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 26451280  52 DMSYISDKLLAMSFPAERMRAVYRNPLWQVKSVLDMRHPDHYKVYNLCIEESYDPDNFYGRVERFPFDDNHVPSLKMIQL 131
Cdd:cd14509   1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26451280 132 FCESVHSWLSLDPKNIAVVHCMAGKGRTGLMVSAYLVYGGM--SAEEALEMYASRRTTNNNGVSIPSQRRYVKYWSDL 207
Cdd:cd14509  81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKfpSAKEALDFYGAKRTKNKKGVTIPSQRRYVYYYSRL 158

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 26451280  52 DMSYISDKLLAMSFPAERMRAVYRNPLWQVKSVLDMRHPDHYKVYNLCIEESYDPDNFYGRVERFPFDDNHVPSLKMIQL 131
Cdd:cd14509   1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26451280 132 FCESVHSWLSLDPKNIAVVHCMAGKGRTGLMVSAYLVYGGM--SAEEALEMYASRRTTNNNGVSIPSQRRYVKYWSDL 207
Cdd:cd14509  81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKfpSAKEALDFYGAKRTKNKKGVTIPSQRRYVYYYSRL 158

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26451280   327 FDKPVRVSGDIRITFYQKMIGS----RLFYTCFNTAFITNGLLQFSIGELDKVGGN-GRSISGPDFSLELLFGP 395
Cdd:pfam10409  60 FPKGIPVQGDVLVEFYHKGSDLlseeKMFRFWFNTSFIEDNTLTLPKNELDKADKDkKDKRFPKDFKVELLFSE 133

Dual specificity phosphatase, catalytic domain;

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 26451280    150 VHCMAGKGRTGLMVSAYL-VYGGMSAEEALEMYASRR 185
Cdd:smart00195  83 VHCQAGVSRSATLIIAYLmKTRNMSLNDAYDFVKDRR 119

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 26451280  52 DMSYISDKLLAMSFPAERMRAVYRNPLWQVKSVLDMRHPDHYKVYNLCIEESYDPDNFYGRVERFPFDDNHVPSLKMIQL 131
Cdd:cd14509   1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26451280 132 FCESVHSWLSLDPKNIAVVHCMAGKGRTGLMVSAYLVYGGM--SAEEALEMYASRRTTNNNGVSIPSQRRYVKYWSDL 207
Cdd:cd14509  81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKfpSAKEALDFYGAKRTKNKKGVTIPSQRRYVYYYSRL 158

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280  52 DMSYISDKLLAMSFPAER-MRAVYRNPLWQVKSVLDMRHPDHYKVYNLCIEESYDPDNFYGRVERFPFDDNHVPSLKMIQ 130
Cdd:cd14497   1 DLSYITPRIIAMSFPATGyPESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDDSKFEGRVLHYGFPDHHPPPLGLLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280 131 LFCESVHSWLSLDPKNIAVVHCMAGKGRTGLMVSAYLVYGGM--SAEEALEMYASRRTTNN-NGVSIPSQRRYVKYWSDL 207
Cdd:cd14497  81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQysTADEALEYFAKKRFKEGlPGVTIPSQLRYLQYFERL 160

protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular proteins (tensin-1, -2, -3 and -4) act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Dysregulation of tensin expression has been implicated in human cancer. Tensin-1, -2, and -3 contain an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. In addition, tensin-2 contains a zinc finger N-terminal to its PTP domain. Tensin-4 is not included in this model as it does not contain a PTP-like domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280  52 DMSYISDKLLAMSFPAERMRAVYRNPLWQVKSVLDMRHPDHYKVYNLCiEESYDPDNFYGRVERFPFDDNHVPSLKMIQL 131
Cdd:cd14508   1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNLS-ERRHDLRSLNPKVLDFGWPELHAPPLEKLCS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280 132 FCESVHSWLSLDPKNIAVVHCMAGKGRTGLMVSAYLVYGGMSA--EEALEMYASRRTTNNN--GVSIPSQRRYVKYWSDL 207
Cdd:cd14508  80 ICKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISAtaDQALDRFAMKRFYDDKvgPLGQPSQKRYVGYFSGL 159

protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. It plays an essential role in TGF-beta-induced myofibroblast differentiation and myofibroblast-mediated formation of extracellular fibronectin and collagen matrix. It also positively regulates RhoA activity through its interaction with DLC1, a RhoGAP-containing tumor suppressor; the tensin-1-DLC1-RhoA signaling axis is critical in regulating cellular functions that lead to angiogenesis. Tensin-1 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280  52 DMSYISDKLLAMSFPAERMRAVYRNPLWQVKSVLDMRHPDHYKVYNLCiEESYDPDNFYGRVERFPFDDNHVPSLKMIQL 131
Cdd:cd14560   1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNLS-ERRHDISKLHPKVLDFGWPDLHAPALEKICS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280 132 FCESVHSWLSLDPKNIAVVHCMAGKGRTGLMVSAYLVYGGM--SAEEALEMYASRRTTNNNGVSI--PSQRRYVKYWSDL 207
Cdd:cd14560  80 ICKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNIsaSADQALDRFAMKRFYEDKVVPVgqPSQKRYVHYFSGL 159

protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called tensin-like C1 domain-containing phosphatase (TENC1) or C1 domain-containing phosphatase and tensin homolog (C1-TEN). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-2 is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It also modulates cell contractility and remodeling of collagen fibers through the DLC1, a RhoGAP that binds to tensins in focal adhesions. Tensin-2 may have phosphatase activity; it reduces AKT1 phosphorylation. It contains an N-terminal region with a zinc finger, a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280  52 DMSYISDKLLAMSFPAERMRAVYRNPLWQVKSVLDMRHPDHYKVYNLCiEESYDPDNFYGRVERFPFDDNHVPSLKMIQL 131
Cdd:cd14562   1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNLS-EKRHDITRLNPKVQDFGWPDLHAPPLDKICS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280 132 FCESVHSWLSLDPKNIAVVHCMAGKGRTGLMVSAYLVYGGMS--AEEALEMYASRRTTNNN-GVSI-PSQRRYVKYWSDL 207
Cdd:cd14562  80 ICKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISagADQALSTLAMRKFCEDKvATSLqPSQRRYISYFGGL 159

Protein-tyrosine phosphatase [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280  56 ISDKLLAMSFPAERMRAVYRnplWQVKSVLDMRHPDHYKVyNLCIEESYdpdnfygRVERFPFDDNHVPSLKMIQLFCES 135
Cdd:COG2453   4 IPGLLAGGPLPGGGEADLKR---EGIDAVVSLTEEEELLL-GLLEEAGL-------EYLHLPIPDFGAPDDEQLQEAVDF 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26451280 136 VHSWLSLDPKNiaVVHCMAGKGRTGLMVSAYLVYGGMSAEEALEMYASRRTTNnngVSIPSQRRYVKYWSDLL 208
Cdd:COG2453  73 IDEALREGKKV--LVHCRGGIGRTGTVAAAYLVLLGLSAEEALARVRAARPGA---VETPAQRAFLERFAKRL 140

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 26451280  54 SYISDKLLAMSFPAERMRAVYrNPLWQ-----VKSVLDMRHP-DHYKVYNLCIEES---YDPDNFYGR---VERFPFDDN 121
Cdd:cd14506   9 SWITDDILAMARPSTELIDKY-GIIEQfkekgIKTVINLQEPgEHASCGPGLEPESgfsYLPEAFMRAgiyFYNFGWKDY 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26451280 122 HVPSLKMIQLFCESVHSWLSLDPKnIAVvHCMAGKGRTGLMVSAYLVYG-GMSAEEALEMYASRR 185
Cdd:cd14506  88 GVPSLTTILDIVKVMAFALQEGGK-VAV-HCHAGLGRTGVLIACYLVYAlRMSADQAIRLVRSKR 150

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280  54 SYISDK-LLAMSFPAERMRAVYRnPLWQVKsvldmrhpdHYKVYNLCIEesydpdnfygrverfpfddnhvpslkMIQLF 132
Cdd:cd14494   2 NWIDPLrLIAGALPLSPLEADSR-FLKQLG---------VTTIVDLTLA--------------------------MVDRF 45

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280 133 CESVHSWLSLDPKniAVVHCMAGKGRTGLMVSAYLV-YGGMSAEEALEMYASRRTtnNNGVSIPSQRRYV 201
Cdd:cd14494  46 LEVLDQAEKPGEP--VLVHCKAGVGRTGTLVACYLVlLGGMSAEEAVRIVRLIRP--GGIPQTIEQLDFL 111

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280  52 DMSYIS-DKLLAMSFPAERMRAVYRNPlwqvksvldMRHPDHY----KVYNL-CI----EESYDPdnfygrvERF----- 116
Cdd:cd14499  17 DLNWIVpGKFLAFSGPHDTRKDENGYP---------THTPEDYipyfKKLGVtTVvrlnKKLYDA-------KRFtdagi 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26451280 117 -----PFDDNHVPSLKMIQLFCESVHSwlslDPKNIAVvHCMAGKGRTGLMVSAYLVYG-GMSAEEA 177
Cdd:cd14499  81 rhydlYFPDGSTPSDDIVKKFLDICEN----EKGAIAV-HCKAGLGRTGTLIACYLMKHyGFTAREA 142

protein tyrosine phosphatase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280   92 HYKVYNL--CIEESYDPDNFYGR---VERFPFDDNHVPSLKMIQlfcesvhSWLSL----------DPKNIAVvHCMAGK 156
Cdd:PTZ00242  38 RYNVTHLvrVCGPTYDAELLEKNgieVHDWPFDDGAPPPKAVID-------NWLRLldqefakqstPPETIAV-HCVAGL 109

                         90       100       110
                 ....*....|....*....|....*....|
gi 26451280  157 GRTGLMVSAYLV-YGGMSAEEALEMYASRR 185
Cdd:PTZ00242 110 GRAPILVALALVeYGGMEPLDAVGFVREKR 139

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280  66 PAERMRAVYRNplWQVKSVLDMRHPDHYKVYNLCIEEsydPDNFygRVERFPFDDnHVPSLKMIQLFCESVhswLSLDPK 145
Cdd:cd14529  21 SPDEDRALLKK--LGIKTVIDLRGADERAASEEAAAK---IDGV--KYVNLPLSA-TRPTESDVQSFLLIM---DLKLAP 89

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 26451280 146 NIAVVHCMAGKGRTGLMVSAYL-VYGGmSAEEALEMYA 182
Cdd:cd14529  90 GPVLIHCKHGKDRTGLVSALYRiVYGG-SKEEANEDYR 126

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26451280 122 HVPSLKMIQLFCESVHSWLSLdpKNIAVVHCMAGKGRTGLMVSAYLVY-GGMSAEEALEMYASRR 185
Cdd:cd14524  68 GVPSLEDLEKGVDFILKHREK--GKSVYVHCKAGRGRSATIVACYLIQhKGWSPEEAQEFLRSKR 130

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280 109 FYGrverFPFDDnhVPSLKMIQLFCES---VHSWLSlDPKNIAVVHCMAGKGRTGLMVSAYL-VYGGMSAEEALEMYASR 184
Cdd:cd14515  56 YLG----IPASD--LPTFDISQYFDEAadfIDKALS-DPGGKVLVHCVEGVSRSATLVLAYLmIYQNMTLEEAIRTVRKK 128

                .
gi 26451280 185 R 185
Cdd:cd14515 129 R 129

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 26451280  97 NLCIEESYDPDNFYGRVERFPFDDNhvPSLKMIQLFcESVHSWL--SLDPKNIAVVHCMAGKGRTGLMVSAYL-VYGGMS 173
Cdd:cd14498  32 NVAGEPPPNKFPDGIKYLRIPIEDS--PDEDILSHF-EEAIEFIeeALKKGGKVLVHCQAGVSRSATIVIAYLmKKYGWS 108

                        90
                ....*....|..
gi 26451280 174 AEEALEMYASRR 185
Cdd:cd14498 109 LEEALELVKSRR 120

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
                   ....*....|....*....|....*....|....*....|....*....|..
gi 26451280    120 DNHVPSLKMIQL-FCESVHSWLS-LDPKNIAVVHCMAGKGRTGLMVSAYLVY 169
Cdd:smart00012  12 DHGVPESPDSILeLLRAVKKNLNqSESSGPVVVHCSAGVGRTGTFVAIDILL 63

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26451280   115 RFPFDDNHV----PSLKMIQLFCESVHSwlslDPKNIaVVHCMAGKGRTGLMVSAYL-VYGGMSAEEALEMYASRR 185
Cdd:pfam00782  40 RIPVEDNHEtnisKYLEEAVEFIDDARQ----KGGKV-LVHCQAGISRSATLIIAYLmKTRNLSLNEAYSFVKERR 110

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

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26451280 124 PSLKMIQLF---CESVHSWLSlDPKNIAVVHCMAGKGRTGLMVSAYL-VYGGMSAEEALEMYASRR 185
Cdd:cd14575  73 PTFNLSQFFysaAEFIHQALS-DPHNKLLVHCVMGRSRSATLVLAYLmIYKNMTVVDAIEQVAQRR 137

hypothetical protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280  117 PFDDNHVPSLKMIQLFCESVHSWLSlDPKNIaVVHCMAGKGRTGLMVSAYLVYG--GMSAEEALE-MYASRRTTNNNgvs 193
Cdd:PRK12361 149 PILDHSVPTLAQLNQAINWIHRQVR-ANKSV-VVHCALGRGRSVLVLAAYLLCKdpDLTVEEVLQqIKQIRKTARLN--- 223

                         90
                 ....*....|...
gi 26451280  194 iPSQRRYVKYWSD 206
Cdd:PRK12361 224 -KRQLRALEKMLE 235

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26451280  66 PAERMRAVYRNPL---WQVKSVLDMRHPDHYKVYNLCIEESYDPDNFYGRVERFPFDDNHVPSLK-MIQLFcesvhswls 141
Cdd:COG2365  58 PAEVARAPDRLPPgvrYVHLPVLPDDAEALLEELRDGDLTPGDAEEFMLELYRAFVDPDAADAYRaAFRAL--------- 128

                        90       100
                ....*....|....*....|....*..
gi 26451280 142 LDPKNIAV-VHCMAGKGRTGLMVSAYL 167
Cdd:COG2365 129 ADAENGPVlFHCTAGKDRTGVAAALLL 155