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Conserved domains on  [gi|665404815|ref|NP_001285722|]
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cell division cycle 14, isoform E [Drosophila melanogaster]

Protein Classification

CDC14 family protein phosphatase( domain architecture ID 13026096)

cell division control 14 (CDC14) family protein phosphatase similar to human dual-specificity protein phosphatases CDC14A/B/C that may play a key role in cell cycle control in human cells

CATH:  3.90.190.10
EC:  3.1.3.-
Gene Ontology:  GO:0006470|GO:0004721|GO:0004725|GO:0004722
PubMed:  17057753|27514797|19228121|20720150
SCOP:  3000304

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 167-341 1.30e-125

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


:

Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 369.86  E-value: 1.30e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 167 DFDAEEYEYFERVENGDFNWIVPQKFIAFCGPHQKSKTLpNGYPCHAPERYFSYFRDNNVTTVIRLNAKVYHASSFENAG 246
Cdd:cd14499    1 TFDLEEYEHYERVENGDLNWIVPGKFLAFSGPHDTRKDE-NGYPTHTPEDYIPYFKKLGVTTVVRLNKKLYDAKRFTDAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 247 FDHKDLFFIDGSTPSDAIMKKFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRPGSVIGHQQ 326
Cdd:cd14499   80 IRHYDLYFPDGSTPSDDIVKKFLDICENEKGAIAVHCKAGLGRTGTLIACYLMKHYGFTAREAIAWLRICRPGSVIGPQQ 159

                        170
                 ....*....|....*
gi 665404815 327 QWMEDKQSWLWSEGE 341
Cdd:cd14499  160 QFLEEKEARLWRAGD 174
CDC14_N cd17657
N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control ...
 12-158 8.52e-74

N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif. The N-terminal pseudophosphatase domain lacks the catalytic residues.


:

Pssm-ID: 350495  Cd Length: 144  Bit Score: 234.32  E-value: 8.52e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815  12 CASEMQEDRLYFVAFKknIKPKNTVNTHYFSVDEEFIYENFYNDFGPLNICMLYRYCMKLNTKLNAKCHANKKIVHYTSM 91
Cdd:cd17657    1 SAIEIIPDRLYFASLR--GPPKSTDNTHYFSIDDELVYEPFFADFGPLNLAQIYRFCCKLNKKLKSPSLASKKIVHYTSL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404815  92 NPAKRLNAAYLIGSYAIIYLNKTPQEAYRPLVAGEiPAYTRFCDASYGPSNFKISLLDCLNAVHKGL 158
Cdd:cd17657   79 DPKKRANAAFLIGAYAVIYLGKTPEEAYRPLESGE-PPFLPFRDASYGPCTYELTVLDCLKGLEKAL 144
 
Name Accession Description Interval E-value
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 167-341 1.30e-125

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 369.86  E-value: 1.30e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 167 DFDAEEYEYFERVENGDFNWIVPQKFIAFCGPHQKSKTLpNGYPCHAPERYFSYFRDNNVTTVIRLNAKVYHASSFENAG 246
Cdd:cd14499    1 TFDLEEYEHYERVENGDLNWIVPGKFLAFSGPHDTRKDE-NGYPTHTPEDYIPYFKKLGVTTVVRLNKKLYDAKRFTDAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 247 FDHKDLFFIDGSTPSDAIMKKFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRPGSVIGHQQ 326
Cdd:cd14499   80 IRHYDLYFPDGSTPSDDIVKKFLDICENEKGAIAVHCKAGLGRTGTLIACYLMKHYGFTAREAIAWLRICRPGSVIGPQQ 159

                        170
                 ....*....|....*
gi 665404815 327 QWMEDKQSWLWSEGE 341
Cdd:cd14499  160 QFLEEKEARLWRAGD 174
CDC14_N cd17657
N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control ...
 12-158 8.52e-74

N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif. The N-terminal pseudophosphatase domain lacks the catalytic residues.


Pssm-ID: 350495  Cd Length: 144  Bit Score: 234.32  E-value: 8.52e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815  12 CASEMQEDRLYFVAFKknIKPKNTVNTHYFSVDEEFIYENFYNDFGPLNICMLYRYCMKLNTKLNAKCHANKKIVHYTSM 91
Cdd:cd17657    1 SAIEIIPDRLYFASLR--GPPKSTDNTHYFSIDDELVYEPFFADFGPLNLAQIYRFCCKLNKKLKSPSLASKKIVHYTSL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404815  92 NPAKRLNAAYLIGSYAIIYLNKTPQEAYRPLVAGEiPAYTRFCDASYGPSNFKISLLDCLNAVHKGL 158
Cdd:cd17657   79 DPKKRANAAFLIGAYAVIYLGKTPEEAYRPLESGE-PPFLPFRDASYGPCTYELTVLDCLKGLEKAL 144
DSPn pfam14671
Dual specificity protein phosphatase, N-terminal half; The active core of the dual specificity ...
 18-157 5.18e-66

Dual specificity protein phosphatase, N-terminal half; The active core of the dual specificity protein phosphatase is made up of two globular domains both with the DSP-like fold. This family represents the N-terminal half of the core. These domains are arranged in tandem, and are associated via an extensive interface to form a single globular whole. The conserved PTP signature motif (Cys-[X]5-Arg) that defines the catalytic centre of all PTP-family members is located within the C-terminal domain, family DSPc, pfam00782. Although the centre of the catalytic site is formed from DSPc, two loops from the N-terminal domain, DSPn, also contribute to the catalytic site, facilitating peptide substrate specificity.


Pssm-ID: 464252  Cd Length: 140  Bit Score: 213.94  E-value: 5.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815   18 EDRLYFVAFKKniKPKNTVNTHYFSVDEEFIYENFYNDFGPLNICMLYRYCMKLNTKLNAKCHANKKIVHYTSMNPAKRL 97
Cdd:pfam14671   4 PDRLYFATLKS--KPKNTPNYHYFSIDDELVYEPFYFDFGPLNLAHLYRFCIKLNKKLKSPELKKKKIVHYTSQDKQKRA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815   98 NAAYLIGSYAIIYLNKTPQEAYRPLVAGeIPAYTRFCDASYGPSNFKISLLDCLNAVHKG 157
Cdd:pfam14671  82 NAAFLIGAYMVLYLNMSPEEALSPLSSI-SPPFIPFRDASYGPCTYTLTLLDCLKGLEKA 140
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 217-331 2.80e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 79.68  E-value: 2.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 217 YFSYFRDNNVTTVIRLNAKVYHASSFENAGFDHKDLFFIDGSTPSDAIMKKFLSICETTK-------GAIAVHCKAGLGR 289
Cdd:PTZ00242  32 YIKELQRYNVTHLVRVCGPTYDAELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQEFakqstppETIAVHCVAGLGR 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 665404815 290 TGSLIGAYIMKHYGFTALEAIAWLRLCRPGSVIGHQQQWMED 331
Cdd:PTZ00242 112 APILVALALVEYGGMEPLDAVGFVREKRKGAINQTQLQFLKK 153
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
212-329 7.71e-16

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 74.62  E-value: 7.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 212 HAPERYFSYFRDNNVTTVIRLNAKV-YHASSFENAGFDHKDLFFIDGSTPSDAIMKKFLS-ICETTK--GAIAVHCKAGL 287
Cdd:COG2453   12 PLPGGGEADLKREGIDAVVSLTEEEeLLLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDfIDEALRegKKVLVHCRGGI 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 665404815 288 GRTGSLIGAYIMKHyGFTALEAIAWLRLCRPGSVIGHQQQWM 329
Cdd:COG2453   92 GRTGTVAAAYLVLL-GLSAEEALARVRAARPGAVETPAQRAF 132
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 266-330 1.73e-12

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: 64.59  E-value: 1.73e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404815  266 KKFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRPGSV--IGHQQQWME 330
Cdd:pfam00782  59 VEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISpnFGFKRQLLE 125
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
266-330 2.52e-12

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 64.61  E-value: 2.52e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404815   266 KKFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRPGSV--IGHQQQWME 330
Cdd:smart00195  68 VEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISpnFGFLRQLIE 134
 
Name Accession Description Interval E-value
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 167-341 1.30e-125

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 369.86  E-value: 1.30e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 167 DFDAEEYEYFERVENGDFNWIVPQKFIAFCGPHQKSKTLpNGYPCHAPERYFSYFRDNNVTTVIRLNAKVYHASSFENAG 246
Cdd:cd14499    1 TFDLEEYEHYERVENGDLNWIVPGKFLAFSGPHDTRKDE-NGYPTHTPEDYIPYFKKLGVTTVVRLNKKLYDAKRFTDAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 247 FDHKDLFFIDGSTPSDAIMKKFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRPGSVIGHQQ 326
Cdd:cd14499   80 IRHYDLYFPDGSTPSDDIVKKFLDICENEKGAIAVHCKAGLGRTGTLIACYLMKHYGFTAREAIAWLRICRPGSVIGPQQ 159

                        170
                 ....*....|....*
gi 665404815 327 QWMEDKQSWLWSEGE 341
Cdd:cd14499  160 QFLEEKEARLWRAGD 174
CDC14_N cd17657
N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control ...
 12-158 8.52e-74

N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif. The N-terminal pseudophosphatase domain lacks the catalytic residues.


Pssm-ID: 350495  Cd Length: 144  Bit Score: 234.32  E-value: 8.52e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815  12 CASEMQEDRLYFVAFKknIKPKNTVNTHYFSVDEEFIYENFYNDFGPLNICMLYRYCMKLNTKLNAKCHANKKIVHYTSM 91
Cdd:cd17657    1 SAIEIIPDRLYFASLR--GPPKSTDNTHYFSIDDELVYEPFFADFGPLNLAQIYRFCCKLNKKLKSPSLASKKIVHYTSL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404815  92 NPAKRLNAAYLIGSYAIIYLNKTPQEAYRPLVAGEiPAYTRFCDASYGPSNFKISLLDCLNAVHKGL 158
Cdd:cd17657   79 DPKKRANAAFLIGAYAVIYLGKTPEEAYRPLESGE-PPFLPFRDASYGPCTYELTVLDCLKGLEKAL 144
DSPn pfam14671
Dual specificity protein phosphatase, N-terminal half; The active core of the dual specificity ...
 18-157 5.18e-66

Dual specificity protein phosphatase, N-terminal half; The active core of the dual specificity protein phosphatase is made up of two globular domains both with the DSP-like fold. This family represents the N-terminal half of the core. These domains are arranged in tandem, and are associated via an extensive interface to form a single globular whole. The conserved PTP signature motif (Cys-[X]5-Arg) that defines the catalytic centre of all PTP-family members is located within the C-terminal domain, family DSPc, pfam00782. Although the centre of the catalytic site is formed from DSPc, two loops from the N-terminal domain, DSPn, also contribute to the catalytic site, facilitating peptide substrate specificity.


Pssm-ID: 464252  Cd Length: 140  Bit Score: 213.94  E-value: 5.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815   18 EDRLYFVAFKKniKPKNTVNTHYFSVDEEFIYENFYNDFGPLNICMLYRYCMKLNTKLNAKCHANKKIVHYTSMNPAKRL 97
Cdd:pfam14671   4 PDRLYFATLKS--KPKNTPNYHYFSIDDELVYEPFYFDFGPLNLAHLYRFCIKLNKKLKSPELKKKKIVHYTSQDKQKRA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815   98 NAAYLIGSYAIIYLNKTPQEAYRPLVAGeIPAYTRFCDASYGPSNFKISLLDCLNAVHKG 157
Cdd:pfam14671  82 NAAFLIGAYMVLYLNMSPEEALSPLSSI-SPPFIPFRDASYGPCTYTLTLLDCLKGLEKA 140
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 184-326 2.08e-21

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 90.80  E-value: 2.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 184 FNWIVPQKFIAFCGPHQksktlpngypchaPERYfSYFRDNNVTTVIRLNAKVYHASSFENAGFDHKDLFFIDGSTPSDA 263
Cdd:cd14504    1 FSWVIPGKLAGMAFPRL-------------PEHY-AYLNENGIRHVVTLTEEPPPEHSDTCPGLRYHHIPIEDYTPPTLE 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665404815 264 IMKKFLSI---CETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRPGSVIGHQQ 326
Cdd:cd14504   67 QIDEFLDIveeANAKNEAVLVHCLAGKGRTGTMLACYLVKTGKISAVDAINEIRRIRPGSIETSEQ 132
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 184-322 7.82e-20

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: 85.48  E-value: 7.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 184 FNWIVPQKFIAFCGPHQKSKTLpngypchaperyFSYFRDNNVTTVIRLNakvyhassfenagfdhkdlffidgstpsDA 263
Cdd:cd14494    1 FNWIDPLRLIAGALPLSPLEAD------------SRFLKQLGVTTIVDLT----------------------------LA 40

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665404815 264 IMKKFLSICETT---KGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRPGSVI 322
Cdd:cd14494   41 MVDRFLEVLDQAekpGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPGGIP 102
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 211-330 2.79e-18

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


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 82.27  E-value: 2.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 211 CHAP-----ERYFSYFRDNNVTTVIRLNAKVYHASSFENAGFDHKDLFFIDGSTPSDAIMKKFLSICETT-------KGA 278
Cdd:cd14500   18 TDAPtdsnlPLYIKELKKYNVTDLVRVCEPTYDKEPLEKAGIKVHDWPFDDGSPPPDDVVDDWLDLLKTRfkeegkpGAC 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 665404815 279 IAVHCKAGLGRTGSLIGAYIMKhYGFTALEAIAWLRLCRPGSVIGHQQQWME 330
Cdd:cd14500   98 IAVHCVAGLGRAPVLVAIALIE-LGMKPEDAVEFIRKKRRGAINSKQLQFLE 148
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 217-331 2.80e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 79.68  E-value: 2.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 217 YFSYFRDNNVTTVIRLNAKVYHASSFENAGFDHKDLFFIDGSTPSDAIMKKFLSICETTK-------GAIAVHCKAGLGR 289
Cdd:PTZ00242  32 YIKELQRYNVTHLVRVCGPTYDAELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQEFakqstppETIAVHCVAGLGR 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 665404815 290 TGSLIGAYIMKHYGFTALEAIAWLRLCRPGSVIGHQQQWMED 331
Cdd:PTZ00242 112 APILVALALVEYGGMEPLDAVGFVREKRKGAINQTQLQFLKK 153
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
212-329 7.71e-16

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 74.62  E-value: 7.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 212 HAPERYFSYFRDNNVTTVIRLNAKV-YHASSFENAGFDHKDLFFIDGSTPSDAIMKKFLS-ICETTK--GAIAVHCKAGL 287
Cdd:COG2453   12 PLPGGGEADLKREGIDAVVSLTEEEeLLLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDfIDEALRegKKVLVHCRGGI 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 665404815 288 GRTGSLIGAYIMKHyGFTALEAIAWLRLCRPGSVIGHQQQWM 329
Cdd:COG2453   92 GRTGTVAAAYLVLL-GLSAEEALARVRAARPGAVETPAQRAF 132
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 266-330 1.73e-12

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: 64.59  E-value: 1.73e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404815  266 KKFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRPGSV--IGHQQQWME 330
Cdd:pfam00782  59 VEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISpnFGFKRQLLE 125
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
266-330 2.52e-12

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 64.61  E-value: 2.52e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404815   266 KKFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRPGSV--IGHQQQWME 330
Cdd:smart00195  68 VEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISpnFGFLRQLIE 134
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 221-321 2.63e-12

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 66.22  E-value: 2.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 221 FRDNNVTTVIRLNAKVYHAS----------------SFENAGFDHKDLFFIDGSTPSDAI---MKKFLSICETTKGAIAV 281
Cdd:cd14506   35 FKEKGIKTVINLQEPGEHAScgpglepesgfsylpeAFMRAGIYFYNFGWKDYGVPSLTTildIVKVMAFALQEGGKVAV 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 665404815 282 HCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRPGSV 321
Cdd:cd14506  115 HCHAGLGRTGVLIACYLVYALRMSADQAIRLVRSKRPNSI 154
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 217-330 2.90e-12

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 66.88  E-value: 2.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 217 YFSYFRDNNVTTVIRLNAKVYHASSFENAGFDHKDLFFIDGSTPSDAIMKKFLSICETT---KGAIAVHCKAGLGRTGSL 293
Cdd:PTZ00393 108 YIKEMKNYNVTDLVRTCERTYNDGEITSAGINVHELIFPDGDAPTVDIVSNWLTIVNNViknNRAVAVHCVAGLGRAPVL 187

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 665404815 294 IgAYIMKHYGFTALEAIAWLRLCRPGSVIGHQQQWME 330
Cdd:PTZ00393 188 A-SIVLIEFGMDPIDAIVFIRDRRKGAINKRQLQFLK 223
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 223-328 6.20e-11

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 61.12  E-value: 6.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 223 DNNVTTVIRLN-----------AKVYHASSFENAGFDHKDLFFidgsTPSDAIMKK---FLSICETTKGAIAVHCKAGLG 288
Cdd:cd14524   26 KENVRGVITMNeeyetrffcnsKEEWKALGVEQLRLPTVDFTG----VPSLEDLEKgvdFILKHREKGKSVYVHCKAGRG 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 665404815 289 RTGSLIGAYIMKHYGFTALEAIAWLRLCRPgSVIGHQQQW 328
Cdd:cd14524  102 RSATIVACYLIQHKGWSPEEAQEFLRSKRP-HILLRLSQR 140
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 222-318 7.73e-11

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: 60.25  E-value: 7.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 222 RDNNVTTVIRLNAKVYhaSSFENAGFDHKDLFFIDgsTPSDAIMKKFLSICE------TTKGAIAVHCKAGLGRTGSLIG 295
Cdd:cd14498   23 KKLGITHILNVAGEPP--PNKFPDGIKYLRIPIED--SPDEDILSHFEEAIEfieealKKGGKVLVHCQAGVSRSATIVI 98

                         90       100
                 ....*....|....*....|...
gi 665404815 296 AYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd14498   99 AYLMKKYGWSLEEALELVKSRRP 121
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 187-318 2.60e-10

RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes baculovirus RNA 5'-triphosphatase, dual specificity protein phosphatase 11 (DUSP11), and the RNA triphosphatase domains of metazoan and plant mRNA capping enzymes. RNA/polynucleotide 5'-triphosphatase (EC 3.1.3.33) catalyzes the removal of the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end. mRNA capping enzyme is a bifunctional enzyme that catalyzes the first two steps of cap formation. DUSP11 has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity.


Pssm-ID: 350352 [Multi-domain]  Cd Length: 167  Bit Score: 59.59  E-value: 2.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 187 IVPQKFIAFCGPHQKSKT-LPNGYPCHAPERYFSYFR-DNNVTTVIRLNA--KVYHASSFENAGFDHKDLFFIDGSTPSD 262
Cdd:cd14502   12 VGPTRFIPMKTPLSDDYEhLFAPEIRFTPSALAEKFRqDRKVGLVIDLTNtdRYYDPNDLDDDGYVYYKKVCVRKEPPDA 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665404815 263 AIMKKFLSIC------ETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd14502   92 EEVNKFIELVdkflaeDNPDKLIAVHCTHGFNRTGFMIVSYLVERLGLTVEQALEAFAQARP 153
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 226-330 6.58e-09

protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), also known as protein-tyrosine phosphatase of regenerating liver 3 (PRL-3), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It exerts its oncogenic functions through activation of PI3K/Akt, which is a key regulator of the rapamycin-sensitive mTOR complex 1. PRL-3 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350511 [Multi-domain]  Cd Length: 154  Bit Score: 55.42  E-value: 6.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 226 VTTVIRLNAKVYHASSFENAGFDHKDLFFIDGSTPSDAIMKKFLSI-----CETTKGAIAVHCKAGLGRTGSLIGAYIMK 300
Cdd:cd18535   38 ATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLlktkfCEDPGCCVAVHCVAGLGRAPVLVALALIE 117

                         90       100       110
                 ....*....|....*....|....*....|
gi 665404815 301 HyGFTALEAIAWLRLCRPGSVIGHQQQWME 330
Cdd:cd18535  118 S-GMKYEDAIQFIRQKRRGAINSKQLTYLE 146
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 220-321 4.03e-08

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 53.04  E-value: 4.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 220 YFRDNNVTTVI---------RLNAKVYHaSSFENAGFDHKDLFFIDGSTPSDaiMKKFLSICETTKGA------IAVHCK 284
Cdd:cd14505   38 ELKDQGVDDVVtlctdgeleELGVPDLL-EQYQQAGITWHHLPIPDGGVPSD--IAQWQELLEELLSAlengkkVLIHCK 114

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 665404815 285 AGLGRTGsLIGA--YIMKHYGFTALEAIAWLRLCRPGSV 321
Cdd:cd14505  115 GGLGRTG-LIAAclLLELGDTLDPEQAIAAVRALRPGAI 152
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 216-330 6.69e-08

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 52.77  E-value: 6.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 216 RYFSYFRDNNVTTVIRLNAKVYHASSFENAGFDHKDLFFIDGSTPSDAIMKKFLSIC-----ETTKGAIAVHCKAGLGRT 290
Cdd:cd18537   32 KFIEELKKYGVTTVVRVCEATYDTTLVEKEGIQVLDWPFDDGAPPSNQIVDDWLNLLkvkfrEEPGCCIAVHCVAGLGRA 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 665404815 291 GSLIGAYIMKHyGFTALEAIAWLRLCRPGSVIGHQQQWME 330
Cdd:cd18537  112 PVLVALALIEC-GMKYEDAVQFIRQKRRGAFNSKQLLYLE 150
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
265-321 7.11e-08

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 50.82  E-value: 7.11e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665404815   265 MKKFLSICETtKGAIAVHCKAGLGRTGSLIGAYIM-----KHYGFTALEAIAW-LRLCRPGSV 321
Cdd:smart00404  29 VKKNLNQSES-SGPVVVHCSAGVGRTGTFVAIDILlqqleAEAGEVDIFDTVKeLRSQRPGMV 90
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 265-321 7.11e-08

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: 50.82  E-value: 7.11e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665404815   265 MKKFLSICETtKGAIAVHCKAGLGRTGSLIGAYIM-----KHYGFTALEAIAW-LRLCRPGSV 321
Cdd:smart00012  29 VKKNLNQSES-SGPVVVHCSAGVGRTGTFVAIDILlqqleAEAGEVDIFDTVKeLRSQRPGMV 90
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 185-324 8.52e-08

dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus.


Pssm-ID: 350503  Cd Length: 169  Bit Score: 52.28  E-value: 8.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 185 NWIVP-QKFIAFCGPHQKSKTLPNgypchAPERYFSYF--------RDNNVTTVIRLN--AKVYHASSFENAGFDHKDLF 253
Cdd:cd17665    9 GQRIPgTRFIAFKVPLRKSFFANL-----PPEQRFTPKdlveqvekRGEKLGLVIDLTntTRYYDPRDLTNHGVYYKKIT 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665404815 254 FIDGSTPSDA-------IMKKFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRpgsviGH 324
Cdd:cd17665   84 CPGHQVPDDKtiqsfkdAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQAR-----GH 156
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 262-318 1.02e-07

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: 52.10  E-value: 1.02e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 665404815 262 DAIMKKFLSIcETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd14573   66 DPIADKIHTV-EARGGRTLLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTWVKSCRP 121
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 256-321 1.67e-07

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 52.29  E-value: 1.67e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665404815 256 DGSTPSD-----AIMKKFLSICETTKGAIAVHCKAGLGRTGSLIGAYIM----KHYG-FTALEAIAWLRLCRPGSV 321
Cdd:cd00047  114 DHGVPSSpedllALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAIDILlerlEAEGeVDVFEIVKALRKQRPGMV 189
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
256-321 1.90e-07

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 53.05  E-value: 1.90e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665404815   256 DGSTPSD-----AIMKKFLSICETTKGAIAVHCKAGLGRTGSLIGAYIM-----KHYGFTALEAIAWLRLCRPGSV 321
Cdd:smart00194 169 DHGVPESpesilDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILlqqleAGKEVDIFEIVKELRSQRPGMV 244
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
 273-318 3.68e-07

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: 50.01  E-value: 3.68e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 665404815 273 ETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd14518   87 KKHGGAVLVHCAMGKSRSVTVVIAYLMYKYNLSVSQALHAVRRKRP 132
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 277-318 5.05e-07

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


Pssm-ID: 350364 [Multi-domain]  Cd Length: 133  Bit Score: 49.09  E-value: 5.05e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 665404815 277 GAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd14514   78 GRTLVHCVAGVSRSATLCLAYLMKYEGMTLREAYKHVKAARP 119
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 226-330 6.09e-07

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


Pssm-ID: 350512 [Multi-domain]  Cd Length: 155  Bit Score: 49.61  E-value: 6.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 226 VTTVIRLNAKVYHASSFENAGFDHKDLFFIDGSTPSDAIMKKFLSICETT-----KGAIAVHCKAGLGRTGSLIgAYIMK 300
Cdd:cd18536   39 VTTLVRVCDATYDKAPVEKEGIQVLDWPFDDGAPPPNQIVDDWLNLLKTKfreepGCCVAVHCVAGLGRAPVLV-ALALI 117

                         90       100       110
                 ....*....|....*....|....*....|
gi 665404815 301 HYGFTALEAIAWLRLCRPGSVIGHQQQWME 330
Cdd:cd18536  118 ECGMKYEDAVQFIRQKRRGAFNSKQLLYLE 147
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
256-327 8.40e-07

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 51.25  E-value: 8.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 256 DGSTPSDAIMKKFLS-------ICETTKGAIAVHCKAGLGRTGSLIGAYIM-------KHYGFTALEAIAWLRLCRPGSV 321
Cdd:COG5599  179 DHGAISAEALKNLADlidkkekIKDPDKLLPVVHCRAGVGRTGTLIACLALsksinalVQITLSVEEIVIDMRTSRNGGM 258


                 ....*.
gi 665404815 322 IGHQQQ 327
Cdd:COG5599  259 VQTSEQ 264
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
 277-318 4.20e-06

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: 47.17  E-value: 4.20e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 665404815 277 GAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd14572   86 GATLVHCAAGVSRSATLCIAYLMKYHRVSLLEAYNWVKARRP 127
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 274-317 7.34e-06

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: 46.44  E-value: 7.34e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 665404815 274 TTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCR 317
Cdd:cd14515   86 DPGGKVLVHCVEGVSRSATLVLAYLMIYQNMTLEEAIRTVRKKR 129
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 265-310 2.07e-05

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 45.26  E-value: 2.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 665404815 265 MKKFLSicETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGF-TALEAI 310
Cdd:cd14497   86 IDSWLS--EDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYsTADEAL 130
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 266-316 2.45e-05

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


Pssm-ID: 350372 [Multi-domain]  Cd Length: 151  Bit Score: 45.01  E-value: 2.45e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665404815 266 KKFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWL---RLC 316
Cdd:cd14522   79 KEFIDDCLQTGGKVLVHGNAGISRSAALVIAYIMETYGLSYRDAFAYVqqrRFC 132
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
 276-318 3.04e-05

dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar proteins; Dual specificity protein phosphatase 12 (DUSP12), also called YVH1, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP12 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It targets p38 MAPK to regulate macrophage response to bacterial infection. It also ameliorates cardiac hypertrophy in response to pressure overload through c-Jun N-terminal kinase (JNK) inhibition. DUSP12 has been identified as a modulator of cell cycle progression, a function independent of phosphatase activity and mediated by its C-terminal zinc-binding domain.


Pssm-ID: 350370 [Multi-domain]  Cd Length: 144  Bit Score: 44.55  E-value: 3.04e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 665404815 276 KGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd14520   79 EGAVLVHCHAGVSRSAAVVTAYLMKTEQLSFEEALASLRECKP 121
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 208-312 4.65e-05

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 44.12  E-value: 4.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 208 GYPChapERYFSYFRdNNVTTVIRL-------NAKVYH--------ASSFEN--AGFDhkdlfFIDGSTPSDAIMKKFls 270
Cdd:cd14509   13 GFPA---EGVEGVYR-NPIDDVQRFletkhkgHYKVYNlcsersydPSKFNGrvAEYP-----FDDHNPPPLELIKPF-- 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 665404815 271 iCETT--------KGAIAVHCKAGLGRTGSLIGAYIMkHYGF--TALEAIAW 312
Cdd:cd14509   82 -CEDVdewlkedeKNVAAVHCKAGKGRTGVMICCYLL-YLGKfpSAKEALDF 131
DUSP22 cd14581
dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), ...
 267-330 4.80e-05

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


Pssm-ID: 350429 [Multi-domain]  Cd Length: 149  Bit Score: 44.02  E-value: 4.80e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665404815 267 KFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP--GSVIGHQQQWME 330
Cdd:cd14581   71 KFIHECRLRGEGCLVHCLAGVSRSVTLVVAYIMTVTDFGWEDALSAVKAARScaNPNMGFQRQLQE 136
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 267-318 6.91e-05

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


Pssm-ID: 350510 [Multi-domain]  Cd Length: 130  Bit Score: 42.91  E-value: 6.91e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 665404815 267 KFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd18534   64 DFIEQCRKDKARVLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRP 115
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 267-318 1.28e-04

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


Pssm-ID: 350363 [Multi-domain]  Cd Length: 139  Bit Score: 42.38  E-value: 1.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 665404815 267 KFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd14513   69 RFIKEARRKGSKVLVHCKMGVSRSASTVIAYAMKEYGWSLEQALEHVKERRS 120
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
 267-318 1.51e-04

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


Pssm-ID: 350419 [Multi-domain]  Cd Length: 144  Bit Score: 42.54  E-value: 1.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 665404815 267 KFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd14571   72 RFIEAARAQGTRVLVHCKMGVSRSASTVIAYAMKQYGWTLEQALRHVRERRP 123
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 256-321 2.52e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 42.75  E-value: 2.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665404815 256 DGSTPSDAI-MKKFLSICET--TKGAIAVHCKAGLGRTGSLIG-----AYIMKHYGFTALEAIAWLRLCRPGSV 321
Cdd:cd14538  117 DHGTPQSADpLLRFIRYMRRihNSGPIVVHCSAGIGRTGVLITidvalGLIERDLPFDIQDIVKDLREQRQGMI 190
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
256-321 3.14e-04

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 43.00  E-value: 3.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665404815  256 DGSTPSDAimKKFLSICETTK--------GAIAVHCKAGLGRTGSLIGAYIM-----KHYGFTALEAIAWLRLCRPGSV 321
Cdd:pfam00102 143 DHGVPESP--NSLLDLLRKVRkssldgrsGPIVVHCSAGIGRTGTFIAIDIAlqqleAEGEVDIFQIVKELRSQRPGMV 219
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 222-320 3.68e-04

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: 41.19  E-value: 3.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 222 RDNNVTTVIRLnakvyhASSFENA---GFDHKDLFFIDgsTPSDAIMK------KFLSICETTKGAIAVHCKAGLGRTGS 292
Cdd:cd14523   24 KKHKVTHILNV------AYGVENAfpdDFTYKTISILD--LPETDITSyfpecfEFIDEAKSQDGVVLVHCNAGVSRSAS 95

                         90       100
                 ....*....|....*....|....*...
gi 665404815 293 LIGAYIMKHYGFTALEAIAWLRLCRPGS 320
Cdd:cd14523   96 IVIGYLMATENLSFEDAFSLVKNARPSI 123
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 281-318 4.48e-04

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


Pssm-ID: 350415 [Multi-domain]  Cd Length: 152  Bit Score: 41.27  E-value: 4.48e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 665404815 281 VHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd14567   85 VHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKRP 122
DUSP26 cd14578
dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), ...
 275-310 6.38e-04

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: 40.59  E-value: 6.38e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 665404815 275 TKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAI 310
Cdd:cd14578   83 PGGKILVHCAVGVSRSATLVLAYLMIHHHMTLVEAI 118
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 276-299 1.60e-03

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 40.04  E-value: 1.60e-03
                         10        20
                 ....*....|....*....|....
gi 665404815 276 KGAIAVHCKAGLGRTGSLIGAYIM 299
Cdd:cd14510  108 KNVVAIHCKGGKGRTGTMVCAWLI 131
DSP_fungal_PPS1 cd14516
dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; ...
 255-317 2.09e-03

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: 39.56  E-value: 2.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665404815 255 IDGSTPSDAIMKKFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCR 317
Cdd:cd14516   95 IDSLLPQLTDALDFIQKARLLGGKTLVHCRVGVSRSATVVIAEVMKHLRMSLVDAYLFVRVRR 157
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 268-318 2.22e-03

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: 38.94  E-value: 2.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 665404815 268 FLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd14568   71 FIEKARASNKRVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRP 121
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 257-318 2.64e-03

N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as RNA guanylyltransferase and 5'-phosphatase (RNGTT) or mammalian mRNA capping enzyme (Mce1) in mammals, is a bifunctional enzyme that catalyzes the first two steps of cap formation: (1) by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end using the polynucleotide 5'-phosphatase activity (EC 3.1.3.33) of the N-terminal triphosphatase domain; and (2) by transferring the GMP moiety of GTP to the 5'-diphosphate terminus through the C-terminal mRNA guanylyltransferase domain (EC 2.7.7.50). The enzyme is also referred to as CEL-1 in Caenorhabditis elegans.


Pssm-ID: 350502  Cd Length: 167  Bit Score: 39.20  E-value: 2.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404815 257 GSTPSDAIMKKFLSICET-----TKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd17664   87 GECPSPEQTETFIRLCENfieknPLELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARP 153
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 256-326 3.08e-03

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 39.90  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404815 256 DGSTPSDA--IMKKFLSICE-----TTKGAIAVHCKAGLGRTGSLIGAYI----MKHYGFT-ALEAIAWLRLCRPGSVIG 323
Cdd:cd14611  138 DHKTPDSAqpLLQLMLDVEEdrlasPGRGPVVVHCSAGIGRTGCFIATTIgcqqLKEEGVVdVLSIVCQLRVDRGGMVQT 217


                 ...
gi 665404815 324 HQQ 326
Cdd:cd14611  218 SEQ 220
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
 274-310 3.70e-03

dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 isoform A (DUSP13A), also called branching-enzyme interacting DSP or muscle-restricted DSP (MDSP), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP13A is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP13A also functions as a regulator of apoptosis signal-regulating kinase 1 (ASK1), a MAPK kinase kinase, by interacting with its N-terminal domain and inducing ASK1-mediated apoptosis through the activation of caspase-3. This function is independent of phosphatase activity.


Pssm-ID: 350428 [Multi-domain]  Cd Length: 145  Bit Score: 38.58  E-value: 3.70e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 665404815 274 TTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAI 310
Cdd:cd14580   83 TPGAKVLVHCAVGVSRSATLVLAYLMIYHQLSLVQAI 119
DSP_DUSP15 cd14582
dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual ...
 259-318 5.58e-03

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


Pssm-ID: 350430 [Multi-domain]  Cd Length: 146  Bit Score: 38.01  E-value: 5.58e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665404815 259 TPSDAIMK------KFLSICETTKGAIAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLRLCRP 318
Cdd:cd14582   58 TPEAPIKKhfkeciSFIHQCRLNGGNCLVHCLAGISRSTTIVVAYVMAVTELSWQEVLEAIRAVRP 123
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 270-319 5.59e-03

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 38.92  E-value: 5.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 665404815 270 SICETTKGAIAVHCKAGLGRTGSLIGAY-IMKHYGFTALE-AIAWLRLCRPG 319
Cdd:cd14559  162 AINDKNKLLPVIHCRAGVGRTGQLAAAMeLNKSPNNLSVEdIVSDMRTSRNG 213
DSP_fungal_SDP1-like cd14521
dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, ...
 279-314 5.85e-03

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: 38.07  E-value: 5.85e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 665404815 279 IAVHCKAGLGRTGSLIGAYIMKHYGFTALEAIAWLR 314
Cdd:cd14521   97 VLIHCQCGVSRSASLIIAYIMKKLGLSLNDAYDLLK 132
 
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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