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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  10 LRPAPALIEYKGMKFLITDRPSDITINHYIMELKKNNVNTVVRVCEPSYNTDELETQGITVKDLAFEDGTFPPQQVVDEW 89
Cdd:cd14500   1 LRPAPTLIEYKGMRFLITDAPTDSNLPLYIKELKKYNVTDLVRVCEPTYDKEPLEKAGIKVHDWPFDDGSPPPDDVVDDW 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24584562  90 FEVLKDKYQQN--PEACVAVHCVAGLGRAPVLVALALIELGLKYEAAVEMIRDKRRGAINAKQLSFLEKYKPKARL 163
Cdd:cd14500  81 LDLLKTRFKEEgkPGACIAVHCVAGLGRAPVLVAIALIELGMKPEDAVEFIRKKRRGAINSKQLQFLEKYKPKKKL 156

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  10 LRPAPALIEYKGMKFLITDRPSDITINHYIMELKKNNVNTVVRVCEPSYNTDELETQGITVKDLAFEDGTFPPQQVVDEW 89
Cdd:cd14500   1 LRPAPTLIEYKGMRFLITDAPTDSNLPLYIKELKKYNVTDLVRVCEPTYDKEPLEKAGIKVHDWPFDDGSPPPDDVVDDW 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24584562  90 FEVLKDKYQQN--PEACVAVHCVAGLGRAPVLVALALIELGLKYEAAVEMIRDKRRGAINAKQLSFLEKYKPKARL 163
Cdd:cd14500  81 LDLLKTRFKEEgkPGACIAVHCVAGLGRAPVLVAIALIELGMKPEDAVEFIRKKRRGAINSKQLQFLEKYKPKKKL 156

Protein-tyrosine phosphatase [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  41 ELKKNNVNTVVRVC-EPSYNTDELETQGITVKDLAFEDGTFPPQQVVDEWFEVLKDKYQQNPEacVAVHCVAGLGRAPVL 119
Cdd:COG2453  20 DLKREGIDAVVSLTeEEELLLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKK--VLVHCRGGIGRTGTV 97

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 24584562 120 VALALIELGLKYEAAVEMIRDKRRGAI-NAKQLSFLEKY 157
Cdd:COG2453  98 AAAYLVLLGLSAEEALARVRAARPGAVeTPAQRAFLERF 136

Protein-tyrosine phosphatase;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584562    91 EVLKDKYQQNPEACVAVHCVAGLGRAPVLVALALIELGLKYE------AAVEMIRDKRRGAI-NAKQLSFL 154
Cdd:pfam00102 158 RKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEgevdifQIVKELRSQRPGMVqTLEQYIFL 228

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  10 LRPAPALIEYKGMKFLITDRPSDITINHYIMELKKNNVNTVVRVCEPSYNTDELETQGITVKDLAFEDGTFPPQQVVDEW 89
Cdd:cd14500   1 LRPAPTLIEYKGMRFLITDAPTDSNLPLYIKELKKYNVTDLVRVCEPTYDKEPLEKAGIKVHDWPFDDGSPPPDDVVDDW 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24584562  90 FEVLKDKYQQN--PEACVAVHCVAGLGRAPVLVALALIELGLKYEAAVEMIRDKRRGAINAKQLSFLEKYKPKARL 163
Cdd:cd14500  81 LDLLKTRFKEEgkPGACIAVHCVAGLGRAPVLVAIALIELGMKPEDAVEFIRKKRRGAINSKQLQFLEKYKPKKKL 156

protein tyrosine phosphatase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562   17 IEYKGMKFLITDRPSDITINHYIMELKKNNVNTVVRVCEPSYNTDELETQGITVKDLAFEDGTFPPQQVVDEWFEVLKDK 96
Cdd:PTZ00242  11 IEYVLFKFLILDAPSPSNLPLYIKELQRYNVTHLVRVCGPTYDAELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQE 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584562   97 YQQN--PEACVAVHCVAGLGRAPVLVALALIELG-LKYEAAVEMIRDKRRGAINAKQLSFLEKYKPKARLKH 165
Cdd:PTZ00242  91 FAKQstPPETIAVHCVAGLGRAPILVALALVEYGgMEPLDAVGFVREKRKGAINQTQLQFLKKYKPRKKAAG 162

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  11 RPAPALIEYKGMKFLITDRPSDITINHYIMELKKNNVNTVVRVCEPSYNTDELETQGITVKDLAFEDGTFPPQQVVDEWF 90
Cdd:cd18537   6 RPAPVEITYKNMRFLITHNPTNATLNKFIEELKKYGVTTVVRVCEATYDTTLVEKEGIQVLDWPFDDGAPPSNQIVDDWL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  91 EVLKDKYQQNPEACVAVHCVAGLGRAPVLVALALIELGLKYEAAVEMIRDKRRGAINAKQLSFLEKYKPKARLKHK--NG 168
Cdd:cd18537  86 NLLKVKFREEPGCCIAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFKdsNG 165

                ..
gi 24584562 169 HK 170
Cdd:cd18537 166 HR 167

Protein-tyrosine phosphatase [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  41 ELKKNNVNTVVRVC-EPSYNTDELETQGITVKDLAFEDGTFPPQQVVDEWFEVLKDKYQQNPEacVAVHCVAGLGRAPVL 119
Cdd:COG2453  20 DLKREGIDAVVSLTeEEELLLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKK--VLVHCRGGIGRTGTV 97

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 24584562 120 VALALIELGLKYEAAVEMIRDKRRGAI-NAKQLSFLEKY 157
Cdd:COG2453  98 AAAYLVLLGLSAEEALARVRAARPGAVeTPAQRAFLERF 136

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  21 GMKFLITDRPSDITINhyimELKKNNVNTVVRVCEP----SYNTDEL----ETQGITVKDLAFEDGTFPP-----QQVVD 87
Cdd:cd14505  22 GCKFKDHRRDLQADLE----ELKDQGVDDVVTLCTDgeleELGVPDLleqyQQAGITWHHLPIPDGGVPSdiaqwQELLE 97

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  88 EWFEVLKDKyqqnpeACVAVHCVAGLGRAPVLVALALIELG--LKYEAAVEMIRDKRRGAI-NAKQLSFL 154
Cdd:cd14505  98 ELLSALENG------KKVLIHCKGGLGRTGLIAACLLLELGdtLDPEQAIAAVRALRPGAIqTPKQENFL 161

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  26 ITD------RPSDITINHY--IMELKKNNVNTVVRVCEP----------------SYNTDELETQGITVKDLAFEDGTFP 81
Cdd:cd14506  11 ITDdilamaRPSTELIDKYgiIEQFKEKGIKTVINLQEPgehascgpglepesgfSYLPEAFMRAGIYFYNFGWKDYGVP 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584562  82 PQQVVDEWFEVLkDKYQQNPEAcVAVHCVAGLGRAPVLVALALIeLGLKYEA--AVEMIRDKRRGAINAK-QLSFLE 155
Cdd:cd14506  91 SLTTILDIVKVM-AFALQEGGK-VAVHCHAGLGRTGVLIACYLV-YALRMSAdqAIRLVRSKRPNSIQTRgQVLCVR 164

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  42 LKKNNVNTVVRVCEPSYNTdeLETQGITVKDLAFEDgtFPPQQVVDEWFEVLK--DKYQQNPEaCVAVHCVAGLGRAPVL 119
Cdd:cd14498  22 LKKLGITHILNVAGEPPPN--KFPDGIKYLRIPIED--SPDEDILSHFEEAIEfiEEALKKGG-KVLVHCQAGVSRSATI 96

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 24584562 120 VALALI-ELGLKYEAAVEMIRDKRRGA-INA---KQL 151
Cdd:cd14498  97 VIAYLMkKYGWSLEEALELVKSRRPIIsPNPgflKQL 133

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584562     91 EVLKDKYQQNPeacVAVHCVAGLGRAPVLVALALIELGLKYEAA-------VEMIRDKRRGAI-NAKQLSFL 154
Cdd:smart00012  31 KNLNQSESSGP---VVVHCSAGVGRTGTFVAIDILLQQLEAEAGevdifdtVKELRSQRPGMVqTEEQYLFL 99

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  60 TDELETQGITVKDLAFEDgtFPPQQV-------VDEWFEVLKDKYQQNPEACVAVHCVAGLGRAPVLVALALIELGLKYE 132
Cdd:cd14629 174 TDARDGQSRTIRQFQFTD--WPEQGVpktgegfIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYE 251

                ....*..
gi 24584562 133 AAVEMIR 139
Cdd:cd14629 252 GVVDMFQ 258

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  60 TDELETQGITVKDLAFEDgtFPPQQV-------VDEWFEVLKDKYQQNPEACVAVHCVAGLGRAPVLVALALIELGLKYE 132
Cdd:cd14627 174 TDARDGQSRTVRQFQFTD--WPEQGVpksgegfIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYE 251

                        90       100
                ....*....|....*....|...
gi 24584562 133 AAVE------MIRDKRRGAINAK 149
Cdd:cd14627 252 GVVDifqtvkMLRTQRPAMVQTE 274

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  60 TDELETQGITVKDLAFEDgtFPPQQV-------VDEWFEVLKDKYQQNPEACVAVHCVAGLGRAPVLVALALIELGLKYE 132
Cdd:cd14554 127 TDARDGQSRTVRQFQFTD--WPEQGVpksgegfIDFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYE 204

                        90       100
                ....*....|....*....|
gi 24584562 133 AAVEM------IRDKRRGAI 146
Cdd:cd14554 205 GVVDVfqtvklLRTQRPAMV 224

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  55 EPSYNTDELETQgitVKDLAFEDGTFPPQQVVDEWFEVLKDKYQQNPEACVAVHCVAGLGRAPVLVALALIELGlKYEAA 134
Cdd:cd14509  50 ERSYDPSKFNGR---VAEYPFDDHNPPPLELIKPFCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLG-KFPSA 125

                ....*
gi 24584562 135 VEMIR 139
Cdd:cd14509 126 KEALD 130

Protein tyrosine phosphatase, catalytic domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562     81 PPQQVVDEWFEVLK-----DKYQQNPEACVAVHCVAGLGRAPVLVALALIELGLKYE------AAVEMIRDKRRGAI-NA 148
Cdd:smart00194 168 PDHGVPESPESILDliravRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGkevdifEIVKELRSQRPGMVqTE 247

                   ....*.
gi 24584562    149 KQLSFL 154
Cdd:smart00194 248 EQYIFL 253

Dual specificity phosphatase, catalytic domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 24584562    105 VAVHCVAGLGRAPVLVALALIE-LGLKYEAAVEMIRDkRRGAIN 147
Cdd:smart00195  81 VLVHCQAGVSRSATLIIAYLMKtRNMSLNDAYDFVKD-RRPIIS 123

dual specificity phosphatase domain of laforin and similar domains; This family is composed of glucan phosphatases including vertebrate dual specificity protein phosphatase laforin, also called lafora PTPase (LAFPTPase), and plant starch excess4 (SEX4). Laforin is a glycogen phosphatase; its gene is mutated in Lafora progressive myoclonus epilepsy or Lafora disease (LD), a fatal autosomal recessive neurodegenerative disorder characterized by the presence of progressive neurological deterioration, myoclonus, and epilepsy. One characteristic of LD is the accumulation of insoluble glucans. Laforin prevents LD by at least two mechanisms: by preventing hyperphosphorylation of glycogen by dephosphorylating it, allowing proper glycogen formation, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with malin. Laforin contains an N-terminal CBM20 (carbohydrate-binding module, family 20) domain and a C-terminal catalytic dual specificity phosphatase (DSP) domain. Plant SEX4 regulate starch metabolism by selectively dephosphorylating glucose moieties within starch glucan chains. It contains an N-terminal catalytic DSP domain and a C-terminal Early (E) set domain.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24584562 104 CVAVHCVAGLGRAP--VLVALALIeLGLKYEAAVEMIRDKR 142
Cdd:cd14526  96 TVYVHCTAGLGRAPatVIAYLYWV-LGYSLDEAYYLLTSKR 135

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs 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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24584562 105 VAVHCVAGLGRAPVL----VALALIELGLKYE--AAVEMIRDKRRGAINAKQ 150
Cdd:cd14596 142 IVVHCSAGIGRAGVLicvdVLLSLIEKDLSFNikDIVREMRQQRYGMIQTKD 193

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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24584562 105 VAVHCVAGLGRAPVLVALALIE-LGLKYEAAVEMIRDkRRGAIN 147
Cdd:cd14522  92 VLVHGNAGISRSAALVIAYIMEtYGLSYRDAFAYVQQ-RRFCIN 134

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584562  42 LKKNNVNTVVRV---CEPSYNTDELETQGITVKDlAFEDGTFPpqqVVDEWFEVLKDKYQQNpeACVAVHCVAGLGRAPV 118
Cdd:cd14568  22 MQRNGISYVLNVsntCPKPDFIPDSHFLRIPVND-SYCEKLLP---WLDKAVEFIEKARASN--KRVLVHCLAGISRSAT 95

                        90       100
                ....*....|....*....|....*
gi 24584562 119 L-VALALIELGLKYEAAVEMIRDKR 142
Cdd:cd14568  96 IaIAYIMKHMRMSLDDAYRFVKEKR 120