKC 286
Cdd:cd14523   3 GVIKPWLLLSSQDVAHDLETLKKHKVTHILNVAYGVENAFPD--DFTYKTISILDLPETDITSYFPECFEFIDEAKSQDG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 35902878 287 GVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFE 343
Cdd:cd14523  81 VVLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNARPSIRPNPGFMEQLKEYQ 137
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 209-343 8.44e-36

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: 127.48  E-value: 8.44e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 209 ILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFEnagEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLKCGV 288
Cdd:cd14519   4 ILPGLYVGNFRDAKDAEQLRENGITHILSIHDSARPLLE---DIKYLCIPAADTPEQNISQHFRECINFIHEARLNGGNV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 35902878 289 LVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFE 343
Cdd:cd14519  81 LVHCLAGVSRSVTIVAAYLMTVTDLGWRDALKAVRAARPCANPNFGFQRQLQEFE 135
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 206-343 1.14e-35

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: 127.13  E-value: 1.14e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFenAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14513   1 ASKIFDHLYLGSEWNASNLEELQNNGVKYILNVTREIDNFF--PGRFTYHNIRVWDEESTNLLPYWNETYRFIKEARRKG 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFE 343
Cdd:cd14513  79 SKVLVHCKMGVSRSASTVIAYAMKEYGWSLEQALEHVKERRSCIKPNPGFLRQLITYE 136
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
 206-345 1.11e-33

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: 122.36  E-value: 1.11e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGlK 285
Cdd:cd14520   1 MKLVRPGLYIGNADDAADYLSLREAGITHVLTVDSEEPIDAPPVGKLVRKFVPALDEESTDLLSRLDECLDFIDEGRA-E 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERT 345
Cdd:cd14520  80 GAVLVHCHAGVSRSAAVVTAYLMKTEQLSFEEALASLRECKPDVKPNDGFLKQLKLYEAM 139
DUSP22 cd14581
dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), ...
 208-345 1.71e-33

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: 121.83  E-value: 1.71e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFEnagEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLKCG 287
Cdd:cd14581   6 KVLPGLYLGNFKDARDREQLSKNNITHILSVHDSARPMLE---GMTYLCIPAADSPSQNLTQHFKESIKFIHECRLRGEG 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 35902878 288 VLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERT 345
Cdd:cd14581  83 CLVHCLAGVSRSVTLVVAYIMTVTDFGWEDALSAVKAARSCANPNMGFQRQLQEFEKH 140
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 208-346 1.03e-30

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: 114.62  E-value: 1.03e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGEFKYKQ-------IPISDHWSQNLSQFFPEAISFIDE 280
Cdd:cd14515   3 EVWPGIYIGDESTAKNKAKLKKLGITHVLNAAEGKKNGEVNTNAKFYKGsgiiylgIPASDLPTFDISQYFDEAADFIDK 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 35902878 281 ARGLKCG-VLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKsNISPNFNFMGQLLDFERTL 346
Cdd:cd14515  83 ALSDPGGkVLVHCVEGVSRSATLVLAYLMIYQNMTLEEAIRTVRKKR-EIRPNRGFLQQLCELNDKL 148
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 208-341 1.98e-30

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: 113.03  E-value: 1.98e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLGCAkDSTNLDILEEFGIKYILNVTPNLPNMfeNAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARgLKCG 287
Cdd:cd14514   3 QITPHLFLSGA-SAATPPLLLSRGITCIINATTELPDP--SYPGIEYLRVPVEDSPHADLSPHFDEVADKIHQVK-RRGG 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 35902878 288 -VLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLD 341
Cdd:cd14514  79 rTLVHCVAGVSRSATLCLAYLMKYEGMTLREAYKHVKAARPIIRPNVGFWRQLIE 133
DSP_STYXL1 cd14517
dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; ...
 203-346 7.76e-30

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


Pssm-ID: 350367 [Multi-domain]  Cd Length: 155  Bit Score: 112.37  E-value: 7.76e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 203 PSFPVEILP-HLYLGCAKDSTNLDILEEFGIKYILNVTPNlPNMFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEA 281
Cdd:cd14517   8 KTYPVEILPgFLYMGNYKQACDKKIQKDLKIKAHINVSMD-ADELFKSGNDQVLHIPVEDSVEADLLSFFERACSFIDKH 86

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 35902878 282 RGLKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 346
Cdd:cd14517  87 KNNGSRVLVFSTLGISRSVAVAIAYLMYHYKWSLKDAWKYLLKCKNNMRPNRGFVKQLSEWEEKL 151
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
 206-339 8.59e-30

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: 112.03  E-value: 8.59e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTP-NLPNMFENagEFKYKQIPISDHWSQNLSQFFPEAISFIDEA--- 281
Cdd:cd14518   1 LSRILGGLYLGGIEPLNRNRLLKAENITHILSVIPgDVPEEYFK--GYEHKQIEIDDVEDENILQHFPETNRFIDSAlfg 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 35902878 282 --------RGLKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQL 339
Cdd:cd14518  79 ngkdedeeKKHGGAVLVHCAMGKSRSVTVVIAYLMYKYNLSVSQALHAVRRKRPIAEPNDGFMEQL 144
DSP_slingshot_1 cd14570
dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein ...
 206-346 1.81e-29

dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein phosphatase slingshot homolog 1 (SSH1), also called SSH-like protein 1, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. SSH1 links NOD1 signaling to actin remodeling, facilitating the changes that leads to NF-kappaB activation and innate immune responses. There are at least two human SSH1 isoforms reported: hSSH-1L (long) and hSSH-1S (short). As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. They also contain C-terminal tails, differing in the lengths of the tail.


Pssm-ID: 350418 [Multi-domain]  Cd Length: 144  Bit Score: 110.93  E-value: 1.81e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFenAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14570   4 ASLIFDHLYLGSEWNASNLEELQGSGVGYILNVTREIDNFF--PGLFAYHNIRVYDEETTDLLAHWNDAYHFINKAKKNH 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 346
Cdd:cd14570  82 SKCLVHCKMGVSRSASTVIAYAMKEFGWSLEKAYNFVKQKRSITRPNAGFMRQLLEYEGIL 142
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 208-343 4.10e-28

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: 107.80  E-value: 4.10e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLG--CAKDSTNLDILEEFGIKYILNVTPNL------PNMFENageFKYKQIPISDHWSQNLSQFFPEAISFID 279
Cdd:cd14522   7 EILPGLYLGpySAAMKSKLEVLLKHGITHIVCVRQNIeanfikPNFPDH---FRYLVLDVADNPTENIIRHFPTVKEFID 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 35902878 280 EARGLKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFE 343
Cdd:cd14522  84 DCLQTGGKVLVHGNAGISRSAALVIAYIMETYGLSYRDAFAYVQQRRFCINPNEGFVHQLKEYE 147
DSP_slingshot_2 cd14569
dual specificity phosphatase domain of slingshot homolog 2; Dual specificity protein ...
 206-346 4.02e-26

dual specificity phosphatase domain of slingshot homolog 2; Dual specificity protein phosphatase slingshot homolog 2 (SSH2), also called SSH-like protein 2, 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. SSH2 has been identified as a target of protein kinase D1 that regulates cofilin phosphorylation and remodeling of the actin cytoskeleton during neutrophil chemotaxis. There are at least two human SSH2 isoforms reported: hSSH-2L (long) and hSSH-2. 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-2L contains a long C-terminal tail while hSSH-2 does not.


Pssm-ID: 350417 [Multi-domain]  Cd Length: 144  Bit Score: 102.02  E-value: 4.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFenAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEAR--G 283
Cdd:cd14569   4 PTQIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREIDNFF--PGLFEYHNIRVYDEEATDLLAYWNDTYKFISKAKkhG 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 35902878 284 LKCgvLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 346
Cdd:cd14569  82 SKC--LVHCKMGVSRSASTVIAYAMKEYGWNLDRAYDYVKERRTVTKPNPSFMRQLEEYQGIL 142
DSP_fungal_SDP1-like cd14521
dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, ...
 203-346 4.45e-26

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: 102.40  E-value: 4.45e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 203 PSFPVEIL-PHLYLGcAKDStnLDILEEFGIkyILNVTPNLPNMFENAGEFKYKQIPISD------------HWSQN--L 267
Cdd:cd14521   2 PDGPVCVLpPNIYLY-SEPT--LEEASSFDV--VINVAKEVKNPFLSDASLAEKEKTILPgqqvknpeyihvPWDHNsqI 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 35902878 268 SQFFPEAISFIDEARGLKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 346
Cdd:cd14521  77 QKDLPKLTSIIEDATQSGKKVLIHCQCGVSRSASLIIAYIMKKLGLSLNDAYDLLKSRSPWIGPNMSLIFQLMEFEKVL 155
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
 208-350 2.55e-24

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: 97.25  E-value: 2.55e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMfeNAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLKCG 287
Cdd:cd14572  10 QITPSLYLSRGNVASNRHLLLSRGITCIVNATIEIPNF--NWPQFEYVKVPLADMPHAPISLYFDSVADKIHSVGRKHGA 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 35902878 288 VLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTLGLKS 350
Cdd:cd14572  88 TLVHCAAGVSRSATLCIAYLMKYHRVSLLEAYNWVKARRPVIRPNVGFWRQLIDYERKLFGKS 150
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
 206-347 5.98e-24

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: 96.09  E-value: 5.98e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENagEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLK 285
Cdd:cd14571   4 PSRIFPYLYLGSEWNAANLEELQRNRVSHILNVTREIDNFFPE--RFTYMNIRVYDEEATQLLPHWKETHRFIEAARAQG 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTLG 347
Cdd:cd14571  82 TRVLVHCKMGVSRSASTVIAYAMKQYGWTLEQALRHVRERRPIVQPNPGFLRQLQTYQGILT 143
DSP_fungal_PPS1 cd14516
dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; ...
 204-343 1.07e-23

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: 96.57  E-value: 1.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 204 SFPVEILPHLYLGCAKDSTNLDILEEFGIKYILNV------TPNLPNMFENAGEFKYKQIPISDHWSQN----------- 266
Cdd:cd14516   5 SLPSRILPHLYLGSLNHASNATLLESLGITHIVSVgespswFSNLKIKYIFDFSLQDLSNLDSNSEGSLwaaeykglisv 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 267 -------------LSQFFPEAISFIDEARGLKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSN--ISP 331
Cdd:cd14516  85 lyihnlkddgidsLLPQLTDALDFIQKARLLGGKTLVHCRVGVSRSATVVIAEVMKHLRMSLVDAYLFVRVRRLNiiIQP 164

                       170
                ....*....|..
gi 35902878 332 NFNFMGQLLDFE 343
Cdd:cd14516 165 NLRFFYELFKWE 176
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 203-346 2.32e-22

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: 92.52  E-value: 2.32e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 203 PSFPV-EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAG-EF------KYKQIPISDHWSQNLSQFFPEA 274
Cdd:cd14579  17 PSQHCnEVYPRIYVGNASVAQNIMRLQRLGITHVLNAAEGKSFMHVNTNaEFyedtgiTYHGIKANDTQHFNLSAYFEEA 96

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 35902878 275 ISFIDEARGLKCG-VLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSnISPNFNFMGQLLDFERTL 346
Cdd:cd14579  97 ADFIDKALAQKNGrVLVHCREGYSRSPTLVIAYLMLRQKMDVKSALSTVRQKRE-IGPNDGFLKQLCQLNDKL 168
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 206-342 1.17e-21

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: 89.51  E-value: 1.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPH-LYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAgeFKYKQIpisdhwSQNLSQFFPEAISFIDEARGL 284
Cdd:cd18534   1 PTEILPGfLYLGSYDNASRAELLKAQGITRILNTVPDCQNLYKNS--FTYHVL------SEEKTVPFAEAVDFIEQCRKD 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 285 KCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKS--NISPnfNFMGQLLDF 342
Cdd:cd18534  73 KARVLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRPsiNLSP--AVAKQLQEF 130
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 208-346 2.38e-21

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: 89.46  E-value: 2.38e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFenAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLKCG 287
Cdd:cd14573   4 RITESLYLSNGVAANNRTLLAANRITCVINVSLEVANGL--PPGIEYLHVPVADSPDTRLRDYFDPIADKIHTVEARGGR 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 35902878 288 VLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 346
Cdd:cd14573  82 TLLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTWVKSCRPIIRPNNGFWEQLIHYEFEL 140
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
208-346 1.57e-20

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 86.56  E-value: 1.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGE--FKYKQIPISDHWSQNLSQFfPEAISFIDEARGLK 285
Cdd:COG2453   2 WIIPGLLAGGPLPGGGEADLKREGIDAVVSLTEEEELLLGLLEEagLEYLHLPIPDFGAPDDEQL-QEAVDFIDEALREG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLMqKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 346
Cdd:COG2453  81 KKVLVHCRGGIGRTGTVAAAYLV-LLGLSAEEALARVRAARPGAVETPAQRAFLERFAKRL 140
DUSP28 cd14574
dual specificity protein phosphatase 28; Dual specificity protein phosphatase 28 (DUSP28), ...
 209-346 3.31e-20

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: 85.98  E-value: 3.31e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 209 ILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPnmFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEA--RGLKC 286
Cdd:cd14574   4 VTDSLFISNARAACNEELLAREGVTLCVNVSRQQP--FPRAPRVSTLRVPVFDDPAEDLYRHFEQCADAIEAAvrRGGKC 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 287 gvLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 346
Cdd:cd14574  82 --LVYCKNGRSRSAAVCIAYLMKHRGLSLQDAFQVVKAARPVAEPNPGFWSQLQRYEEEL 139
DSP_DUSP15 cd14582
dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual ...
 208-342 3.03e-19

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: 83.46  E-value: 3.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFEnagEFKYKQIPISDHWSQNLSQFFPEAISFIDEAR--GLK 285
Cdd:cd14582   7 KVLPGLYLGNFIDAKDLEQLSRNKITHIISIHESPQPLLQ---DITYLRIPLPDTPEAPIKKHFKECISFIHQCRlnGGN 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 35902878 286 CgvLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDF 342
Cdd:cd14582  84 C--LVHCLAGISRSTTIVVAYVMAVTELSWQEVLEAIRAVRPIANPNPGFKQQLEEF 138
DUPD1 cd14575
dual specificity phosphatase and pro isomerase domain containing 1; Dual specificity ...
 208-349 2.52e-16

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


Pssm-ID: 350423 [Multi-domain]  Cd Length: 160  Bit Score: 75.63  E-value: 2.52e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMFENAGEFK-----YKQIPISDHWSQNLSQFFPEAISFIDEA- 281
Cdd:cd14575  13 EVWPGLYIGDEKTALDRYSLQKLGITHILNAAHGKWNVDTGAEYYKdmtihYYGVEADDLPTFNLSQFFYSAAEFIHQAl 92

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 35902878 282 RGLKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVkMKKSNISPNFNFMGQLLDFERTLGLK 349
Cdd:cd14575  93 SDPHNKLLVHCVMGRSRSATLVLAYLMIYKNMTVVDAIEQV-AQRRCILPNRGFLKQLRELDIQLAEE 159
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
 208-346 3.49e-16

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: 74.79  E-value: 3.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNlpNMFENAGE------FKYKQIPISDHWSQNLSQFFPEAISFIDEA 281
Cdd:cd14580   3 EVWPNLFLGDLATAHNRFGLWKLGITHVLNAAHG--KLFCQGGDdfygtsVDYYGVPANDLPDFDISPYFYSAAEFIHRA 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 35902878 282 RGLKCG-VLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSnISPNFNFMGQLLDFERTL 346
Cdd:cd14580  81 LNTPGAkVLVHCAVGVSRSATLVLAYLMIYHQLSLVQAIKTVKERRW-IFPNRGFLKQLRKLDQQL 145
DUSP26 cd14578
dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), ...
 208-346 1.92e-15

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: 72.56  E-value: 1.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNL----PNMFENAGeFKYKQIPISDHWSQNLSQFFPEAISFIDEA-R 282
Cdd:cd14578   3 EVWPGLYLGDQDIAANRRELRRLGITHILNASHSKwrggAEYYEGLN-IRYLGIEAHDSPAFDMSIHFYPAADFIHRAlS 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 35902878 283 GLKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSnISPNFNFMGQLLDFERTL 346
Cdd:cd14578  82 QPGGKILVHCAVGVSRSATLVLAYLMIHHHMTLVEAIKTVKDHRG-IIPNRGFLRQLLALDRRL 144
DUSP13B cd14577
dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 ...
 208-346 2.56e-15

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: 72.91  E-value: 2.56e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLPNMfeNAGEFKYKQIPIS-------DHWSQNLSQFFPEAISFIDE 280
Cdd:cd14577  20 EVWPNLYLGDAYAARDKSVLIQLGITHIVNAASGKFHV--NTGPKFYRDMNIDyygveadDNPFFDLSVYFYPVARFIRA 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 35902878 281 ARGLKCG-VLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKmKKSNISPNFNFMGQLLDFERTL 346
Cdd:cd14577  98 ALSSPNGrVLVHCAMGISRSATLVLAFLMICEDLTLVDAIQTVR-AHRDICPNSGFLRQLRELDNRL 163
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 208-327 3.29e-13

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: 66.45  E-value: 3.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLG-CAKDSTNLDILEEFGIKYILN-----------VTPnlPNMFENA--GEFKYKQIPISDHWSQNLSQFFPE 273
Cdd:cd14526   5 RILPNLIVGsCPQNPEDVDRLKKEGVTAVLNlqtdsdmeywgVDI--DSIRKACkeSGIRYVRLPIRDFDTEDLRQKLPQ 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 35902878 274 AISFIDEARGLKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKS 327
Cdd:cd14526  83 AVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRP 136
PRK12361 PRK12361
hypothetical protein; Provisional
 208-333 7.56e-13

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 69.65  E-value: 7.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878  208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNLP----NMFENagEFKYKQIPISDHWSQNLSQFFpEAISFIDEARG 283
Cdd:PRK12361  97 KIDENLYLGCRLFPADLEKLKSNKITAILDVTAEFDgldwSLTEE--DIDYLNIPILDHSVPTLAQLN-QAINWIHRQVR 173

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 35902878  284 LKCGVLVHCLAGISRSVTVTVAYLM-QKLNLSMNDAYDIVKMKKSNISPNF 333
Cdd:PRK12361 174 ANKSVVVHCALGRGRSVLVLAAYLLcKDPDLTVEEVLQQIKQIRKTARLNK 224
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 206-323 7.86e-13

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: 64.99  E-value: 7.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCAKDSTNLDIleefGIKYILNVTPNLPNmfeNAGEFKYKQIPISDHWSQNLSQFfPEAISFIDEARGLK 285
Cdd:cd14527   5 YDEVLPGLYLGRWPSADELPP----GVPAVLDLTAELPR---PRKRQAYRCVPLLDLVAPTPEQL-ERAVAWIEELRAQG 76

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 35902878 286 CGVLVHCLAGISRSVTVTVAYLM-QKLNLSMNDAYDIVK 323
Cdd:cd14527  77 GPVLVHCALGYGRSATVVAAWLLaYGRAKSVAEAEALIR 115
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 223-318 4.40e-12

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: 63.07  E-value: 4.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 223 NLDILEEFGIKYILNVTPNLPNM-FENAGEFKYKQIPISDHWSQNLSQFfPEAISFIDEARGLKCGVLVHCLAGISRSVT 301
Cdd:cd14504  20 HYAYLNENGIRHVVTLTEEPPPEhSDTCPGLRYHHIPIEDYTPPTLEQI-DEFLDIVEEANAKNEAVLVHCLAGKGRTGT 98

                        90
                ....*....|....*..
gi 35902878 302 VTVAYLMQKLNLSMNDA 318
Cdd:cd14504  99 MLACYLVKTGKISAVDA 115
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 234-331 1.14e-11

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: 62.28  E-value: 1.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 234 YILNVTPNLPNMFENAGeFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLKCGVLVHCLAGISRSVTVTVAYLMQKLNL 313
Cdd:cd14524  39 YETRFFCNSKEEWKALG-VEQLRLPTVDFTGVPSLEDLEKGVDFILKHREKGKSVYVHCKAGRGRSATIVACYLIQHKGW 117

                        90
                ....*....|....*...
gi 35902878 314 SMNDAYDIVKMKKSNISP 331
Cdd:cd14524 118 SPEEAQEFLRSKRPHILL 135
DSP_iDUSP27 cd14576
dual specificity phosphatase-like domain of inactive dual specificity protein phosphatase 27; ...
 208-346 1.40e-11

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: 62.19  E-value: 1.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 208 EILPHLYLGCAKDSTNLDILEEFGIKYILNVTPNL-----PNmFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEA- 281
Cdd:cd14576  13 EVWPNVFIAEKSVAVNKGRLKRLGITHVLNAAHGTgvytgPE-FYSGMNIQYMGIEVDDFPDVDISKHFRKGAEFLDEAl 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 35902878 282 ---RGlkcGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKmKKSNISPNFNFMGQLLDFERTL 346
Cdd:cd14576  92 ltyRG---KVLVSSEMGISRSAVLVAAYLMIFHNMTIMEALMTLR-KKRAIYPNEGFLKQLRELNEKL 155
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 30-145 5.69e-11

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 58.62  E-value: 5.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878     30 RRDCLLVmDCRAQELYESSHVETAINVAIPSLMLRRLKKGNLPIKSLLsngedreRFARRCKTDTIVLYDEYSREWneni 109
Cdd:smart00450   2 DEKVVLL-DVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELL-------KRLGLDKDKPVVVYCRSGNRS---- 69

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 35902878    110 dggSVLGLLLRRMkdeGYK-AFYLEGGFSKFQTDFPA 145
Cdd:smart00450  70 ---AKAAWLLREL---GFKnVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 31-140 3.40e-10

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 56.34  E-value: 3.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878    31 RDCLLVMDCRAQELYESSHVETAINVAIPSLMLRRLKKGNLPiksllsngedrERFARRCKTDTIVLYDeysrewneniD 110
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELL-----------EKLLELLKDKPIVVYC----------N 61

                          90       100       110
                  ....*....|....*....|....*....|.
gi 35902878   111 GGSVLGLLLRRMKDEGY-KAFYLEGGFSKFQ 140
Cdd:pfam00581  62 SGNRAAAAAALLKALGYkNVYVLDGGFEAWK 92
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 206-331 1.34e-09

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: 55.43  E-value: 1.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 206 PVEILPHLYLGCA----KDSTNLDILEEFGIKYILNVTPnlpnmfenagefkykqipisdhwsqnlsQFFPEAISFIDEA 281
Cdd:cd14494   1 FNWIDPLRLIAGAlplsPLEADSRFLKQLGVTTIVDLTL----------------------------AMVDRFLEVLDQA 52

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 35902878 282 RGLKCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISP 331
Cdd:cd14494  53 EKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPGGIP 102
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 288-330 1.05e-04

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 42.18  E-value: 1.05e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 35902878 288 VLVHCLAGISRSVTVTVAYLM-QKLNLSMNDAYDIVKMKKSNIS 330
Cdd:cd14497  98 AVVHCKAGKGRTGTVICAYLLyYGQYSTADEALEYFAKKRFKEG 141
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
288-324 1.80e-04

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 40.42  E-value: 1.80e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 35902878    288 VLVHCLAGISRSVT-VTVAYLMQKLNLSMN--DAYDIVKM 324
Cdd:smart00404  42 VVVHCSAGVGRTGTfVAIDILLQQLEAEAGevDIFDTVKE 81
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 288-324 1.80e-04

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 40.42  E-value: 1.80e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 35902878    288 VLVHCLAGISRSVT-VTVAYLMQKLNLSMN--DAYDIVKM 324
Cdd:smart00012  42 VVVHCSAGVGRTGTfVAIDILLQQLEAEAGevDIFDTVKE 81
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 23-140 2.22e-04

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 39.59  E-value: 2.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878  23 LKEQLETRRDCLLvmDCRAQELYESSHVETAINvaIPslmlrrlkkgnlpikslLSNGEDRERFARRCKTDTIVLYDEys 102
Cdd:cd00158   2 LKELLDDEDAVLL--DVREPEEYAAGHIPGAIN--IP-----------------LSELEERAALLELDKDKPIVVYCR-- 58

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 35902878 103 rewnenidGGSVLGLLLRRMKDEGY-KAFYLEGGFSKFQ 140
Cdd:cd00158  59 --------SGNRSARAAKLLRKAGGtNVYNLEGGMLAWK 89
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 227-323 3.02e-03

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: 38.01  E-value: 3.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902878 227 LEEFGIkyilnvtPNLPNMFENAGeFKYKQIPISDHWSQNLSQFFPEAISFIDEARGLKCGVLVHCLAGISRSVTVTVAY 306
Cdd:cd14505  56 LEELGV-------PDLLEQYQQAG-ITWHHLPIPDGGVPSDIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACL 127

                        90
                ....*....|....*...
gi 35902878 307 LMQ-KLNLSMNDAYDIVK 323
Cdd:cd14505 128 LLElGDTLDPEQAIAAVR 145
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
288-324 3.45e-03

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 38.79  E-value: 3.45e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 35902878    288 VLVHCLAGISRSVT-VTVAYLMQKLNLSMN-DAYDIVKM 324
Cdd:smart00194 197 IVVHCSAGVGRTGTfIAIDILLQQLEAGKEvDIFEIVKE 235
 
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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