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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300652  34 RWKDYLPVGQRMPGTRFIAFKVPLQKSFEKKLAPEECFSPLDLFNKIREQNEELGLIIDLTYTQRYYKPEDLPETVPYLK 113
Cdd:cd17665     1 RWIDYLPVGQRIPGTRFIAFKVPLRKSFFANLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPRDLTNHGVYYK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300652 114 IFTV-GHQVPDDETIFKFKHAVNGFLKENKDNDKLIGVHCTHGLNRTGYLICRYLIDVEGVRPDDAIELFNRCRGHCLER 192
Cdd:cd17665    81 KITCpGHQVPDDKTIQSFKDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGHPIER 160

                  ....*....
gi 2066300652 193 QNYIEDLQN 201
Cdd:cd17665   161 ENYLEDLLK 169

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300652  34 RWKDYLPVGQRMPGTRFIAFKVPLQKSFEKKLAPEECFSPLDLFNKIREQNEELGLIIDLTYTQRYYKPEDLPETVPYLK 113
Cdd:cd17665     1 RWIDYLPVGQRIPGTRFIAFKVPLRKSFFANLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPRDLTNHGVYYK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300652 114 IFTV-GHQVPDDETIFKFKHAVNGFLKENKDNDKLIGVHCTHGLNRTGYLICRYLIDVEGVRPDDAIELFNRCRGHCLER 192
Cdd:cd17665    81 KITCpGHQVPDDKTIQSFKDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGHPIER 160

                  ....*....
gi 2066300652 193 QNYIEDLQN 201
Cdd:cd17665   161 ENYLEDLLK 169

Dual specificity phosphatase, catalytic domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300652   82 EQNEELG--LIIDLTYTQRYYKPEDlpetVPYLKIftvghQVPDDET--IFKFKHAVNGFLKENKDNDKLIGVHCTHGLN 157
Cdd:smart00195  20 ALLKKLGitHVINVTNEVPNYNGSD----FTYLGV-----PIDDNTEtkISPYFPEAVEFIEDAESKGGKVLVHCQAGVS 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2066300652  158 RTGYLICRYLIDVEGVRPDDAIELFNRCRGHCLERQNYIEDLQ 200
Cdd:smart00195  91 RSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLI 133

protein tyrosine phosphatase; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2066300652 137 FLKENKDNDKlIGVHCTHGLNRTGYLICRYLIDVEGVRPDDAIELFNRCR 186
Cdd:PTZ00242   91 FAKQSTPPET-IAVHCVAGLGRAPILVALALVEYGGMEPLDAVGFVREKR 139

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300652  34 RWKDYLPVGQRMPGTRFIAFKVPLQKSFEKKLAPEECFSPLDLFNKIREQNEELGLIIDLTYTQRYYKPEDLPETVPYLK 113
Cdd:cd17665     1 RWIDYLPVGQRIPGTRFIAFKVPLRKSFFANLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPRDLTNHGVYYK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300652 114 IFTV-GHQVPDDETIFKFKHAVNGFLKENKDNDKLIGVHCTHGLNRTGYLICRYLIDVEGVRPDDAIELFNRCRGHCLER 192
Cdd:cd17665    81 KITCpGHQVPDDKTIQSFKDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGHPIER 160

                  ....*....
gi 2066300652 193 QNYIEDLQN 201
Cdd:cd17665   161 ENYLEDLLK 169

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300652  34 RWKDYLPVGQRMPGtRFIAFKVPLQKSFEKKLAPEECFSPLDLFNKIREQNEELGLIIDLTYTQRYYKPEDLPE-TVPYL 112
Cdd:cd17664     1 RWLNCPRKGQPVAG-KFLPFKTPLGPRYDDQVPEENRFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNEVEKeGCKYI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300652 113 KIFTVGH-QVPDDETIFKFKHAVNGFLKENKDndKLIGVHCTHGLNRTGYLICRYLIDVEGVRPDDAIELFNRCRGHCLE 191
Cdd:cd17664    80 KLQCKGHgECPSPEQTETFIRLCENFIEKNPL--ELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGIY 157

                  ....*...
gi 2066300652 192 RQNYIEDL 199
Cdd:cd17664   158 KGDYLKEL 165

Dual specificity phosphatase, catalytic domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300652   82 EQNEELG--LIIDLTYTQRYYKPEDlpetVPYLKIftvghQVPDDET--IFKFKHAVNGFLKENKDNDKLIGVHCTHGLN 157
Cdd:smart00195  20 ALLKKLGitHVINVTNEVPNYNGSD----FTYLGV-----PIDDNTEtkISPYFPEAVEFIEDAESKGGKVLVHCQAGVS 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2066300652  158 RTGYLICRYLIDVEGVRPDDAIELFNRCRGHCLERQNYIEDLQ 200
Cdd:smart00195  91 RSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLI 133

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
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2066300652 137 FLKENKDNDKLIGVHCTHGLNRTGYLICRYLIDVEGVRPDDAIELFNRCRGH 188
Cdd:cd14494    48 VLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPG 99

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2066300652 112 LKIFTVGHQVPDDETIFKFKHAVNGFLkeNKDNDKLIGVHCTHGLNRTGYLICRYLID 169
Cdd:cd14510    77 ERVPIDDHNVPTLDEMLSFTAEVREWM--AADPKNVVAIHCKGGKGRTGTMVCAWLIY 132

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 2066300652  46 PGTRFIAFKVPLQKSFE--KKLAPEECFSPLdlfnkireQNEELgliidltytqRYYKPEDLPETVPYLKIfTVGH---- 119
Cdd:cd14505    21 PGCKFKDHRRDLQADLEelKDQGVDDVVTLC--------TDGEL----------EELGVPDLLEQYQQAGI-TWHHlpip 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300652 120 --QVPDDETIFKFkhaVNGFLKENKDNDKLIGVHCTHGLNRTGYLICRYLIDVEG-VRPDDAIELFNRCRGHCLE--RQ- 193
Cdd:cd14505    82 dgGVPSDIAQWQE---LLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDtLDPEQAIAAVRALRPGAIQtpKQe 158

                  ....*
gi 2066300652 194 NYIED 198
Cdd:cd14505   159 NFLHQ 163

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2066300652 119 HQVPDDETIFKFKHAVNGFLKENKDNdkLIGVHCTHGLNRTGYLICRYLIDVEGVR-PDDAIELFNRCR 186
Cdd:cd14509    70 HNPPPLELIKPFCEDVDEWLKEDEKN--VAAVHCKAGKGRTGVMICCYLLYLGKFPsAKEALDFYGAKR 136

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 2066300652  119 HQVPDD-ETIFKFKHAVNGFLKENKDNdKLIGVHCTHGLNRTGYLICRYLI 168
Cdd:smart00012  13 HGVPESpDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDIL 62

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300652 118 GHQVPDDETIFKFKHAVNGFLKENKDNdkLIGVHCTHGLNRTGYLICRYLI-DVEGVRPDDAIELFNRCR 186
Cdd:cd14497    70 DHHPPPLGLLLEIVDDIDSWLSEDPNN--VAVVHCKAGKGRTGTVICAYLLyYGQYSTADEALEYFAKKR 137

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300652 109 VPYLKIFTVGH-QVPDDETIFKfkhAVNgFLKENKDNDKLIGVHCTHGLNRTGYLICRYLIDVEGVRPDDAIELFNRCRG 187
Cdd:cd14524    56 VEQLRLPTVDFtGVPSLEDLEK---GVD-FILKHREKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRP 131

                  ....*
gi 2066300652 188 HCLER 192
Cdd:cd14524   132 HILLR 136

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2066300652 141 NKDNDKLIGVHCTHGLNRTGYLICRYLIDVEGVRPDDAIELFNRCRGHCLERQNYIEDLQNGPIR 205
Cdd:cd14529    85 LKLAPGPVLIHCKHGKDRTGLVSALYRIVYGGSKEEANEDYRLSNRHLEGLRSGIALDSKGGVKG 149