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Conserved domains on  [gi|171689904|ref|XP_001909891|]
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uncharacterized protein PODANS_6_3960 [Podospora anserina S mat+]

Protein Classification

dual specificity protein phosphatase family protein( domain architecture ID 12998330)

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_fungal_PPS1 cd14516
dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; ...
 522-692 1.79e-75

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: 240.64  E-value: 1.79e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 522 FDGSFPSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAMWRDGE--------------------------LEQWGE 575
Cdd:cd14516    2 FDGSLPSRILPHLYLGSLNHASNATLLESLGITHIVSVGESPSWFSNLkikyifdfslqdlsnldsnsegslwaAEYKGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 576 ENTCVVQGVQDNGIDPLTDEFERCLEFIgkfpfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMR 655
Cdd:cd14516   82 ISVLYIHNLKDDGIDSLLPQLTDALDFI---------------------QKARLLGGKTLVHCRVGVSRSATVVIAEVMK 140

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 171689904 656 SLRMSFPRAYCFVRARRLNVIIQPHLRFGYELLKWEE 692
Cdd:cd14516  141 HLRMSLVDAYLFVRVRRLNIIIQPNLRFFYELFKWEE 177
 
Name Accession Description Interval E-value
DSP_fungal_PPS1 cd14516
dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; ...
 522-692 1.79e-75

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: 240.64  E-value: 1.79e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 522 FDGSFPSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAMWRDGE--------------------------LEQWGE 575
Cdd:cd14516    2 FDGSLPSRILPHLYLGSLNHASNATLLESLGITHIVSVGESPSWFSNLkikyifdfslqdlsnldsnsegslwaAEYKGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 576 ENTCVVQGVQDNGIDPLTDEFERCLEFIgkfpfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMR 655
Cdd:cd14516   82 ISVLYIHNLKDDGIDSLLPQLTDALDFI---------------------QKARLLGGKTLVHCRVGVSRSATVVIAEVMK 140

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 171689904 656 SLRMSFPRAYCFVRARRLNVIIQPHLRFGYELLKWEE 692
Cdd:cd14516  141 HLRMSLVDAYLFVRVRRLNIIIQPNLRFFYELFKWEE 177
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
527-693 2.93e-26

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 104.67  E-value: 2.93e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904   527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAMWrdgeLEQWGEENTCVVqgVQDNGIDPLTDEFERCLEFIgkf 606
Cdd:smart00195   1 PSEILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPN----YNGSDFTYLGVP--IDDNTETKISPYFPEAVEFI--- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904   607 pfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGYE 686
Cdd:smart00195  72 ------------------EDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRR--PIISPNFGFLRQ 131


                   ....*..
gi 171689904   687 LLKWEEQ 693
Cdd:smart00195 132 LIEYERK 138
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 535-691 1.43e-14

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: 70.75  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904  535 YLGNLGHANNPdLLKSLGIGQILSVGELAMWRDGELEQ---WGEENTCvvqgvqdngiDPLTDEFERCLEFIGKfpfgcf 611
Cdd:pfam00782   2 YLGSKPTASDA-FLSKLGITAVINVTREVDLYNSGILYlriPVEDNHE----------TNISKYLEEAVEFIDD------ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904  612 lpspkikltnpATERGRRngtaTLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGYELLKWE 691
Cdd:pfam00782  65 -----------ARQKGGK----VLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERR--PGISPNFGFKRQLLEYE 127
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
584-693 8.96e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 45.73  E-value: 8.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 584 VQDNGIDP---LTDEFERCLEFIGKFPFGCF--------LPSPK-IKLTNPATERGRRNGTATLVHCRVGVSRSATICIA 651
Cdd:COG2453   21 LKREGIDAvvsLTEEEELLLGLLEEAGLEYLhlpipdfgAPDDEqLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAA 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 171689904 652 eVMRSLRMSFPRAYCFVRARRLNVIIQP-HLRFgyeLLKWEEQ 693
Cdd:COG2453  101 -YLVLLGLSAEEALARVRAARPGAVETPaQRAF---LERFAKR 139
 
Name Accession Description Interval E-value
DSP_fungal_PPS1 cd14516
dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; ...
 522-692 1.79e-75

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: 240.64  E-value: 1.79e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 522 FDGSFPSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAMWRDGE--------------------------LEQWGE 575
Cdd:cd14516    2 FDGSLPSRILPHLYLGSLNHASNATLLESLGITHIVSVGESPSWFSNLkikyifdfslqdlsnldsnsegslwaAEYKGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 576 ENTCVVQGVQDNGIDPLTDEFERCLEFIgkfpfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMR 655
Cdd:cd14516   82 ISVLYIHNLKDDGIDSLLPQLTDALDFI---------------------QKARLLGGKTLVHCRVGVSRSATVVIAEVMK 140

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 171689904 656 SLRMSFPRAYCFVRARRLNVIIQPHLRFGYELLKWEE 692
Cdd:cd14516  141 HLRMSLVDAYLFVRVRRLNIIIQPNLRFFYELFKWEE 177
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 527-683 2.20e-29

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: 113.41  E-value: 2.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAMWRDGEleqwGEENTCVVQgVQDNGIDPLTDEFERCLEFIgkf 606
Cdd:cd14498    1 PSEILPGLYLGSLDAAQDKELLKKLGITHILNVAGEPPPNKFP----DGIKYLRIP-IEDSPDEDILSHFEEAIEFI--- 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171689904 607 pfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLnvIIQPHLRF 683
Cdd:cd14498   73 ------------------EEALKKGGKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRP--IISPNPGF 129
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
527-693 2.93e-26

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 104.67  E-value: 2.93e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904   527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAMWrdgeLEQWGEENTCVVqgVQDNGIDPLTDEFERCLEFIgkf 606
Cdd:smart00195   1 PSEILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPN----YNGSDFTYLGVP--IDDNTETKISPYFPEAVEFI--- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904   607 pfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGYE 686
Cdd:smart00195  72 ------------------EDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRR--PIISPNFGFLRQ 131


                   ....*..
gi 171689904   687 LLKWEEQ 693
Cdd:smart00195 132 LIEYERK 138
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 527-696 5.15e-22

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: 92.89  E-value: 5.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSV---------GELAMwrdgeleqwgeenTCVVQGVQDNGIDPLTDEFE 597
Cdd:cd14567    1 LTPILPFLYLGNERDAQDIDTLQRLNIGYVLNVtthlplyheGKGGF-------------RYKRLPATDSNKQNLRQYFE 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 598 RCLEFIgkfpfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVII 677
Cdd:cd14567   68 EAFEFI---------------------EEAHQSGKGVLVHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKR--PII 124

                        170       180
                 ....*....|....*....|
gi 171689904 678 QPHLRFGYELLKWEEQ-NQG 696
Cdd:cd14567  125 SPNLNFMGQLLEFEEDlNNG 144
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 527-692 4.25e-21

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: 89.78  E-value: 4.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVgelamwrdgeleqwgeENTCVVQG-----------VQDNGIDPLTDE 595
Cdd:cd14568    1 PTRILPHLYLGSQRDVLDKDLMQRNGISYVLNV----------------SNTCPKPDfipdshflripVNDSYCEKLLPW 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 596 FERCLEFIgkfpfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnV 675
Cdd:cd14568   65 LDKAVEFI---------------------EKARASNKRVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKR--P 121

                        170
                 ....*....|....*..
gi 171689904 676 IIQPHLRFGYELLKWEE 692
Cdd:cd14568  122 TISPNFNFLGQLLEFEK 138
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 527-690 1.68e-19

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: 85.23  E-value: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAMWRDGEleqwGEENTCVVQgVQDNGIDPLTDEFERCLEFIgkf 606
Cdd:cd14512    1 PTRILPNLYLGSQRDSLNLELMQQLGIGYVLNVSNTCPNPDFI----GLFHYKRIP-VNDSFCQNISPWFDEAIEFI--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 607 pfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGYE 686
Cdd:cd14512   73 ------------------EEAKASNGGVLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKR--PTISPNFNFMGQ 132


                 ....
gi 171689904 687 LLKW 690
Cdd:cd14512  133 LLDF 136
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 527-693 1.99e-19

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: 85.13  E-value: 1.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAmwrdgeleqwgeENTCVVQ------GVQDNGIDPLTDEFERCL 600
Cdd:cd14565    1 PVEILPFLYLGSAYHASRREVLKALGITAVLNVSRNC------------PNHFEDHfqyksiPVEDSHNADISSWFEEAI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 601 EFIGKFpfgcflpspkikltnpatergRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPH 680
Cdd:cd14565   69 GFIDKV---------------------KASGGRVLVHCQAGISRSATICLAYLMTTRRVRLNEAFDYVKQRR--SVISPN 125

                        170
                 ....*....|...
gi 171689904 681 LRFGYELLKWEEQ 693
Cdd:cd14565  126 FNFMGQLLQYESQ 138
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 527-688 1.01e-17

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: 80.06  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGE---LAMWRDGELEqwgeentcVVQ-GVQDNGIDPLTDEFERCLEF 602
Cdd:cd14566    1 PVEILPFLYLGNAKDSANIDLLKKYNIKYILNVTPnlpNTFEEDGGFK--------YLQiPIDDHWSQNLSAFFPEAISF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 603 IgkfpfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLNviIQPHLR 682
Cdd:cd14566   73 I---------------------DEARSKKCGVLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKRKSN--ISPNFN 129


                 ....*.
gi 171689904 683 FGYELL 688
Cdd:cd14566  130 FMGQLL 135
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 527-683 6.79e-17

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: 77.59  E-value: 6.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANnPDLLKSLGIGQILSV-GELAMWRDGELEqwgeentCVVQGVQDNGIDPLTDEFERCLEFIgk 605
Cdd:cd14514    1 ISQITPHLFLSGASAAT-PPLLLSRGITCIINAtTELPDPSYPGIE-------YLRVPVEDSPHADLSPHFDEVADKI-- 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171689904 606 fpfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRF 683
Cdd:cd14514   71 -------------------HQVKRRGGRTLVHCVAGVSRSATLCLAYLMKYEGMTLREAYKHVKAAR--PIIRPNVGF 127
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 527-693 2.33e-16

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: 76.49  E-value: 2.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGElamwRDGELEQwGEENTCVVQgVQDNGIDPLTDEFERCLEFIgkf 606
Cdd:cd14639    1 PVEILPFLYLGSAYHASKCEFLANLHITALLNVSR----RSSEACK-GQYHYKWIP-VEDSHTADISSHFQEAIDFI--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 607 pfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGYE 686
Cdd:cd14639   72 ------------------DCVRRAGGKVLVHCEAGISRSPTICMAYLMKTKRFRLEEAFDYIKQRR--SLISPNFGFMGQ 131


                 ....*..
gi 171689904 687 LLKWEEQ 693
Cdd:cd14639  132 LLQYESE 138
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
 527-693 3.54e-16

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: 75.84  E-value: 3.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSV-GELAMWRDGELEQwgeenTCVvqGVQDNGIDPLTDEFERCLEFIGK 605
Cdd:cd14640    1 PVEILPFLYLGSAYHAARRDMLDALGITALLNVsSDCPNHFEGHYQY-----KCI--PVEDNHKADISSWFMEAIEYIDS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 606 FpfgcflpspkikltnpATERGRrngtaTLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGY 685
Cdd:cd14640   74 V----------------KDCNGR-----VLVHCQAGISRSATICLAYLMMKKRVRLEEAFEFVKQRR--SIISPNFSFMG 130


                 ....*...
gi 171689904 686 ELLKWEEQ 693
Cdd:cd14640  131 QLLQFESQ 138
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
 527-693 4.38e-15

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: 72.97  E-value: 4.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAMWRDGELEQWgeenTCVvqGVQDNGIDPLTDEFERCLEFIGKF 606
Cdd:cd14641    4 PVEILPFLFLGSAHHSSRRETLESLGITAVLNVSSSCPNYFEGQFQY----KSI--PVEDSHMADISAWFQEAIDFIDSV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 607 pfgcflpspkikltnpatergRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGYE 686
Cdd:cd14641   78 ---------------------KNSGGRVLVHCQAGISRSATICLAYLIQSQRVRLDEAFDFVKQRR--GVISPNFSFMGQ 134


                 ....*..
gi 171689904 687 LLKWEEQ 693
Cdd:cd14641  135 LLQFETQ 141
DSP_DUSP1 cd14638
dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual ...
 527-693 1.11e-14

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: 72.02  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAMWRDGELEQWGEentcvvQGVQDNGIDPLTDEFERCLEFIGKF 606
Cdd:cd14638    1 PVEILPFLYLGSAYHASRKDMLDTLGITALINVSANCPNHFEGHYQYKS------IPVEDNHKADISSWFNEAIDFIDSV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 607 pfgcflpspkikltnpatergRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGYE 686
Cdd:cd14638   75 ---------------------KNAGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRR--SIISPNFSFMGQ 131


                 ....*..
gi 171689904 687 LLKWEEQ 693
Cdd:cd14638  132 LLQFESQ 138
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 535-691 1.43e-14

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: 70.75  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904  535 YLGNLGHANNPdLLKSLGIGQILSVGELAMWRDGELEQ---WGEENTCvvqgvqdngiDPLTDEFERCLEFIGKfpfgcf 611
Cdd:pfam00782   2 YLGSKPTASDA-FLSKLGITAVINVTREVDLYNSGILYlriPVEDNHE----------TNISKYLEEAVEFIDD------ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904  612 lpspkikltnpATERGRRngtaTLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGYELLKWE 691
Cdd:pfam00782  65 -----------ARQKGGK----VLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERR--PGISPNFGFKRQLLEYE 127
DSP_STYXL1 cd14517
dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; ...
 534-698 1.59e-13

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: 68.84  E-value: 1.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 534 MYLGNLGHANNPDLLKSLGIGQILSVGElamwrDGELEQWGEENTCVVQGVQDNGIDPLTDEFERCLEFIGKFpfgcflp 613
Cdd:cd14517   19 LYMGNYKQACDKKIQKDLKIKAHINVSM-----DADELFKSGNDQVLHIPVEDSVEADLLSFFERACSFIDKH------- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 614 spkikltnpatergRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLNviIQPHLRFGYELLKWEEQ 693
Cdd:cd14517   87 --------------KNNGSRVLVFSTLGISRSVAVAIAYLMYHYKWSLKDAWKYLLKCKNN--MRPNRGFVKQLSEWEEK 150


                 ....*
gi 171689904 694 NQGEG 698
Cdd:cd14517  151 LLGTT 155
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 527-691 2.07e-13

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: 67.80  E-value: 2.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVG-ELAMWRDGELEQ-----WGEENTCVVQgvqdngidpltdEFERCL 600
Cdd:cd14513    1 ASKIFDHLYLGSEWNASNLEELQNNGVKYILNVTrEIDNFFPGRFTYhnirvWDEESTNLLP------------YWNETY 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 601 EFIgkfpfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPH 680
Cdd:cd14513   69 RFI---------------------KEARRKGSKVLVHCKMGVSRSASTVIAYAMKEYGWSLEQALEHVKERR--SCIKPN 125

                        170
                 ....*....|.
gi 171689904 681 LRFGYELLKWE 691
Cdd:cd14513  126 PGFLRQLITYE 136
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
 627-693 5.31e-13

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: 67.20  E-value: 5.31e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171689904 627 GRRNGtATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGYELLKWEEQ 693
Cdd:cd14572   82 GRKHG-ATLVHCAAGVSRSATLCIAYLMKYHRVSLLEAYNWVKARR--PVIRPNVGFWRQLIDYERK 145
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 528-692 1.48e-12

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: 65.46  E-value: 1.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 528 SRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAMWRDGELEQwgeenTCVVqgVQDNGIDPLTDEFERCLEFIgkfp 607
Cdd:cd14519    2 NKILPGLYVGNFRDAKDAEQLRENGITHILSIHDSARPLLEDIKY-----LCIP--AADTPEQNISQHFRECINFI---- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 608 fgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGYEL 687
Cdd:cd14519   71 -----------------HEARLNGGNVLVHCLAGVSRSVTIVAAYLMTVTDLGWRDALKAVRAAR--PCANPNFGFQRQL 131


                 ....*
gi 171689904 688 LKWEE 692
Cdd:cd14519  132 QEFEK 136
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
 534-670 1.63e-12

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: 65.35  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 534 MYLGNLGHANNPDLLKSLGIGQILSVGELAMWRDGELEQWgeeNTCVVQGVQDNGIDpLTDEFERCLEFIgkfpfgcflp 613
Cdd:cd14520    8 LYIGNADDAADYLSLREAGITHVLTVDSEEPIDAPPVGKL---VRKFVPALDEESTD-LLSRLDECLDFI---------- 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 171689904 614 spkikltnpatERGRRNGtATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRA 670
Cdd:cd14520   74 -----------DEGRAEG-AVLVHCHAGVSRSAAVVTAYLMKTEQLSFEEALASLRE 118
DSP_slingshot_1 cd14570
dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein ...
 527-691 3.72e-12

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: 64.32  E-value: 3.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGElamwrdgELEQWGEENTCVVQ-GVQDNGIDPLTDEFERCLEFIGK 605
Cdd:cd14570    4 ASLIFDHLYLGSEWNASNLEELQGSGVGYILNVTR-------EIDNFFPGLFAYHNiRVYDEETTDLLAHWNDAYHFINK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 606 fpfgcflpspkikltnpaterGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGY 685
Cdd:cd14570   77 ---------------------AKKNHSKCLVHCKMGVSRSASTVIAYAMKEFGWSLEKAYNFVKQKR--SITRPNAGFMR 133


                 ....*.
gi 171689904 686 ELLKWE 691
Cdd:cd14570  134 QLLEYE 139
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
 527-695 3.78e-12

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: 64.65  E-value: 3.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAM----WRDGELEQW---GEENTCVVQgvqdngidpltdEFERC 599
Cdd:cd14518    1 LSRILGGLYLGGIEPLNRNRLLKAENITHILSVIPGDVpeeyFKGYEHKQIeidDVEDENILQ------------HFPET 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 600 LEFI--GKFPFGcflpspkikltnPATERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVII 677
Cdd:cd14518   69 NRFIdsALFGNG------------KDEDEEKKHGGAVLVHCAMGKSRSVTVVIAYLMYKYNLSVSQALHAVRRKR--PIA 134

                        170
                 ....*....|....*...
gi 171689904 678 QPHLRFGYELLKWEEQNQ 695
Cdd:cd14518  135 EPNDGFMEQLELYHEMGC 152
DSP_DUSP8 cd14645
dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual ...
 527-692 9.22e-12

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: 63.49  E-value: 9.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAMWRDgeleqWGEENTCVVQGVQDNGIDPLTDEFERCLEFIGkf 606
Cdd:cd14645   12 PTRILPHLYLGSQKDVLNKDLMAQNGITYVLNASNSCPKPD-----FICESHFMRIPVNDNYCEKLLPWLDKSIEFID-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 607 pfgcflpspKIKLTNpatergrrngTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLNviIQPHLRFGYE 686
Cdd:cd14645   85 ---------KAKVSN----------CRVIVHCLAGISRSATIAIAYIMKTMGLSSDDAYRFVKDRRPS--ISPNFNFLGQ 143


                 ....*.
gi 171689904 687 LLKWEE 692
Cdd:cd14645  144 LLEYEK 149
DSP_DUSP7 cd14643
dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual ...
 525-691 2.60e-11

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: 62.34  E-value: 2.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 525 SFPSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAmwrDGELEQWGEENTCVVQgVQDNGIDPLTDEFERCLEFIg 604
Cdd:cd14643    4 AFPVQILPYLYLGCAKDSTNLDVLGKYGIKYILNVTPNL---PNMFEHDGEFKYKQIP-ISDHWSQNLSQFFPEAISFI- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 605 kfpfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLNviIQPHLRFG 684
Cdd:cd14643   79 --------------------DEARSKKCGILVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDFVKRKKSN--ISPNFNFM 136


                 ....*..
gi 171689904 685 YELLKWE 691
Cdd:cd14643  137 GQLLDFE 143
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 527-693 4.78e-11

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: 61.20  E-value: 4.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAMWRDgeleqWGEENTCVVQGVQDNGIDPLTDEFERCLEFIgkf 606
Cdd:cd14646    3 PTRILPHLYLGCQRDVLNKELMQQNGIGYVLNASNTCPKPD-----FIPESHFLRVPVNDSFCEKILPWLDKSVDFI--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 607 pfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLNviIQPHLRFGYE 686
Cdd:cd14646   75 ------------------EKAKASNGRVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPT--ISPNFNFLGQ 134


                 ....*..
gi 171689904 687 LLKWEEQ 693
Cdd:cd14646  135 LLDFEKK 141
DSP_DUSP9 cd14644
dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual ...
 525-692 1.05e-10

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: 60.40  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 525 SFPSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGElamwrdgELEQWGEENtcvvqGVQDNGIDPLTDEFERCLEFig 604
Cdd:cd14644    1 SFPVQILPNLYLGSARDSANLETLAKLGIRYILNVTP-------NLPNFFEKN-----GDFHYKQIPISDHWSQNLSQ-- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 605 kfpfgcFLPSpKIKLTNPATERGrrngTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLNviIQPHLRFG 684
Cdd:cd14644   67 ------FFPE-AIEFIDEALSQN----CGVLVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDLVKRKKSN--ISPNFNFM 133


                 ....*...
gi 171689904 685 YELLKWEE 692
Cdd:cd14644  134 GQLLDFEK 141
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 527-679 1.26e-10

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: 59.47  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRIL-DYMYLGNLGHANNPDLLKSLGIGQILSVgelamWRDGeleQWGEENTCVVQGVQDNGIDPltdeFERCLEFIgk 605
Cdd:cd18534    1 PTEILpGFLYLGSYDNASRAELLKAQGITRILNT-----VPDC---QNLYKNSFTYHVLSEEKTVP----FAEAVDFI-- 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171689904 606 fpfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLNVIIQP 679
Cdd:cd18534   67 -------------------EQCRKDKARVLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRPSINLSP 121
DUSP28 cd14574
dual specificity protein phosphatase 28; Dual specificity protein phosphatase 28 (DUSP28), ...
 584-695 6.53e-10

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: 57.86  E-value: 6.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 584 VQDNGIDPLTDEFERCLEfigkfpfgcflpspkikltnpATERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPR 663
Cdd:cd14574   52 VFDDPAEDLYRHFEQCAD---------------------AIEAAVRRGGKCLVYCKNGRSRSAAVCIAYLMKHRGLSLQD 110

                         90       100       110
                 ....*....|....*....|....*....|..
gi 171689904 664 AYCFVRARRlnVIIQPHLRFGYELLKWEEQNQ 695
Cdd:cd14574  111 AFQVVKAAR--PVAEPNPGFWSQLQRYEEELQ 140
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
 527-687 6.60e-10

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: 57.95  E-value: 6.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVG--------ELAMWRDgeLEQWGEENTCVVqgvqdngidpltdefer 598
Cdd:cd14571    4 PSRIFPYLYLGSEWNAANLEELQRNRVSHILNVTreidnffpERFTYMN--IRVYDEEATQLL----------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 599 clefigkfpfgcflpsPKIKLTNPATERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQ 678
Cdd:cd14571   65 ----------------PHWKETHRFIEAARAQGTRVLVHCKMGVSRSASTVIAYAMKQYGWTLEQALRHVRERR--PIVQ 126


                 ....*....
gi 171689904 679 PHLRFGYEL 687
Cdd:cd14571  127 PNPGFLRQL 135
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 530-672 1.24e-09

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: 56.98  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 530 ILDYMYLGNLGHANNPDLLKSLGIGQILSVGelamwrdgeleqWGEENTCVVQ------GVQDNGIDPLTDEFERCLEFI 603
Cdd:cd14523    5 IKPWLLLSSQDVAHDLETLKKHKVTHILNVA------------YGVENAFPDDftyktiSILDLPETDITSYFPECFEFI 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171689904 604 gkfpfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARR 672
Cdd:cd14523   73 ---------------------DEAKSQDGVVLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNAR 120
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 528-697 1.89e-09

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: 57.11  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 528 SRILDYMYLGNLGHANNPDLLKSLGIGQILSVGElamwrdgeleqwgEENTCVVQGVQDNGIdPLTDEFERCLefigkfp 607
Cdd:cd14573    3 SRITESLYLSNGVAANNRTLLAANRITCVINVSL-------------EVANGLPPGIEYLHV-PVADSPDTRL------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 608 FGCFlpSPKIKLTNPATERGRRngtaTLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGYEL 687
Cdd:cd14573   62 RDYF--DPIADKIHTVEARGGR----TLLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTWVKSCR--PIIRPNNGFWEQL 133

                        170
                 ....*....|
gi 171689904 688 LKWEEQNQGE 697
Cdd:cd14573  134 IHYEFELFGK 143
DSP_fungal_SDP1-like cd14521
dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, ...
 617-692 2.54e-09

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: 56.56  E-value: 2.54e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171689904 617 IKLTNPATERGRRngtaTLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFV--RARRlnviIQPHLRFGYELLKWEE 692
Cdd:cd14521   84 TSIIEDATQSGKK----VLIHCQCGVSRSASLIIAYIMKKLGLSLNDAYDLLksRSPW----IGPNMSLIFQLMEFEK 153
DSP_DUSP6 cd14642
dual specificity phosphatase domain of dual specificity protein phosphatase 6; Dual ...
 525-691 2.60e-09

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: 56.24  E-value: 2.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 525 SFPSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAmwrDGELEQWGEENTCVVQgVQDNGIDPLTDEFERCLEFIG 604
Cdd:cd14642    1 SFPVEILPYLYLGCAKDSTNLDVLEEFGIKYILNVTPNL---PNLFENAGEFKYKQIP-ISDHWSQNLSQFFPEAISFID 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 605 KfpfgcflpspkikltnpatERGRRNGTatLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLNviIQPHLRFG 684
Cdd:cd14642   77 E-------------------ARGKNCGV--LVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSN--ISPNFNFM 133


                 ....*..
gi 171689904 685 YELLKWE 691
Cdd:cd14642  134 GQLLDFE 140
DUSP22 cd14581
dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), ...
 528-672 2.36e-08

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: 53.65  E-value: 2.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 528 SRILDYMYLGNLGHANNPDLLKSLGIGQILSVGELAmwrdgelEQWGEENTCVVQGVQDNGIDPLTDEFERCLEFIGKfp 607
Cdd:cd14581    5 NKVLPGLYLGNFKDARDREQLSKNNITHILSVHDSA-------RPMLEGMTYLCIPAADSPSQNLTQHFKESIKFIHE-- 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171689904 608 fgCflpspkikltnpatergRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARR 672
Cdd:cd14581   76 --C-----------------RLRGEGCLVHCLAGVSRSVTLVVAYIMTVTDFGWEDALSAVKAAR 121
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 535-672 6.91e-08

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: 52.21  E-value: 6.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 535 YLGNLGHANNPDLLKSLGIGQILSVGELamwrDGELEQWGEENTCVVQGVQDNGID----PLTD---EFERCLEFIGKfp 607
Cdd:cd14515    9 YIGDESTAKNKAKLKKLGITHVLNAAEG----KKNGEVNTNAKFYKGSGIIYLGIPasdlPTFDisqYFDEAADFIDK-- 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171689904 608 fgcflpspkikltnpATergRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARR 672
Cdd:cd14515   83 ---------------AL---SDPGGKVLVHCVEGVSRSATLVLAYLMIYQNMTLEEAIRTVRKKR 129
DSP_slingshot_2 cd14569
dual specificity phosphatase domain of slingshot homolog 2; Dual specificity protein ...
 527-691 9.42e-08

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: 51.95  E-value: 9.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 527 PSRILDYMYLGNLGHANNPDLLKSLGIGQILSVG-ELAMWRDGELEQWGEEntcvvqgVQDNGIDPLTDEFERCLEFIgk 605
Cdd:cd14569    4 PTQIFEHVFLGSEWNASNLEDLQNRGVRYILNVTrEIDNFFPGLFEYHNIR-------VYDEEATDLLAYWNDTYKFI-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 606 fpfgcflpspkikltnpatERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRlnVIIQPHLRFGY 685
Cdd:cd14569   75 -------------------SKAKKHGSKCLVHCKMGVSRSASTVIAYAMKEYGWNLDRAYDYVKERR--TVTKPNPSFMR 133


                 ....*.
gi 171689904 686 ELLKWE 691
Cdd:cd14569  134 QLEEYQ 139
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 530-691 2.24e-07

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


Pssm-ID: 350372 [Multi-domain]  Cd Length: 151  Bit Score: 50.79  E-value: 2.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 530 ILDYMYLGNLGHANNPDL--LKSLGIGQILSVgelamwRDGELEQWGEEN-----TCVVQGVQDNGIDPLTDEFERCLEF 602
Cdd:cd14522    8 ILPGLYLGPYSAAMKSKLevLLKHGITHIVCV------RQNIEANFIKPNfpdhfRYLVLDVADNPTENIIRHFPTVKEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 603 IGkfpfGCFLPSPKIkltnpatergrrngtatLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLnvIIQPHLR 682
Cdd:cd14522   82 ID----DCLQTGGKV-----------------LVHGNAGISRSAALVIAYIMETYGLSYRDAFAYVQQRRF--CINPNEG 138


                 ....*....
gi 171689904 683 FGYELLKWE 691
Cdd:cd14522  139 FVHQLKEYE 147
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 528-682 3.72e-07

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: 49.95  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 528 SRILDYMYLGNL---GHANnpDLLKSLGIGQILSVGE-----LAMWRDGELEQWGEENTCVvqGVQDNGIDPLTDEFERC 599
Cdd:cd14524    3 DRIDDTVILGALpfrSMTV--ALVAKENVRGVITMNEeyetrFFCNSKEEWKALGVEQLRL--PTVDFTGVPSLEDLEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 600 LEFIGKFpfgcflpspkikltnpatergRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLNVIIQP 679
Cdd:cd14524   79 VDFILKH---------------------REKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRPHILLRL 137


                 ...
gi 171689904 680 HLR 682
Cdd:cd14524  138 SQR 140
DSP_DUSP15 cd14582
dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual ...
 524-690 3.77e-07

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: 49.95  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 524 GSFPSRILDYMYLGNLGHANNPDLLKSLGIGQILSVGElamwrdgELEQWGEENTCVVQGVQDNGIDPLTDEFERCLEFI 603
Cdd:cd14582    2 GNGMTKVLPGLYLGNFIDAKDLEQLSRNKITHIISIHE-------SPQPLLQDITYLRIPLPDTPEAPIKKHFKECISFI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 604 GKfpfgCflpspkikltnpatergRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLNVIIQPHLRF 683
Cdd:cd14582   75 HQ----C-----------------RLNGGNCLVHCLAGISRSTTIVVAYVMAVTELSWQEVLEAIRAVRPIANPNPGFKQ 133


                 ....*..
gi 171689904 684 GYELLKW 690
Cdd:cd14582  134 QLEEFGW 140
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
 534-693 2.72e-06

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: 47.44  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 534 MYLGNLGHANNPDLLKSLGIGQILSVGELAMWRDGELEQWGeeNTCVVQGVQDNGIDP--LTDEFERCLEFIGKfpfgcf 611
Cdd:cd14580    8 LFLGDLATAHNRFGLWKLGITHVLNAAHGKLFCQGGDDFYG--TSVDYYGVPANDLPDfdISPYFYSAAEFIHR------ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 612 lpspkiKLTNPatergrrnGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLnviIQPHLRFGYELLKWE 691
Cdd:cd14580   80 ------ALNTP--------GAKVLVHCAVGVSRSATLVLAYLMIYHQLSLVQAIKTVKERRW---IFPNRGFLKQLRKLD 142


                 ..
gi 171689904 692 EQ 693
Cdd:cd14580  143 QQ 144
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
584-693 8.96e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 45.73  E-value: 8.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 584 VQDNGIDP---LTDEFERCLEFIGKFPFGCF--------LPSPK-IKLTNPATERGRRNGTATLVHCRVGVSRSATICIA 651
Cdd:COG2453   21 LKREGIDAvvsLTEEEELLLGLLEEAGLEYLhlpipdfgAPDDEqLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAA 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 171689904 652 eVMRSLRMSFPRAYCFVRARRLNVIIQP-HLRFgyeLLKWEEQ 693
Cdd:COG2453  101 -YLVLLGLSAEEALARVRAARPGAVETPaQRAF---LERFAKR 139
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 629-678 1.22e-05

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 45.03  E-value: 1.22e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 171689904 629 RNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARRLNVIIQ 678
Cdd:cd14494   54 KPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPGGIPQ 103
DUSP26 cd14578
dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), ...
 534-672 3.75e-05

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


Pssm-ID: 350426 [Multi-domain]  Cd Length: 144  Bit Score: 44.06  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 534 MYLGNLGHANNPDLLKSLGIGQILSVGElAMWRDGELEQWGEENTCVVQGVQDNGIDPLTDEFERCLEFIGKfpfgcflp 613
Cdd:cd14578    8 LYLGDQDIAANRRELRRLGITHILNASH-SKWRGGAEYYEGLNIRYLGIEAHDSPAFDMSIHFYPAADFIHR-------- 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 171689904 614 spkikltnpateRGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARR 672
Cdd:cd14578   79 ------------ALSQPGGKILVHCAVGVSRSATLVLAYLMIHHHMTLVEAIKTVKDHR 125
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 525-672 1.10e-04

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


Pssm-ID: 350427 [Multi-domain]  Cd Length: 168  Bit Score: 43.22  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171689904 525 SFPSR----ILDYMYLGNLGHANNPDLLKSLGIGQILSV--GELAMWRDGELEQWgEENTCVVQGVQDNGIDP--LTDEF 596
Cdd:cd14579   15 SLPSQhcneVYPRIYVGNASVAQNIMRLQRLGITHVLNAaeGKSFMHVNTNAEFY-EDTGITYHGIKANDTQHfnLSAYF 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171689904 597 ERCLEFIGKfpfgcflpspkikltNPATERGRrngtaTLVHCRVGVSRSATICIAEVMRSLRMSFPRAYCFVRARR 672
Cdd:cd14579   94 EEAADFIDK---------------ALAQKNGR-----VLVHCREGYSRSPTLVIAYLMLRQKMDVKSALSTVRQKR 149
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
628-676 1.08e-03

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 39.26  E-value: 1.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 171689904   628 RRNGTATLVHCRVGVSRSATICIAEVM------RSLRMSFPRAYCFVRARRLNVI 676
Cdd:smart00404  36 SESSGPVVVHCSAGVGRTGTFVAIDILlqqleaEAGEVDIFDTVKELRSQRPGMV 90
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 628-676 1.08e-03

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: 39.26  E-value: 1.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 171689904   628 RRNGTATLVHCRVGVSRSATICIAEVM------RSLRMSFPRAYCFVRARRLNVI 676
Cdd:smart00012  36 SESSGPVVVHCSAGVGRTGTFVAIDILlqqleaEAGEVDIFDTVKELRSQRPGMV 90
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 625-682 7.35e-03

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: 37.25  E-value: 7.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 171689904 625 ERGRRNGTATLVHCRVGVSRSATICIAEVMRSLRMSFPR-AYCFVRARRLNVIIQPHLR 682
Cdd:cd14527   70 EELRAQGGPVLVHCALGYGRSATVVAAWLLAYGRAKSVAeAEALIRAARPQVVLNPAQR 128
 
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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