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 23956130 105 WYHRIDHTVLLGALPLKNMTRRLVLDENVRGVITMNEEYETRFLCNTSKEWKKAGVEQLRLSTVDMTGVPTLANLHKGVQ 184
Cdd:cd14524   1 WYDRIDDTVILGALPFRSMTVALVAKENVRGVITMNEEYETRFFCNSKEEWKALGVEQLRLPTVDFTGVPSLEDLEKGVD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956130 185 FALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEVLKEFHKE 253
Cdd:cd14524  81 FILKHREKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRPHILLRLSQREVLEEFYRK 149

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 23956130 105 WYHRIDHTVLLGALPLKNMTRRLVLDENVRGVITMNEEYETRFLCNTSKEWKKAGVEQLRLSTVDMTGVPTLANLHKGVQ 184
Cdd:cd14524   1 WYDRIDDTVILGALPFRSMTVALVAKENVRGVITMNEEYETRFFCNSKEEWKALGVEQLRLPTVDFTGVPSLEDLEKGVD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956130 185 FALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEVLKEFHKE 253
Cdd:cd14524  81 FILKHREKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRPHILLRLSQREVLEEFYRK 149

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956130   149 CNTSKEWKKAGVEQLRLSTVDMTGVPTLANLHKGVQFALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIE 228
Cdd:pfam00782  25 VTREVDLYNSGILYLRIPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYS 104

                          90       100
                  ....*....|....*....|..
gi 23956130   229 AIAKIRSHISIRPSQLEVLKEF 250
Cdd:pfam00782 105 FVKERRPGISPNFGFKRQLLEY 126

hypothetical protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956130  172 GVPTLANLHKGVQFALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVH-NWSPEEAIEAIAKIRSHISIRPSQLEVLKEF 250
Cdd:PRK12361 154 SVPTLAQLNQAINWIHRQVRANKSVVVHCALGRGRSVLVLAAYLLCKDpDLTVEEVLQQIKQIRKTARLNKRQLRALEKM 233

                 ...
gi 23956130  251 HKE 253
Cdd:PRK12361 234 LEQ 236

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 23956130 105 WYHRIDHTVLLGALPLKNMTRRLVLDENVRGVITMNEEYETRFLCNTSKEWKKAGVEQLRLSTVDMTGVPTLANLHKGVQ 184
Cdd:cd14524   1 WYDRIDDTVILGALPFRSMTVALVAKENVRGVITMNEEYETRFFCNSKEEWKALGVEQLRLPTVDFTGVPSLEDLEKGVD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956130 185 FALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEVLKEFHKE 253
Cdd:cd14524  81 FILKHREKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRPHILLRLSQREVLEEFYRK 149

Protein-tyrosine phosphatase [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956130 106 YHRIDHTVLLGALPLKNMTRrlVLDENVRGVITMNEEYETRFlcntsKEWKKAGVEQLRLSTVDMtGVPTLANLHKGVQF 185
Cdd:COG2453   1 SWIIPGLLAGGPLPGGGEAD--LKREGIDAVVSLTEEEELLL-----GLLEEAGLEYLHLPIPDF-GAPDDEQLQEAVDF 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956130 186 ALKYQALGQCVYVHCKAGRSRSATMVAAYLIQvHNWSPEEAIEAIAKIRSHISIRPSQLEVLKEFHKEI 254
Cdd:COG2453  73 IDEALREGKKVLVHCRGGIGRTGTVAAAYLVL-LGLSAEEALARVRAARPGAVETPAQRAFLERFAKRL 140

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956130   149 CNTSKEWKKAGVEQLRLSTVDMTGVPTLANLHKGVQFALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIE 228
Cdd:pfam00782  25 VTREVDLYNSGILYLRIPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYS 104

                          90       100
                  ....*....|....*....|..
gi 23956130   229 AIAKIRSHISIRPSQLEVLKEF 250
Cdd:pfam00782 105 FVKERRPGISPNFGFKRQLLEY 126

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956130 128 VLDENVRGVITMNEEyetrflCNTSKEWKKAGVEQLRLSTVDMTgVPTLANLHKGVQFALKYQALGQCVYVHCKAGRSRS 207
Cdd:cd14504  24 LNENGIRHVVTLTEE------PPPEHSDTCPGLRYHHIPIEDYT-PPTLEQIDEFLDIVEEANAKNEAVLVHCLAGKGRT 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 23956130 208 ATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEVLKEFHK 252
Cdd:cd14504  97 GTMLACYLVKTGKISAVDAINEIRRIRPGSIETSEQEKFVIQFAK 141

hypothetical protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956130  172 GVPTLANLHKGVQFALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVH-NWSPEEAIEAIAKIRSHISIRPSQLEVLKEF 250
Cdd:PRK12361 154 SVPTLAQLNQAINWIHRQVRANKSVVVHCALGRGRSVLVLAAYLLCKDpDLTVEEVLQQIKQIRKTARLNKRQLRALEKM 233

                 ...
gi 23956130  251 HKE 253
Cdd:PRK12361 234 LEQ 236

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
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23956130 196 VYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRshiSIRPS-----QLEVL 247
Cdd:cd14515  91 VLVHCVEGVSRSATLVLAYLMIYQNMTLEEAIRTVRKKR---EIRPNrgflqQLCEL 144

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956130 193 GQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRP---SQLEVLKEFH 251
Cdd:cd14518  90 GGAVLVHCAMGKSRSVTVVIAYLMYKYNLSVSQALHAVRRKRPIAEPNDgfmEQLELYHEMG 151

dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class I MKPs consist of DUSP1/MKP-1, DUSP2 (PAC1), DUSP4/MKP-2 and DUSP5. They are all mitogen- and stress-inducible nuclear MKPs. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23956130 183 VQFALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHIS 238
Cdd:cd14565  68 IGFIDKVKASGGRVLVHCQAGISRSATICLAYLMTTRRVRLNEAFDYVKQRRSVIS 123

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 23956130 174 PTLANLHKGVQFALKYQALGQ--CVYVHCKAGRSRSATMVAAYLIQVHNWS-PEEAIEAIAKIRSHISIR----PSQLEV 246
Cdd:cd14497  74 PPLGLLLEIVDDIDSWLSEDPnnVAVVHCKAGKGRTGTVICAYLLYYGQYStADEALEYFAKKRFKEGLPgvtiPSQLRY 153

                ....*.
gi 23956130 247 LKEFHK 252
Cdd:cd14497 154 LQYFER 159

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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23956130 196 VYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRShiSIRPSQ--LEVLKEFH 251
Cdd:cd14523  82 VLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNARP--SIRPNPgfMEQLKEYQ 137

dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs, which are involved in gene regulation, cell proliferation, programmed cell death and stress responses, as an important feedback control mechanism that limits MAPK cascades. MKPs, also referred to as typical DUSPs, function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III).

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956130 163 LRLSTVDMTGVPTLANLHKGVQFALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHIS 238
Cdd:cd14512  49 KRIPVNDSFCQNISPWFDEAIEFIEEAKASNGGVLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRPTIS 124

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956130 173 VPTLANLHKG------------VQFALKYQALGQC------VYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIR 234
Cdd:cd18534  35 VPDCQNLYKNsftyhvlseektVPFAEAVDFIEQCrkdkarVLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERR 114

                        90
                ....*....|....*.
gi 23956130 235 SHISIRPSQLEVLKEF 250
Cdd:cd18534 115 PSINLSPAVAKQLQEF 130

dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual specificity protein phosphatase 1 (DUSP1), also called mitogen-activated protein kinase (MAPK) phosphatase 1 (MKP-1), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. Human MKP-1 dephosphorylates MAPK1/ERK2, regulating its activity during the meiotic cell cycle. Although initially MKP-1 was considered to be ERK-specific, it has been shown that MKP-1 also dephosphorylates both JNK and p38 MAPKs. DUSP1/MKP-1 is involved in various functions, including proliferation, differentiation, and apoptosis in normal cells. It is a central regulator of a variety of functions in the immune, metabolic, cardiovascular, and nervous systems. It contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956130 179 LHKGVQFALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEVLKEFHKEITA 256
Cdd:cd14638  64 FNEAIDFIDSVKNAGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQVLA 141

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
                ....*....|....*....|....*....|....*....
gi 23956130 198 VHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSH 236
Cdd:cd17665 118 VHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGH 156

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
                ....*....|....*....|....*....|....*....
gi 23956130 196 VYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIR 234
Cdd:cd14575  99 LLVHCVMGRSRSATLVLAYLMIYKNMTVVDAIEQVAQRR 137

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956130 179 LHKGVQFALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEVLKEFHKEI 254
Cdd:cd14568  65 LDKAVEFIEKARASNKRVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRPTISPNFNFLGQLLEFEKKL 140

dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class II MKPs consist of DUSP6/MKP-3, DUSP7/MKP-X and DUSP9/MKP-4, and are ERK-selective cytoplasmic MKPs. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 23956130 195 CVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHIS 238
Cdd:cd14566  82 GVLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKRKSNIS 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.

                        10        20        30
                ....*....|....*....|....*....|
gi 23956130 198 VHCKAGRSRSATMVAAYLIQVHNWSPEEAI 227
Cdd:cd14499 114 VHCKAGLGRTGTLIACYLMKHYGFTAREAI 143

dual specificity phosphatase domain of slingshot homolog 2; Dual specificity protein phosphatase slingshot homolog 2 (SSH2), also called SSH-like protein 2, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. SSH2 has been identified as a target of protein kinase D1 that regulates cofilin phosphorylation and remodeling of the actin cytoskeleton during neutrophil chemotaxis. There are at least two human SSH2 isoforms reported: hSSH-2L (long) and hSSH-2. As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. In addition, hSSH-2L contains a long C-terminal tail while hSSH-2 does not.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956130 146 RFLCNTSKEWKK--AGV-EQLRLSTVDMTGVPTLANLHKGVQFALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWS 222
Cdd:cd14569  31 RYILNVTREIDNffPGLfEYHNIRVYDEEATDLLAYWNDTYKFISKAKKHGSKCLVHCKMGVSRSASTVIAYAMKEYGWN 110

                        90       100
                ....*....|....*....|....*....
gi 23956130 223 PEEAIEAIAKIRSHISIRPSQLEVLKEFH 251
Cdd:cd14569 111 LDRAYDYVKERRTVTKPNPSFMRQLEEYQ 139

dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual specificity protein phosphatase 5 (DUSP5) functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (MKPs), it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP5 preferentially dephosphorylates extracellular signal-regulated kinase (ERK), and is involved in ERK signaling and ERK-dependent inflammatory gene expression in adipocytes. It also plays a role in regulating pressure-dependent myogenic cerebral arterial constriction, which is crucial for the maintenance of constant cerebral blood flow to the brain. DUSP5 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956130 177 ANLHKGVQFALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHIS 238
Cdd:cd14639  62 SHFQEAIDFIDCVRRAGGKVLVHCEAGISRSPTICMAYLMKTKRFRLEEAFDYIKQRRSLIS 123

dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual specificity protein phosphatase 2 (DUSP2), also called dual specificity protein phosphatase PAC-1, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (MKPs), it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP2 can preferentially dephosphorylate ERK1/2 and p38, but not JNK in vitro. It is predominantly expressed in hematopoietic tissues with high T-cell content, such as thymus, spleen, lymph nodes, peripheral blood and other organs such as the brain and liver. It has a critical and positive role in inflammatory responses. DUSP2 mRNA and protein are significantly reduced in most solid cancers including breast, colon, lung, ovary, kidney and prostate, and the suppression of DUSP2 is associated with tumorigenesis and malignancy. DUSP2 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956130 193 GQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEVLKEFHKEI 254
Cdd:cd14641  81 GGRVLVHCQAGISRSATICLAYLIQSQRVRLDEAFDFVKQRRGVISPNFSFMGQLLQFETQV 142

Protein tyrosine phosphatase, catalytic domain motif;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 23956130    198 VHCKAGRSRSATMVAAYLI--QVHNWSPEEAIEAIAK-IRSH 236
Cdd:smart00404  44 VHCSAGVGRTGTFVAIDILlqQLEAEAGEVDIFDTVKeLRSQ 85

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
                ....*....|....*....|....*....|....*..
gi 23956130 198 VHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIR 234
Cdd:cd17664 116 VHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQAR 152

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 23956130 125 RRLVLDENVRGVITM---NEEYETRflcntSKEWKKAGVEQLRLSTvdMTGVPTLANLH---KGVQFALKYQAlgqcVYV 198
Cdd:cd14529  26 RALLKKLGIKTVIDLrgaDERAASE-----EAAAKIDGVKYVNLPL--SATRPTESDVQsflLIMDLKLAPGP----VLI 94

                        90       100       110
                ....*....|....*....|....*....|
gi 23956130 199 HCKAGRSRSATMVAAYLIQVHNwSPEEAIE 228
Cdd:cd14529  95 HCKHGKDRTGLVSALYRIVYGG-SKEEANE 123

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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23956130 198 VHCKAGRSRSATMVAAYLI--QVHNWSPEEAIEAIAKIRSHISIRP-SQLEVLKE 249
Cdd:cd14559 173 IHCRAGVGRTGQLAAAMELnkSPNNLSVEDIVSDMRTSRNGKMVQKdEQLDTLKE 227

dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; Serine/threonine/tyrosine interacting like 1 (STYXL1), also known as DUSP24 and MK-STYX, is a catalytically inactive phosphatase with homology to the mitogen-activated protein kinase (MAPK) phosphatases (MKPs). STYXL1 plays a role in regulating pathways by competing with active phosphatases for binding to MAPKs. Similar to MKPs, STYXL1 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, however its C-terminal dual specificity phosphatase-like domain is a pseudophosphatase missing the catalytic cysteine.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956130 123 MTRRLVLDENVRGVITMNEEYETRFlcntskewKKAGVEQLRLSTVDMTGVPTLANLHKGVQFALKYQALGQCVYVHCKA 202
Cdd:cd14517  28 CDKKIQKDLKIKAHINVSMDADELF--------KSGNDQVLHIPVEDSVEADLLSFFERACSFIDKHKNNGSRVLVFSTL 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 23956130 203 GRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRShiSIRPSQ 243
Cdd:cd14517 100 GISRSVAVAIAYLMYHYKWSLKDAWKYLLKCKN--NMRPNR 138

dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein phosphatase slingshot homolog 1 (SSH1), also called SSH-like protein 1, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. SSH1 links NOD1 signaling to actin remodeling, facilitating the changes that leads to NF-kappaB activation and innate immune responses. There are at least two human SSH1 isoforms reported: hSSH-1L (long) and hSSH-1S (short). As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. They also contain C-terminal tails, differing in the lengths of the tail.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956130 176 LANLHKGVQFALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRS 235
Cdd:cd14570  64 LAHWNDAYHFINKAKKNHSKCLVHCKMGVSRSASTVIAYAMKEFGWSLEKAYNFVKQKRS 123

dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual specificity protein phosphatase 9 (DUSP9), also called mitogen-activated protein kinase (MAPK) phosphatase 4 (MKP-4), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class II subfamily and is an ERK-selective cytoplasmic MKP. DUSP9 is a mediator of bone morphogenetic protein (BMP) signaling to control the appropriate ERK activity critical for the determination of embryonic stem cell fate. Down-regulation of DUSP9 expression has been linked to severe pre-eclamptic placenta as well as cancers such as hepatocellular carcinoma. DUSP9 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23956130 196 VYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEVLKEFHKEI 254
Cdd:cd14644  85 VLVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDLVKRKKSNISPNFNFMGQLLDFEKSL 143

dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual specificity protein phosphatase 8 (DUSP8), also called DUSP hVH-5 or M3/6, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP8 controls basal and acute stress-induced ERK1/2 signaling in adult cardiac myocytes, which impacts contractility, ventricular remodeling, and disease susceptibility. It also plays a role in decreasing ureteric branching morphogenesis by inhibiting p38MAPK. DUSP8 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956130 179 LHKGVQFALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEVLKEFHKEI 254
Cdd:cd14645  76 LDKSIEFIDKAKVSNCRVIVHCLAGISRSATIAIAYIMKTMGLSSDDAYRFVKDRRPSISPNFNFLGQLLEYEKSL 151

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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 23956130 196 VYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIaKIRSHIsIRPS 242
Cdd:cd14572  88 TLVHCAAGVSRSATLCIAYLMKYHRVSLLEAYNWV-KARRPV-IRPN 132

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.

                        10        20        30
                ....*....|....*....|....*....|.
gi 23956130 193 GQCVYVHCKAGRSRSATMVAAYLIQvHNWSP 223
Cdd:cd14567  80 GKGVLVHCQAGVSRSATIVIAYLMK-HTRMT 109

bacterial tyrosine-protein phosphataseS similar to Neisseria NMA1982; This subfamily is composed of bacterial tyrosine-protein phosphatases similar to Neisseria meningitidis NMA1982, which displays phosphatase activity but whose biological function is still unknown.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956130 174 PTLANLHkgvQFALKYQAL-GQCVYVHCKAGrSRSATMVAAYLIQVHNWSPEEAIEAIAKI 233
Cdd:cd14503  67 PTPEDVE---RFFEVMDAAqGKPVLVHCASN-MRASAFWYLYRALDGGVSEEEAIQLMRSA 123

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956130 191 ALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAiAKIRSHiSIRP--SQLEVLKEFHKEI 254
Cdd:cd14521  92 QSGKKVLIHCQCGVSRSASLIIAYIMKKLGLSLNDAYDL-LKSRSP-WIGPnmSLIFQLMEFEKVL 155