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Conserved domains on  [gi|1819252707|ref|WP_164963067|]
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MULTISPECIES: cyclin-dependent kinase inhibitor 3 family protein [unclassified Rubrivivax]

Protein Classification

cyclin-dependent kinase inhibitor 3 family protein( domain architecture ID 12998225)

cyclin-dependent kinase inhibitor 3 family protein belongs to a superfamily of protein tyrosine phosphatases and dual-specificity phosphatases, such as eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 24-179 2.58e-55

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


:

Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 172.45  E-value: 2.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  24 GRIGITFCPGKHDRSaatgaWARDLGMDLDTIAAWGAKLVLTLVEPAELSALKVPQLGHEVRRRGIAWQHLPIPDFGVPG 103
Cdd:cd14505    13 GSLGLTPCPGCKFKD-----HRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPIPDGGVPS 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819252707 104 EhfERQWVQAGAEIRALLRAGDDVLVHCKGGLGRAGMIAARLLAELGVA--PEQAIRDVRRARHGAIETPAQMMLVQR 179
Cdd:cd14505    88 D--IAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTldPEQAIAAVRALRPGAIQTPKQENFLHQ 163
 
Name Accession Description Interval E-value
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 24-179 2.58e-55

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 172.45  E-value: 2.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  24 GRIGITFCPGKHDRSaatgaWARDLGMDLDTIAAWGAKLVLTLVEPAELSALKVPQLGHEVRRRGIAWQHLPIPDFGVPG 103
Cdd:cd14505    13 GSLGLTPCPGCKFKD-----HRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPIPDGGVPS 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819252707 104 EhfERQWVQAGAEIRALLRAGDDVLVHCKGGLGRAGMIAARLLAELGVA--PEQAIRDVRRARHGAIETPAQMMLVQR 179
Cdd:cd14505    88 D--IAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTldPEQAIAAVRALRPGAIQTPKQENFLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
23-179 7.19e-35

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 119.31  E-value: 7.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  23 HGRIGITFCPGKHDrsaatgawardlgmdlDTIAAWGAKLVLTLVEPAELsalkvpqLGHEVRRRGIAWQHLPIPDFGVP 102
Cdd:COG2453     5 PGLLAGGPLPGGGE----------------ADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAP 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819252707 103 GEhfeRQWVQAGAEIRALLRAGDDVLVHCKGGLGRAGMIAARLLAELGVAPEQAIRDVRRARHGAIETPAQMMLVQR 179
Cdd:COG2453    62 DD---EQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYLVLLGLSAEEALARVRAARPGAVETPAQRAFLER 135
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 46-157 2.11e-11

Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase inhibitor 3 or kinase associated phosphatase proteins from several mammalian species. The cyclin-dependent kinase (Cdk)-associated protein phosphatase (KAP) is a human dual specificity protein phosphatase that dephosphorylates Cdk2 on threonine 160 in a cyclin-dependent manner.


Pssm-ID: 399018  Cd Length: 168  Bit Score: 59.27  E-value: 2.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  46 RDLGMDLDTIAAWGAKLVLTLVEPAELSALKVPQLGHEVRRRGIAWQHLPIPDFGVPgeHFERQWvQAGAEIRALLRAGD 125
Cdd:pfam05706  58 RNIQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPIADGGTP--DIASCC-EIMEELATCLKNNR 134

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1819252707 126 DVLVHCKGGLGRAGMIAARLLAELG--VAPEQAI 157
Cdd:pfam05706 135 KTLIHCYGGLGRSCLVAACLLLYLSdsISPEQAI 168
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 84-182 1.51e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 54.26  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  84 VRRRGIAWQHLPIPDFGVPGEHFERQWVQAGAEIRAllRAGDD---VLVHCKGGLGRAGMIAARLLAELG-VAPEQAIRD 159
Cdd:PTZ00242   57 LEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQEFA--KQSTPpetIAVHCVAGLGRAPILVALALVEYGgMEPLDAVGF 134

                          90       100
                  ....*....|....*....|...
gi 1819252707 160 VRRARHGAIETPaQMMLVQRTRP 182
Cdd:PTZ00242  135 VREKRKGAINQT-QLQFLKKYKP 156
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
92-173 2.65e-08

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 49.66  E-value: 2.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707   92 QHLPIPDFGVPGEHFE-RQWVQAgaeIRALLRAGDD---VLVHCKGGLGRAG------MIAARLLAELG-VAPEQAIRDV 160
Cdd:smart00404   6 HYTGWPDHGVPESPDSiLELLRA---VKKNLNQSESsgpVVVHCSAGVGRTGtfvaidILLQQLEAEAGeVDIFDTVKEL 82

                           90
                   ....*....|...
gi 1819252707  161 RRARHGAIETPAQ 173
Cdd:smart00404  83 RSQRPGMVQTEEQ 95
 
Name Accession Description Interval E-value
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 24-179 2.58e-55

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 172.45  E-value: 2.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  24 GRIGITFCPGKHDRSaatgaWARDLGMDLDTIAAWGAKLVLTLVEPAELSALKVPQLGHEVRRRGIAWQHLPIPDFGVPG 103
Cdd:cd14505    13 GSLGLTPCPGCKFKD-----HRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPIPDGGVPS 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819252707 104 EhfERQWVQAGAEIRALLRAGDDVLVHCKGGLGRAGMIAARLLAELGVA--PEQAIRDVRRARHGAIETPAQMMLVQR 179
Cdd:cd14505    88 D--IAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTldPEQAIAAVRALRPGAIQTPKQENFLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
23-179 7.19e-35

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 119.31  E-value: 7.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  23 HGRIGITFCPGKHDrsaatgawardlgmdlDTIAAWGAKLVLTLVEPAELsalkvpqLGHEVRRRGIAWQHLPIPDFGVP 102
Cdd:COG2453     5 PGLLAGGPLPGGGE----------------ADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAP 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819252707 103 GEhfeRQWVQAGAEIRALLRAGDDVLVHCKGGLGRAGMIAARLLAELGVAPEQAIRDVRRARHGAIETPAQMMLVQR 179
Cdd:COG2453    62 DD---EQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYLVLLGLSAEEALARVRAARPGAVETPAQRAFLER 135
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 51-177 3.52e-15

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 68.84  E-value: 3.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  51 DLDTIAAWGAKLVLTLVEPaelsalkvPQLGHEVRRRGIAWQHLPIPDFGVPgehferQWVQAGAEIRALLRA---GDDV 127
Cdd:cd14504    20 HYAYLNENGIRHVVTLTEE--------PPPEHSDTCPGLRYHHIPIEDYTPP------TLEQIDEFLDIVEEAnakNEAV 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1819252707 128 LVHCKGGLGRAGMIAARLLAELG-VAPEQAIRDVRRARHGAIETPAQMMLV 177
Cdd:cd14504    86 LVHCLAGKGRTGTMLACYLVKTGkISAVDAINEIRRIRPGSIETSEQEKFV 136
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 86-178 7.39e-13

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 63.91  E-value: 7.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  86 RRGIAWQHLPIPDFGVPGEHFERQWVQAGAeirALLRAGDDVLVHCKGGLGRAGM-IAARLLAELGVAPEQAIRDVRRAR 164
Cdd:cd14506    74 RAGIYFYNFGWKDYGVPSLTTILDIVKVMA---FALQEGGKVAVHCHAGLGRTGVlIACYLVYALRMSADQAIRLVRSKR 150

                          90
                  ....*....|....
gi 1819252707 165 HGAIETPAQMMLVQ 178
Cdd:cd14506   151 PNSIQTRGQVLCVR 164
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 46-157 2.11e-11

Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase inhibitor 3 or kinase associated phosphatase proteins from several mammalian species. The cyclin-dependent kinase (Cdk)-associated protein phosphatase (KAP) is a human dual specificity protein phosphatase that dephosphorylates Cdk2 on threonine 160 in a cyclin-dependent manner.


Pssm-ID: 399018  Cd Length: 168  Bit Score: 59.27  E-value: 2.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  46 RDLGMDLDTIAAWGAKLVLTLVEPAELSALKVPQLGHEVRRRGIAWQHLPIPDFGVPgeHFERQWvQAGAEIRALLRAGD 125
Cdd:pfam05706  58 RNIQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPIADGGTP--DIASCC-EIMEELATCLKNNR 134

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1819252707 126 DVLVHCKGGLGRAGMIAARLLAELG--VAPEQAI 157
Cdd:pfam05706 135 KTLIHCYGGLGRSCLVAACLLLYLSdsISPEQAI 168
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 83-168 5.63e-10

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


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 55.30  E-value: 5.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  83 EVRRRGIAWQHLPIPDFGVPGEHFERQWVQagaeiraLLRA--------GDDVLVHCKGGLGRAGMIAARLLAELGVAPE 154
Cdd:cd14500    53 PLEKAGIKVHDWPFDDGSPPPDDVVDDWLD-------LLKTrfkeegkpGACIAVHCVAGLGRAPVLVAIALIELGMKPE 125

                          90
                  ....*....|....
gi 1819252707 155 QAIRDVRRARHGAI 168
Cdd:cd14500   126 DAVEFIRKKRRGAI 139
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 84-182 1.51e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 54.26  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  84 VRRRGIAWQHLPIPDFGVPGEHFERQWVQAGAEIRAllRAGDD---VLVHCKGGLGRAGMIAARLLAELG-VAPEQAIRD 159
Cdd:PTZ00242   57 LEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQEFA--KQSTPpetIAVHCVAGLGRAPILVALALVEYGgMEPLDAVGF 134

                          90       100
                  ....*....|....*....|...
gi 1819252707 160 VRRARHGAIETPaQMMLVQRTRP 182
Cdd:PTZ00242  135 VREKRKGAINQT-QLQFLKKYKP 156
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 117-179 5.12e-09

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 51.58  E-value: 5.12e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819252707 117 IRALLRAGDDVLVHCKGGLGRAG-MIAARLLAELGVAPEQAIRDVRRAR-HGAIETPAQMMLVQR 179
Cdd:cd14494    49 LDQAEKPGEPVLVHCKAGVGRTGtLVACYLVLLGGMSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 49-165 1.85e-08

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


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 51.11  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  49 GMDLDTIAAWGAKLVLTLVEPAELSALKVPQlgHEVRRRGIAWQHLPIPDF-GVPgehfERQWVQAGAE-IRALLRAGDD 126
Cdd:cd14524    18 SMTVALVAKENVRGVITMNEEYETRFFCNSK--EEWKALGVEQLRLPTVDFtGVP----SLEDLEKGVDfILKHREKGKS 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1819252707 127 VLVHCKGGLGRAGMIAARLLAEL-GVAPEQAIRDVRRARH 165
Cdd:cd14524    92 VYVHCKAGRGRSATIVACYLIQHkGWSPEEAQEFLRSKRP 131
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 63-182 2.15e-08

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


Pssm-ID: 350511 [Multi-domain]  Cd Length: 154  Bit Score: 50.79  E-value: 2.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  63 VLTLVEPAELSALKVPqlgheVRRRGIAWQHLPIPDFGVPGEHFERQWVQAgAEIRALLRAGDDVLVHCKGGLGRAGMIA 142
Cdd:cd18535    38 ATTVVRVCEVTYDKTP-----LEKDGITVVDWPFDDGAPPPGKVVEDWLSL-LKTKFCEDPGCCVAVHCVAGLGRAPVLV 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1819252707 143 ARLLAELGVAPEQAIRDVRRARHGAIETpAQMMLVQRTRP 182
Cdd:cd18535   112 ALALIESGMKYEDAIQFIRQKRRGAINS-KQLTYLEKYRP 150
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
92-173 2.65e-08

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 49.66  E-value: 2.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707   92 QHLPIPDFGVPGEHFE-RQWVQAgaeIRALLRAGDD---VLVHCKGGLGRAG------MIAARLLAELG-VAPEQAIRDV 160
Cdd:smart00404   6 HYTGWPDHGVPESPDSiLELLRA---VKKNLNQSESsgpVVVHCSAGVGRTGtfvaidILLQQLEAEAGeVDIFDTVKEL 82

                           90
                   ....*....|...
gi 1819252707  161 RRARHGAIETPAQ 173
Cdd:smart00404  83 RSQRPGMVQTEEQ 95
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 92-173 2.65e-08

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 49.66  E-value: 2.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707   92 QHLPIPDFGVPGEHFE-RQWVQAgaeIRALLRAGDD---VLVHCKGGLGRAG------MIAARLLAELG-VAPEQAIRDV 160
Cdd:smart00012   6 HYTGWPDHGVPESPDSiLELLRA---VKKNLNQSESsgpVVVHCSAGVGRTGtfvaidILLQQLEAEAGeVDIFDTVKEL 82

                           90
                   ....*....|...
gi 1819252707  161 RRARHGAIETPAQ 173
Cdd:smart00012  83 RSQRPGMVQTEEQ 95
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 63-182 6.98e-08

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


Pssm-ID: 350512 [Multi-domain]  Cd Length: 155  Bit Score: 49.61  E-value: 6.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  63 VLTLVEPAELSALKVPqlgheVRRRGIAWQHLPIPDFGVPGEHFERQWVQAgaeIRALLR--AGDDVLVHCKGGLGRAGM 140
Cdd:cd18536    39 VTTLVRVCDATYDKAP-----VEKEGIQVLDWPFDDGAPPPNQIVDDWLNL---LKTKFReePGCCVAVHCVAGLGRAPV 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1819252707 141 IAARLLAELGVAPEQAIRDVRRARHGAIETpAQMMLVQRTRP 182
Cdd:cd18536   111 LVALALIECGMKYEDAVQFIRQKRRGAFNS-KQLLYLEKYRP 151
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 51-162 2.10e-07

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.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 48.14  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  51 DLDTIAAWGAKLVLTLVEPAELSALKVPQLghevRRRGIAWQHLPIPDFGVPGEHferqwVQAGAEIRALLRAGDDVLVH 130
Cdd:cd14529    25 DRALLKKLGIKTVIDLRGADERAASEEAAA----KIDGVKYVNLPLSATRPTESD-----VQSFLLIMDLKLAPGPVLIH 95

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1819252707 131 CKGGLGRAGMIAARLLAELGVAPEQAIRDVRR 162
Cdd:cd14529    96 CKHGKDRTGLVSALYRIVYGGSKEEANEDYRL 127
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 83-168 2.53e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 49.16  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  83 EVRRRGIAWQHLPIPDFGVPGEHFERQWVQAgaeIRALLRAGDDVLVHCKGGLGRAGMIAARLLAELGVAPEQAIRDVRR 162
Cdd:PTZ00393  132 EITSAGINVHELIFPDGDAPTVDIVSNWLTI---VNNVIKNNRAVAVHCVAGLGRAPVLASIVLIEFGMDPIDAIVFIRD 208


                  ....*.
gi 1819252707 163 ARHGAI 168
Cdd:PTZ00393  209 RRKGAI 214
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 84-182 3.33e-07

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


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 47.76  E-value: 3.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  84 VRRRGIAWQHLPIPDFGVPGEHFERQWVQAgAEIRALLRAGDDVLVHCKGGLGRAGMIAARLLAELGVAPEQAIRDVRRA 163
Cdd:cd18537    58 VEKEGIQVLDWPFDDGAPPSNQIVDDWLNL-LKVKFREEPGCCIAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQK 136

                          90
                  ....*....|....*....
gi 1819252707 164 RHGAIETpAQMMLVQRTRP 182
Cdd:cd18537   137 RRGAFNS-KQLLYLEKYRP 154
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
72-173 9.46e-07

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 47.24  E-value: 9.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  72 LSALKVPQLGHEVRRRGIAWQHLPIPDFGVPGEHfeRQWVQAGAEIRALLRAGDD--VLVHCKGGLGRAG------MIAA 143
Cdd:pfam00102 117 VRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESP--NSLLDLLRKVRKSSLDGRSgpIVVHCSAGIGRTGtfiaidIALQ 194

                          90       100       110
                  ....*....|....*....|....*....|
gi 1819252707 144 RLLAELGVAPEQAIRDVRRARHGAIETPAQ 173
Cdd:pfam00102 195 QLEAEGEVDIFQIVKELRSQRPGMVQTLEQ 224
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 97-173 1.95e-06

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


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 46.12  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  97 PDFGVP--GEHFERQWvqagAEIRALLRAGDD-VLVHCKGGLGRAGMIAA------RLLAELGVAPEQAIRDVRRARHGA 167
Cdd:cd00047   113 PDHGVPssPEDLLALV----RRVRKEARKPNGpIVVHCSAGVGRTGTFIAidilleRLEAEGEVDVFEIVKALRKQRPGM 188


                  ....*.
gi 1819252707 168 IETPAQ 173
Cdd:cd00047   189 VQTLEQ 194
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 92-177 3.09e-06

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 45.71  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  92 QHLPIPDFGVPGEhfERQWVQAGAEIRALlRAGDD--VLVHCKGGLGRAG----MIAARLLAELG--VAPEQAIRDVRRA 163
Cdd:cd14601   112 QYIAWPDHGVPDD--SSDFLDFVCLVRNK-RAGKDepVVVHCSAGIGRTGvlitMETAMCLIECNqpVYPLDIVRTMRDQ 188

                          90
                  ....*....|....
gi 1819252707 164 RHGAIETPAQMMLV 177
Cdd:cd14601   189 RAMMIQTPSQYRFV 202
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 127-179 4.13e-06

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 45.11  E-value: 4.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819252707 127 VLVHCKGGLGRAGMIAA----RLLAELGVAPE-----QAIRDVRRARHGAIETPAQMMLVQR 179
Cdd:cd14542   141 ICVHCSAGCGRTGTICAidyvWNLLKTGKIPEefslfDLVREMRKQRPAMVQTKEQYELVYR 202
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 85-173 5.46e-06

unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily is composed of uncharacterized bacterial and plant dual-specificity protein phosphatases. DUSPs function as a protein-serine/threonine phosphatases (EC 3.1.3.16) and a protein-tyrosine-phosphatases (EC 3.1.3.48).


Pssm-ID: 350376 [Multi-domain]  Cd Length: 136  Bit Score: 43.80  E-value: 5.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  85 RRRGIAWQHLPIPDFGVPGEHferQWVQAGAEIRALLRAGDDVLVHCKGGLGRAGMIAARLLAELGVAP--EQAIRDVRR 162
Cdd:cd14527    40 PRKRQAYRCVPLLDLVAPTPE---QLERAVAWIEELRAQGGPVLVHCALGYGRSATVVAAWLLAYGRAKsvAEAEALIRA 116

                          90
                  ....*....|.
gi 1819252707 163 ARHGAIETPAQ 173
Cdd:cd14527   117 ARPQVVLNPAQ 127
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 85-138 1.13e-05

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.


Pssm-ID: 350375 [Multi-domain]  Cd Length: 146  Bit Score: 43.34  E-value: 1.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1819252707  85 RRRGIAWQHLPIPDFGvpGEHFERQWVQAGAEIRALLRAGDDVLVHCKGGLGRA 138
Cdd:cd14526    57 KESGIRYVRLPIRDFD--TEDLRQKLPQAVALLYRLLKNGGTVYVHCTAGLGRA 108
PRK12361 PRK12361
hypothetical protein; Provisional
 51-167 2.22e-05

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 43.84  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  51 DLDTIAAWGAKLVLTLVepAELSALKVPQLGHEvrrrgIAWQHLPIPDFGVPGEHferQWVQAGAEIRALLRAGDDVLVH 130
Cdd:PRK12361  112 DLEKLKSNKITAILDVT--AEFDGLDWSLTEED-----IDYLNIPILDHSVPTLA---QLNQAINWIHRQVRANKSVVVH 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1819252707 131 CKGGLGRAGMI-AARLLA---ELGVapEQAIRDVRRARHGA 167
Cdd:PRK12361  182 CALGRGRSVLVlAAYLLCkdpDLTV--EEVLQQIKQIRKTA 220
PTP-bact cd14503
bacterial tyrosine-protein phosphataseS similar to Neisseria NMA1982; This subfamily is ...
 50-163 2.96e-05

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.


Pssm-ID: 350353 [Multi-domain]  Cd Length: 136  Bit Score: 41.85  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  50 MDLDTIAAWGAKLVLTLVEPAELSALkvPQLGHEVRRRGIAWQHLPIpDFGVPG-EHFERQwvqagaeiRALLRA--GDD 126
Cdd:cd14503    18 EQFAALAAAGFKTVINLRPDGEENAL--PNEAAAVTAAGMEYVHIPV-DWDNPTpEDVERF--------FEVMDAaqGKP 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1819252707 127 VLVHCKGGlGRAGMIAA-RLLAELGVAPEQAIRDVRRA 163
Cdd:cd14503    87 VLVHCASN-MRASAFWYlYRALDGGVSEEEAIQLMRSA 123
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 51-159 4.75e-05

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 42.23  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  51 DLDTIAAWGAKLVLTLVEPAELSAlkvpqlghEVRRRGIAWQHLPIPDFGVPGEHFE------------------RQWVQ 112
Cdd:pfam13350  41 DLATLADLGIRTVIDLRSPAERAA--------PGPAPDVRYVHLPVADSEASSPELLarraldpddgeefmaelyRDMVT 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1819252707 113 -AGAEIRALLRA----GDDVLVHCKGGLGRAGMIAARLLAELGVAPEQAIRD 159
Cdd:pfam13350 113 sARAAYRALFEAladnDGPVLFHCTAGKDRTGVAAALLLSLLGVPEDTIVAD 164
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
93-164 4.93e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 41.50  E-value: 4.93e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819252707   93 HLPIPDFgvPGEHFERQWVQAGAEIRALLRAGDDVLVHCKGGLGR-AGMIAARLLAELGVAPEQAIRDVRRAR 164
Cdd:smart00195  49 GVPIDDN--TETKISPYFPEAVEFIEDAESKGGKVLVHCQAGVSRsATLIIAYLMKTRNMSLNDAYDFVKDRR 119
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 86-178 7.41e-05

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 41.28  E-value: 7.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  86 RRGIawQH--LPIPDFGVPGEHFERQWVQAgAEirallRAGDDVLVHCKGGLGRAG-MIAARLLAELGVAPEQAIRDVRR 162
Cdd:cd14499    77 DAGI--RHydLYFPDGSTPSDDIVKKFLDI-CE-----NEKGAIAVHCKAGLGRTGtLIACYLMKHYGFTAREAIAWLRI 148

                          90
                  ....*....|....*.
gi 1819252707 163 ARHGAIETPAQMMLVQ 178
Cdd:cd14499   149 CRPGSVIGPQQQFLEE 164
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 89-174 8.24e-05

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 41.61  E-value: 8.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  89 IAWqhlpiPDFGVPGE-----HFERQWVQAGAeiraLLRAGDDVLVHCKGGLGRAG----------MIAARLLAELGVap 153
Cdd:cd14545   137 TTW-----PDFGVPESpaaflNFLQKVRESGS----LSSDVGPPVVHCSAGIGRSGtfclvdtclvLIEKGNPSSVDV-- 205

                          90       100
                  ....*....|....*....|.
gi 1819252707 154 EQAIRDVRRARHGAIETPAQM 174
Cdd:cd14545   206 KKVLLEMRKYRMGLIQTPDQL 226
COG3453 COG3453
Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family ...
 51-163 8.92e-05

Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family [General function prediction only];


Pssm-ID: 442676 [Multi-domain]  Cd Length: 125  Bit Score: 40.20  E-value: 8.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  51 DLDTIAAWGAKLVLTLVEPAE-LSALKVPQLGHEVRRRGIAWQHLPIPDFGVPGEHFERQwvqagaeIRALLRAGDDVLV 129
Cdd:COG3453    18 DLAALAAAGFKTVINLRPDGEePDQPAAADEAAAAEAAGLEYVHIPVTGGAITDEDVEAF-------AAALAAAPGPVLA 90

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1819252707 130 HCKGGLgRAGMIAARLLA-ELGVAPEQAIRDVRRA 163
Cdd:COG3453    91 HCRSGT-RSSALWALYQAgKGGMSPEEALAAAAAA 124
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
51-159 1.06e-04

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


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 41.48  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  51 DLDTIAAWGAKLVLTLVEPAELSALKVPQLGhevrrrGIAWQHLPIPDF----------------GVPGEHFERQWVQ-- 112
Cdd:COG2365    40 DLARLADLGIRTVIDLRSPAEVARAPDRLPP------GVRYVHLPVLPDdaealleelrdgdltpGDAEEFMLELYRAfv 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1819252707 113 ---AGAEIRALLRA---GDD--VLVHCKGGLGRAGMIAARLLAELGVAPEQAIRD 159
Cdd:COG2365   114 dpdAADAYRAAFRAladAENgpVLFHCTAGKDRTGVAAALLLLALGVPRETIMAD 168
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
97-173 1.08e-04

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 41.49  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707   97 PDFGVPgEHFErqwvqagaEIRALLRAGDD--------VLVHCKGGLGRAG------MIAARLLAELGVAPEQAIRDVRR 162
Cdd:smart00194 168 PDHGVP-ESPE--------SILDLIRAVRKsqststgpIVVHCSAGVGRTGtfiaidILLQQLEAGKEVDIFEIVKELRS 238

                           90
                   ....*....|.
gi 1819252707  163 ARHGAIETPAQ 173
Cdd:smart00194 239 QRPGMVQTEEQ 249
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 85-173 1.28e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 41.20  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  85 RRRGIAWQHLPIPDFGVPGE-----HFERQWVQAGAeiRALLRAGDD---------VLVHCKGGLGRAGM-----IAARL 145
Cdd:cd14543   159 SRQVTHFQFTSWPDFGVPSSaaallDFLGEVRQQQA--LAVKAMGDRwkghppgppIVVHCSAGIGRTGTfctldICLSQ 236

                          90       100
                  ....*....|....*....|....*....
gi 1819252707 146 LAELGVAP-EQAIRDVRRARHGAIETPAQ 173
Cdd:cd14543   237 LEDVGTLNvMQTVRRMRTQRAFSIQTPDQ 265
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 127-179 1.85e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 41.07  E-value: 1.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819252707 127 VLVHCKGGLGRAGMIAA-----RLLaELGVAPE-----QAIRDVRRARHGAIETPAQMMLVQR 179
Cdd:cd14604   226 ICIHCSAGCGRTGAICAidytwNLL-KAGKIPEefnvfNLIQEMRTQRHSAVQTKEQYELVHR 287
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 89-177 2.40e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 40.39  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  89 IAWqhlpiPDFGVPGEhfERQWVQAGAEIRALlRAG--DDVLVHCKGGLGRAG----MIAARLLAE--LGVAPEQAIRDV 160
Cdd:cd14541   114 LAW-----PDHGVPDD--SSDFLDFVKRVRQN-RVGmvEPTVVHCSAGIGRTGvlitMETAMCLIEanEPVYPLDIVRTM 185

                          90
                  ....*....|....*..
gi 1819252707 161 RRARHGAIETPAQMMLV 177
Cdd:cd14541   186 RDQRAMLIQTPSQYRFV 202
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 72-178 2.55e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 40.39  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  72 LSALKVPQLGHEVRRRGIaWQ-HLPI-PDFGVPGE-----HFERQwVQAGAEirALLRAGDdVLVHCKGGLGRAGM---- 140
Cdd:cd14605   127 LRELKLSKVGQGNTERTV-WQyHFRTwPDHGVPSDpggvlDFLEE-VHHKQE--SIMDAGP-VVVHCSAGIGRTGTfivi 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1819252707 141 -IAARLLAELGVAPE----QAIRDVRRARHGAIETPAQ----MMLVQ 178
Cdd:cd14605   202 dILIDIIREKGVDCDidvpKTIQMVRSQRSGMVQTEAQyrfiYMAVQ 248
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 91-173 2.72e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 40.25  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  91 WQHLPIPDFGVPGE-----HFERQWVQAGAEIRallRAGDdVLVHCKGGLGRAG-MIAARLLAEL--------GVAPEQA 156
Cdd:cd14606   160 YQYLSWPDHGVPSEpggvlSFLDQINQRQESLP---HAGP-IIVHCSAGIGRTGtIIVIDMLMENistkgldcDIDIQKT 235

                          90
                  ....*....|....*..
gi 1819252707 157 IRDVRRARHGAIETPAQ 173
Cdd:cd14606   236 IQMVRAQRSGMVQTEAQ 252
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 92-177 4.14e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 39.83  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  92 QHLPIPDFGVPGEhfERQWVQAGAEIRALLRAGDDVLVHCKGGLGRAG----MIAARLLAE--LGVAPEQAIRDVRRARH 165
Cdd:cd14600   175 QYVAWPDHGVPDD--SSDFLEFVNYVRSKRVENEPVLVHCSAGIGRTGvlvtMETAMCLTErnQPVYPLDIVRKMRDQRA 252

                          90
                  ....*....|..
gi 1819252707 166 GAIETPAQMMLV 177
Cdd:cd14600   253 MMVQTSSQYKFV 264
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 93-164 5.15e-04

dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase.


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 38.30  E-value: 5.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819252707  93 HLPIPDFgvPGE----HFErqwvQAGAEIRALLRAGDDVLVHCKGGLGR-AGMIAARLLAELGVAPEQAIRDVRRAR 164
Cdd:cd14498    50 RIPIEDS--PDEdilsHFE----EAIEFIEEALKKGGKVLVHCQAGVSRsATIVIAYLMKKYGWSLEEALELVKSRR 120
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
 72-167 6.06e-04

dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; This family is composed of Saccharomyces cerevisiae dual specificity protein phosphatase Yvh1 and similar fungal proteins. Yvh1 could function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It regulates cell growth, sporulation, and glycogen accumulation. It plays an important role in ribosome assembly. Yvh1 associates transiently with late pre-60S particles and is required for the release of the nucleolar/nuclear pre-60S factor Mrt4, which is necessary to construct a translation-competent 60S subunit and mature ribosome stalk. Yvh1 contains an N-terminal catalytic dual specificity phosphatase domain and a C-terminal tail.


Pssm-ID: 350368 [Multi-domain]  Cd Length: 153  Bit Score: 38.45  E-value: 6.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  72 LSALKVPQlgHEVRRRGIAWQHLPIPDfgVPGE----HFER--QWVQAG-----AEIRALLRAGDDVLVHCKGGLGR-AG 139
Cdd:cd14518    31 LSVIPGDV--PEEYFKGYEHKQIEIDD--VEDEnilqHFPEtnRFIDSAlfgngKDEDEEKKHGGAVLVHCAMGKSRsVT 106

                          90       100
                  ....*....|....*....|....*...
gi 1819252707 140 MIAARLLAELGVAPEQAIRDVRRARHGA 167
Cdd:cd14518   107 VVIAYLMYKYNLSVSQALHAVRRKRPIA 134
DUSP28 cd14574
dual specificity protein phosphatase 28; Dual specificity protein phosphatase 28 (DUSP28), ...
 94-167 8.98e-04

dual specificity protein phosphatase 28; Dual specificity protein phosphatase 28 (DUSP28), also called VHP, 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 that 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 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells. DUSP28 has an exceptionally low phosphatase activity due to the presence of bulky residues in the active site pocket resulting in low accessibility.


Pssm-ID: 350422 [Multi-domain]  Cd Length: 140  Bit Score: 37.83  E-value: 8.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819252707  94 LPIPDFGVPGEHFERQWVQAGAEIRALLRAGDDVLVHCKGGLGR-AGMIAARLLAELGVAPEQAIRDVRRARHGA 167
Cdd:cd14574    48 LRVPVFDDPAEDLYRHFEQCADAIEAAVRRGGKCLVYCKNGRSRsAAVCIAYLMKHRGLSLQDAFQVVKAARPVA 122
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 97-173 1.56e-03

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.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 37.80  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  97 PDFGVPgeHFERQWVQAGAEIRALLRAGDdVLVHCKGGLGRAG------MIAARLLAELGVAPEQAIRDVRRARHGAIET 170
Cdd:cd14596   115 PDHGTP--QSSDQLVKFICYMRKVHNTGP-IVVHCSAGIGRAGvlicvdVLLSLIEKDLSFNIKDIVREMRQQRYGMIQT 191


                  ...
gi 1819252707 171 PAQ 173
Cdd:cd14596   192 KDQ 194
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
 110-164 1.56e-03

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


Pssm-ID: 350419 [Multi-domain]  Cd Length: 144  Bit Score: 37.15  E-value: 1.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1819252707 110 WVQAGAEIRALLRAGDDVLVHCKGGLGR-AGMIAARLLAELGVAPEQAIRDVRRAR 164
Cdd:cd14571    67 WKETHRFIEAARAQGTRVLVHCKMGVSRsASTVIAYAMKQYGWTLEQALRHVRERR 122
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 97-174 3.22e-03

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 37.25  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  97 PDFGVPGEHFE-RQWVQAGAEIRALLRAGDDVLVHCKGGLGRAGMIA----ARLLAE----LGVAPEQAIRDVRRARHGA 167
Cdd:cd14607   164 PDFGVPESPASfLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSlvdtCLVLMEkkdpDSVDIKQVLLDMRKYRMGL 243


                  ....*..
gi 1819252707 168 IETPAQM 174
Cdd:cd14607   244 IQTPDQL 250
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 93-164 5.28e-03

dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class III MKPs consist of DUSP8, DUSP10/MKP-5 and DUSP16/MKP-7, and are JNK/p38-selective phosphatases, which are found in both the cell nucleus and cytoplasm. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350416 [Multi-domain]  Cd Length: 140  Bit Score: 35.47  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  93 HLPIPDFgVPGEHFER------------QWVQAGAE-IRALLRAGDDVLVHCKGGLGRAGMIA-ARLLAELGVAPEQAIR 158
Cdd:cd14568    36 TCPKPDF-IPDSHFLRipvndsycekllPWLDKAVEfIEKARASNKRVLVHCLAGISRSATIAiAYIMKHMRMSLDDAYR 114


                  ....*.
gi 1819252707 159 DVRRAR 164
Cdd:cd14568   115 FVKEKR 120
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 88-164 5.56e-03

dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is composed of dual specificity protein phosphatase 3 (DUSP3, also known as VHR), 13B (DUSP13B, also known as TMDP), 26 (DUSP26, also known as MPK8), 13A (DUSP13A, also known as MDSP), dual specificity phosphatase and pro isomerase domain containing 1 (DUPD1), and inactive DUSP27. In general, DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Members of this family are atypical DUSPs; they contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Inactive DUSP27 contains a dual specificity phosphatase-like domain with the active site cysteine substituted to serine.


Pssm-ID: 350365 [Multi-domain]  Cd Length: 148  Bit Score: 35.65  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  88 GIAWQHLPIPDFGVP--GEHFErqwvQAGAEI-RALLRAGDDVLVHCKGGLGR-AGMIAARLLAELGVAPEQAIRDVRRA 163
Cdd:cd14515    53 GIIYLGIPASDLPTFdiSQYFD----EAADFIdKALSDPGGKVLVHCVEGVSRsATLVLAYLMIYQNMTLEEAIRTVRKK 128


                  .
gi 1819252707 164 R 164
Cdd:cd14515   129 R 129
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 96-174 6.00e-03

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 35.32  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  96 IPDFGVPGEHF----ERQWVQAGAE-IRALLRAGDDVLVHCKGGLGRAG-MIAARLLAELGVAPEQAIRDVRRARHGAIE 169
Cdd:pfam00782  36 ILYLRIPVEDNhetnISKYLEEAVEfIDDARQKGGKVLVHCQAGISRSAtLIIAYLMKTRNLSLNEAYSFVKERRPGISP 115


                  ....*
gi 1819252707 170 TPAQM 174
Cdd:pfam00782 116 NFGFK 120
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 97-180 6.19e-03

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).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 36.35  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  97 PDFGVP--GEHF-------ERQWVQAGAEirallragDDVLVHCKGGLGRAGMIAA------RLLAELGVAPEQAIRDVR 161
Cdd:cd14554   146 PEQGVPksGEGFidfigqvHKTKEQFGQE--------GPITVHCSAGVGRTGVFITlsivleRMRYEGVVDVFQTVKLLR 217

                          90
                  ....*....|....*....
gi 1819252707 162 RARHGAIETPAQMMLVQRT 180
Cdd:cd14554   218 TQRPAMVQTEDQYQFCYRA 236
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 95-173 6.41e-03

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


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 35.80  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  95 PIPDFGVPGEHferQWVQAGAEIRALLRAGDD--VLVHCKGGLGRAG-MIAARLLA-ELGVAPEQAIR--DVRRARHGA- 167
Cdd:cd14510    80 PIDDHNVPTLD---EMLSFTAEVREWMAADPKnvVAIHCKGGKGRTGtMVCAWLIYsGQFESAKEALEyfGERRTDKSVs 156

                          90
                  ....*....|.
gi 1819252707 168 -----IETPAQ 173
Cdd:cd14510   157 skfqgVETPSQ 167
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 129-169 6.50e-03

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


Pssm-ID: 350503  Cd Length: 169  Bit Score: 35.72  E-value: 6.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1819252707 129 VHCKGGLGRAG-MIAARLLAELGVAPEQAIRDVRRARHGAIE 169
Cdd:cd17665   118 VHCTHGLNRTGyLICRYLIDVDGMSPDDAIEAFEQARGHPIE 159
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 95-164 9.23e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual specificity protein phosphatase 16 (DUSP16), also called mitogen-activated protein kinase (MAPK) phosphatase 7 (MKP-7), 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. DUSP16/MKP-7 plays an essential role in perinatal survival and selectively controls the differentiation and cytokine production of myeloid cells. It is acetylated by Mycobacterium tuberculosis Eis protein, which leads to the inhibition of JNK-dependent autophagy, phagosome maturation, and ROS generation, and thus, initiating suppression of host immune responses. DUSP16/MKP-7 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350494 [Multi-domain]  Cd Length: 145  Bit Score: 35.00  E-value: 9.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819252707  95 PIPDFgVPGEHFER------------QWVQAGAEIRALLRAGDD-VLVHCKGGLGRAGMIA-ARLLAELGVAPEQAIRDV 160
Cdd:cd14646    40 PKPDF-IPESHFLRvpvndsfcekilPWLDKSVDFIEKAKASNGrVLVHCLAGISRSATIAiAYIMKRMDMSLDEAYRFV 118


                  ....
gi 1819252707 161 RRAR 164
Cdd:cd14646   119 KEKR 122
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 110-164 9.31e-03

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


Pssm-ID: 350363 [Multi-domain]  Cd Length: 139  Bit Score: 35.06  E-value: 9.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1819252707 110 WVQAGAEIRALLRAGDDVLVHCKGGLGR-AGMIAARLLAELGVAPEQAIRDVRRAR 164
Cdd:cd14513    64 WNETYRFIKEARRKGSKVLVHCKMGVSRsASTVIAYAMKEYGWSLEQALEHVKERR 119
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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