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Conserved domains on  [gi|568988872|ref|XP_006519656|]
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cyclin-dependent kinase inhibitor 3 isoform X2 [Mus musculus]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 17-154 8.62e-102

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.


The actual alignment was detected with superfamily member pfam05706:

Pssm-ID: 475123  Cd Length: 168  Bit Score: 290.77  E-value: 8.62e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872   17 WLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPD 96
Cdd:pfam05706  31 WLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPIAD 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568988872   97 GGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPQQAI 154
Cdd:pfam05706 111 GGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPEQAI 168
 
Name Accession Description Interval E-value
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 17-154 8.62e-102

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: 290.77  E-value: 8.62e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872   17 WLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPD 96
Cdd:pfam05706  31 WLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPIAD 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568988872   97 GGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPQQAI 154
Cdd:pfam05706 111 GGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPEQAI 168
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 16-177 1.01e-84

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: 247.56  E-value: 1.01e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  16 QWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIP 95
Cdd:cd14505    2 DWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPIP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  96 DGGTPD-IGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPQQAIDSLRDVRGsGAIQTIKQYNY 174
Cdd:cd14505   82 DGGVPSdIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTLDPEQAIAAVRALRP-GAIQTPKQENF 160


                 ...
gi 568988872 175 LHE 177
Cdd:cd14505  161 LHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
48-182 3.91e-27

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 100.05  E-value: 3.91e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  48 KDTEELKSYGIQDVFVFCTRGELskyrvpnLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCY 127
Cdd:COG2453   16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLVHCR 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568988872 128 GGLGRSCLVAACLLLYLsdSISPQQAIDSLRDVRgSGAIQTIKQYNYLHEFRDKL 182
Cdd:COG2453   89 GGIGRTGTVAAAYLVLL--GLSAEEALARVRAAR-PGAVETPAQRAFLERFAKRL 140
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 51-181 1.46e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 55.71  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  51 EELKSYGIQDVFVFCTR----GELskyrvpnlldlyQQYGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKTLI 124
Cdd:PTZ00393 110 KEMKNYNVTDLVRTCERtyndGEI------------TSAGINVHELIFPDGDAPtvDIVSNW--LTIVNNVIKNNRAVAV 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568988872 125 HCYGGLGRSCLVAACLLLYLsdSISPQQAIDSLRDvRGSGAIQTiKQYNYLHEFRDK 181
Cdd:PTZ00393 176 HCVAGLGRAPVLASIVLIEF--GMDPIDAIVFIRD-RRKGAINK-RQLQFLKAYKKK 228
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
90-177 3.88e-09

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 51.98  E-value: 3.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872    90 HHHPIPDGGTPDigSCWEIMEELATCLKNNRK------TLIHCYGGLGRSC-LVAACLLLYL----SDSISPQQAIDSLR 158
Cdd:smart00404   6 HYTGWPDHGVPE--SPDSILELLRAVKKNLNQsessgpVVVHCSAGVGRTGtFVAIDILLQQleaeAGEVDIFDTVKELR 83

                           90
                   ....*....|....*....
gi 568988872   159 DVRgSGAIQTIKQYNYLHE 177
Cdd:smart00404  84 SQR-PGMVQTEEQYLFLYR 101
 
Name Accession Description Interval E-value
CDKN3 pfam05706
Cyclin-dependent kinase inhibitor 3 (CDKN3); This family consists of cyclin-dependent kinase ...
 17-154 8.62e-102

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: 290.77  E-value: 8.62e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872   17 WLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPD 96
Cdd:pfam05706  31 WLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPIAD 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568988872   97 GGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPQQAI 154
Cdd:pfam05706 111 GGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPEQAI 168
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 16-177 1.01e-84

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: 247.56  E-value: 1.01e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  16 QWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIP 95
Cdd:cd14505    2 DWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPIP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  96 DGGTPD-IGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPQQAIDSLRDVRGsGAIQTIKQYNY 174
Cdd:cd14505   82 DGGVPSdIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDTLDPEQAIAAVRALRP-GAIQTPKQENF 160


                 ...
gi 568988872 175 LHE 177
Cdd:cd14505  161 LHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
48-182 3.91e-27

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 100.05  E-value: 3.91e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  48 KDTEELKSYGIQDVFVFCTRGELskyrvpnLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCY 127
Cdd:COG2453   16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLVHCR 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568988872 128 GGLGRSCLVAACLLLYLsdSISPQQAIDSLRDVRgSGAIQTIKQYNYLHEFRDKL 182
Cdd:COG2453   89 GGIGRTGTVAAAYLVLL--GLSAEEALARVRAAR-PGAVETPAQRAFLERFAKRL 140
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 27-177 3.92e-16

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: 70.84  E-value: 3.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  27 QFLGLCALPGCkfkdvrrNIQKDTEELKSYGIQDVFVFCtrgelskyrvpnLLDLYqqygivthhhpipdggtpdigscw 106
Cdd:cd14494    7 LRLIAGALPLS-------PLEADSRFLKQLGVTTIVDLT------------LAMVD------------------------ 43

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568988872 107 EIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSDsISPQQAIDSLRDVRGSGAIQTIKQYNYLHE 177
Cdd:cd14494   44 RFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGG-MSAEEAVRIVRLIRPGGIPQTIEQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 73-178 1.92e-14

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: 67.30  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  73 YRVPNLlDLYQQYGIVTHHHPIPDGGTP---DIGSCWEIMEElatCLKNNRKTLIHCYGGLGRSCLVAACLLLYlSDSIS 149
Cdd:cd14504   37 EEPPPE-HSDTCPGLRYHHIPIEDYTPPtleQIDEFLDIVEE---ANAKNEAVLVHCLAGKGRTGTMLACYLVK-TGKIS 111

                         90       100
                 ....*....|....*....|....*....
gi 568988872 150 PQQAIDSLRDVRGsGAIQTIKQYNYLHEF 178
Cdd:cd14504  112 AVDAINEIRRIRP-GSIETSEQEKFVIQF 139
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 51-178 5.95e-14

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: 67.37  E-value: 5.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  51 EELKSYGIQDVF--------VFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKT 122
Cdd:cd14506   33 EQFKEKGIKTVInlqepgehASCGPGLEPESGFSYLPEAFMRAGIYFYNFGWKDYGVPSLTTILDIVKVMAFALQEGGKV 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568988872 123 LIHCYGGLGRSCLVAACLLLYLSDsISPQQAIDSLRDVRgSGAIQTIKQYNYLHEF 178
Cdd:cd14506  113 AVHCHAGLGRTGVLIACYLVYALR-MSADQAIRLVRSKR-PNSIQTRGQVLCVREF 166
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 45-181 1.26e-09

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: 54.53  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  45 NIQKDTEELKSYGIQDVFVFCTRgelsKYRVPNLLDLyqqyGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKT 122
Cdd:cd14500   25 NLPLYIKELKKYNVTDLVRVCEP----TYDKEPLEKA----GIKVHDWPFDDGSPPpdDVVDDW--LDLLKTRFKEEGKP 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568988872 123 L----IHCYGGLGRS-CLVAACLLLYlsdSISPQQAIDSLRDVRgSGAIqTIKQYNYLHEFRDK 181
Cdd:cd14500   95 GaciaVHCVAGLGRApVLVAIALIEL---GMKPEDAVEFIRKKR-RGAI-NSKQLQFLEKYKPK 153
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 51-181 1.46e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 55.71  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  51 EELKSYGIQDVFVFCTR----GELskyrvpnlldlyQQYGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKTLI 124
Cdd:PTZ00393 110 KEMKNYNVTDLVRTCERtyndGEI------------TSAGINVHELIFPDGDAPtvDIVSNW--LTIVNNVIKNNRAVAV 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568988872 125 HCYGGLGRSCLVAACLLLYLsdSISPQQAIDSLRDvRGSGAIQTiKQYNYLHEFRDK 181
Cdd:PTZ00393 176 HCVAGLGRAPVLASIVLIEF--GMDPIDAIVFIRD-RRKGAINK-RQLQFLKAYKKK 228
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
90-177 3.88e-09

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 51.98  E-value: 3.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872    90 HHHPIPDGGTPDigSCWEIMEELATCLKNNRK------TLIHCYGGLGRSC-LVAACLLLYL----SDSISPQQAIDSLR 158
Cdd:smart00404   6 HYTGWPDHGVPE--SPDSILELLRAVKKNLNQsessgpVVVHCSAGVGRTGtFVAIDILLQQleaeAGEVDIFDTVKELR 83

                           90
                   ....*....|....*....
gi 568988872   159 DVRgSGAIQTIKQYNYLHE 177
Cdd:smart00404  84 SQR-PGMVQTEEQYLFLYR 101
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 90-177 3.88e-09

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: 51.98  E-value: 3.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872    90 HHHPIPDGGTPDigSCWEIMEELATCLKNNRK------TLIHCYGGLGRSC-LVAACLLLYL----SDSISPQQAIDSLR 158
Cdd:smart00012   6 HYTGWPDHGVPE--SPDSILELLRAVKKNLNQsessgpVVVHCSAGVGRTGtFVAIDILLQQleaeAGEVDIFDTVKELR 83

                           90
                   ....*....|....*....
gi 568988872   159 DVRgSGAIQTIKQYNYLHE 177
Cdd:smart00012  84 SQR-PGMVQTEEQYLFLYR 101
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 48-161 5.28e-08

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: 49.85  E-value: 5.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  48 KDTEELKSYGIQdvFVFCTRGELSKYRVPNlldlyqqyGIVTHHHPIPDGGTPDIGS----CWEIMEElatCLKNNRKTL 123
Cdd:cd14498   17 QDKELLKKLGIT--HILNVAGEPPPNKFPD--------GIKYLRIPIEDSPDEDILShfeeAIEFIEE---ALKKGGKVL 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568988872 124 IHCYGGLGRSC-LVAACLLLYLsdSISPQQAIDSLRDVR 161
Cdd:cd14498   84 VHCQAGVSRSAtIVIAYLMKKY--GWSLEEALELVKSRR 120
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
87-177 6.20e-08

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 51.12  E-value: 6.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872    87 IVTHHHPI--PDGGTP-DIGSCWEIMEELATCLKNNRK-TLIHCYGGLGRS-CLVAACLLLYL---SDSISPQQAIDSLR 158
Cdd:smart00194 158 TVTHYHYTnwPDHGVPeSPESILDLIRAVRKSQSTSTGpIVVHCSAGVGRTgTFIAIDILLQQleaGKEVDIFEIVKELR 237

                           90
                   ....*....|....*....
gi 568988872   159 DVRgSGAIQTIKQYNYLHE 177
Cdd:smart00194 238 SQR-PGMVQTEEQYIFLYR 255
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 87-177 5.21e-07

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: 48.05  E-value: 5.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  87 IVTHHHPI--PDGGTPDIGScwEIMEELA----TCLKNNRKTLIHCYGGLGRS----CLVAACLLLYLSDSISPQQAIDS 156
Cdd:cd00047  103 EVTHLHYTgwPDHGVPSSPE--DLLALVRrvrkEARKPNGPIVVHCSAGVGRTgtfiAIDILLERLEAEGEVDVFEIVKA 180

                         90       100
                 ....*....|....*....|.
gi 568988872 157 LRDVRgSGAIQTIKQYNYLHE 177
Cdd:cd00047  181 LRKQR-PGMVQTLEQYEFIYE 200
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 69-179 5.71e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 47.32  E-value: 5.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  69 ELSKYRVPNLL---------DLYQQYGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKTL----IHCYGGLGRS 133
Cdd:PTZ00242  35 ELQRYNVTHLVrvcgptydaELLEKNGIEVHDWPFDDGAPPpkAVIDNW--LRLLDQEFAKQSTPPetiaVHCVAGLGRA 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568988872 134 -CLVAACLLLYlsDSISPQQAIDSLRDVRgSGAIQtIKQYNYLHEFR 179
Cdd:PTZ00242 113 pILVALALVEY--GGMEPLDAVGFVREKR-KGAIN-QTQLQFLKKYK 155
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 82-181 8.15e-07

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: 46.87  E-value: 8.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  82 YQQYGIVTHHHPIPD-GGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYlSDSISPQQAIDSLRDV 160
Cdd:cd14524   51 WKALGVEQLRLPTVDfTGVPSLEDLEKGVDFILKHREKGKSVYVHCKAGRGRSATIVACYLIQ-HKGWSPEEAQEFLRSK 129

                         90       100
                 ....*....|....*....|.
gi 568988872 161 RGSGAIQTiKQYNYLHEFRDK 181
Cdd:cd14524  130 RPHILLRL-SQREVLEEFYRK 149
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
88-177 2.71e-06

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 46.08  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872   88 VTHHHPI--PDGGTP-DIGSCWEIMEELATCLKNNRKT--LIHCYGGLGRS-CLVAACLLLYL---SDSISPQQAIDSLR 158
Cdd:pfam00102 133 VKHFHYTgwPDHGVPeSPNSLLDLLRKVRKSSLDGRSGpiVVHCSAGIGRTgTFIAIDIALQQleaEGEVDIFQIVKELR 212

                          90
                  ....*....|....*....
gi 568988872  159 DVRGsGAIQTIKQYNYLHE 177
Cdd:pfam00102 213 SQRP-GMVQTLEQYIFLYD 230
PRK12361 PRK12361
hypothetical protein; Provisional
 117-181 4.70e-06

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 46.15  E-value: 4.70e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568988872 117 KNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPQQAIDSLRDVRGSGAIQTiKQYNYLHEFRDK 181
Cdd:PRK12361 173 RANKSVVVHCALGRGRSVLVLAAYLLCKDPDLTVEEVLQQIKQIRKTARLNK-RQLRALEKMLEQ 236
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
99-163 1.44e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 43.04  E-value: 1.44e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568988872    99 TPDIGSCWEIMEElatCLKNNRKTLIHCYGGLGRSCLVAACLLLYlSDSISPQQAIDSLRDVRGS 163
Cdd:smart00195  61 SPYFPEAVEFIED---AESKGGKVLVHCQAGVSRSATLIIAYLMK-TRNMSLNDAYDFVKDRRPI 121
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 109-161 1.46e-05

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: 43.03  E-value: 1.46e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568988872 109 MEELAtclKNNRKTLIHCYGGLGRSCLVAACLLLYLSDSISPQQAIDSLRDVR 161
Cdd:cd14527   69 IEELR---AQGGPVLVHCALGYGRSATVVAAWLLAYGRAKSVAEAEALIRAAR 118
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 72-155 2.02e-05

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.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 42.95  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  72 KYRVPNL----LDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLK--NNRKTLIHCYGGLGRSCLVAACLLLYLS 145
Cdd:cd14497   42 HYMIFNLseeeYDDDSKFEGRVLHYGFPDHHPPPLGLLLEIVDDIDSWLSedPNNVAVVHCKAGKGRTGTVICAYLLYYG 121

                         90
                 ....*....|
gi 568988872 146 DSISPQQAID 155
Cdd:cd14497  122 QYSTADEALE 131
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 51-181 2.33e-05

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: 42.70  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  51 EELKSYGIQDVFVFCtrgELSKYRVPnlldlYQQYGIVTHHHPIPDGGTP--DIGSCWEIMEELATCLKNNRKTLIHCYG 128
Cdd:cd18535   31 EDLKKYGATTVVRVC---EVTYDKTP-----LEKDGITVVDWPFDDGAPPpgKVVEDWLSLLKTKFCEDPGCCVAVHCVA 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568988872 129 GLGRSCLVAACLLlyLSDSISPQQAIDSLRDVRgSGAIQTiKQYNYLHEFRDK 181
Cdd:cd18535  103 GLGRAPVLVALAL--IESGMKYEDAIQFIRQKR-RGAINS-KQLTYLEKYRPK 151
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 44-144 4.25e-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: 41.80  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  44 RNIQkDTEELKSYGIQDVFVFCTRGELSKYRV--PNLLDLYQQYGIVTHHHPIPDGGTPD----IGSCWEIMEELatcLK 117
Cdd:cd14526   17 QNPE-DVDRLKKEGVTAVLNLQTDSDMEYWGVdiDSIRKACKESGIRYVRLPIRDFDTEDlrqkLPQAVALLYRL---LK 92

                         90       100
                 ....*....|....*....|....*..
gi 568988872 118 NNRKTLIHCYGGLGRSCLVaACLLLYL 144
Cdd:cd14526   93 NGGTVYVHCTAGLGRAPAT-VIAYLYW 118
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 46-182 5.20e-05

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: 41.91  E-value: 5.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  46 IQKDTEELKSYGIQDVFVFCTrgelSKYRVPnlldLYQQYGIVTHHHPIPDGGTP--DIGSCW------EIMEELATCLK 117
Cdd:cd18536   27 LNKFTEELKKYGVTTLVRVCD----ATYDKA----PVEKEGIQVLDWPFDDGAPPpnQIVDDWlnllktKFREEPGCCVA 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568988872 118 nnrktlIHCYGGLGRSCLVAACLLLYLsdSISPQQAIDSLRDVRgSGAIQTiKQYNYLHEFRDKL 182
Cdd:cd18536   99 ------VHCVAGLGRAPVLVALALIEC--GMKYEDAVQFIRQKR-RGAFNS-KQLLYLEKYRPKM 153
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 95-176 5.21e-05

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 42.50  E-value: 5.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  95 PDGGTPDIGSCWEIMEELATCLKNNRKT--LIHCYGGLGRS---CLVAACLLLYLSDSISPQ----QAIDSLRDVRGSgA 165
Cdd:cd14603  170 PDHGIPDSPDCMLAMIELARRLQGSGPEplCVHCSAGCGRTgviCTVDYVRQLLLTQRIPPDfsifDVVLEMRKQRPA-A 248

                         90
                 ....*....|.
gi 568988872 166 IQTIKQYNYLH 176
Cdd:cd14603  249 VQTEEQYEFLY 259
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 47-185 7.26e-05

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: 41.21  E-value: 7.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  47 QKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLyqqyGIVTHHHPIPDGGTPDIGscwEIMEELATCLKNNRK-TLIH 125
Cdd:cd14529   23 DEDRALLKKLGIKTVIDLRGADERAASEEAAAKID----GVKYVNLPLSATRPTESD---VQSFLLIMDLKLAPGpVLIH 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568988872 126 CYGGLGRSCLVAA-CLLLYlsdSISPQQAIDSLRdvRGSGAIQTIKQYNYLHE----FRDKLAAY 185
Cdd:cd14529   96 CKHGKDRTGLVSAlYRIVY---GGSKEEANEDYR--LSNRHLEGLRSGIALDSkggvKGRYLAAY 155
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 40-177 9.63e-05

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.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 41.62  E-value: 9.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  40 KDVRRNIQKDTEELKSYGIQdvfvfcTRGELSKYRVPnlldlyqqygiVTHHHPIPDGGTpdIGScwEIMEELATCLKNN 119
Cdd:cd14559   89 KKTGKDELVDGLKADMYNLK------ITDGNKTITIP-----------VVHVTNWPDHTA--ISS--EGLKELADLVNKS 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872 120 RKT---------------------LIHCYGGLGRS-CLVAACLLLYLSDSISPQQAIDSLRDVRGSGAIQTIKQYNYLHE 177
Cdd:cd14559  148 AEEkrnfykskgssaindknkllpVIHCRAGVGRTgQLAAAMELNKSPNNLSVEDIVSDMRTSRNGKMVQKDEQLDTLKE 227
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 95-176 9.83e-05

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 41.75  E-value: 9.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  95 PDGGTPDigsCWEIMEELATCLKNNRKT-------LIHCYGGLGRS-CLVAA---CLLLYLSDSISPQQAIDSLRDVRGs 163
Cdd:cd14612  153 PDHQTPE---SAGPLLRLVAEVEESRQTaaspgpiVVHCSAGIGRTgCFIATsigCQQLKDTGKVDILGIVCQLRLDRG- 228

                         90
                 ....*....|...
gi 568988872 164 GAIQTIKQYNYLH 176
Cdd:cd14612  229 GMIQTSEQYQFLH 241
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 112-163 1.81e-04

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: 39.55  E-value: 1.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568988872  112 LATCLKNNRKTLIHCYGGLGRS-CLVAACLLLYLSDSISpqQAIDSLRDVRGS 163
Cdd:pfam00782  62 IDDARQKGGKVLVHCQAGISRSaTLIIAYLMKTRNLSLN--EAYSFVKERRPG 112
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 95-176 2.52e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 40.52  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  95 PDGGTP-DIGSCWEIMEEL---------ATCLKN-NRKTLIHCYGGLGRSCLVAAC-LLLYLSDS---ISPQQAIDSLRD 159
Cdd:cd14540  117 PDHGCPeDVSGFLDFLEEInsvrrhtnqDVAGHNrNPPTLVHCSAGVGRTGVVILAdLMLYCLDHneeLDIPRVLALLRH 196

                         90
                 ....*....|....*..
gi 568988872 160 VRGSgAIQTIKQYNYLH 176
Cdd:cd14540  197 QRML-LVQTLAQYKFVY 212
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 46-182 3.07e-04

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: 39.67  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  46 IQKDTEELKSYGIQDVFVFCTrgelSKYRVpnllDLYQQYGIVTHHHPIPDGGTPD--IGSCW------EIMEELATCLK 117
Cdd:cd18537   30 LNKFIEELKKYGVTTVVRVCE----ATYDT----TLVEKEGIQVLDWPFDDGAPPSnqIVDDWlnllkvKFREEPGCCIA 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568988872 118 nnrktlIHCYGGLGRSCLVAAclLLYLSDSISPQQAIDSLRDVRgSGAIQTiKQYNYLHEFRDKL 182
Cdd:cd18537  102 ------VHCVAGLGRAPVLVA--LALIECGMKYEDAVQFIRQKR-RGAFNS-KQLLYLEKYRPKM 156
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 95-176 6.20e-04

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 39.30  E-value: 6.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  95 PDGGTPDigsCWEIMEELATCLKNNRKT-------LIHCYGGLGRS-CLVAAclllylsdSISPQQ-----AIDSLRDV- 160
Cdd:cd14547  135 PDHKTPE---AAQPLLSLVQEVEEARQTephrgpiVVHCSAGIGRTgCFIAT--------SIGCQQlreegVVDVLGIVc 203

                         90       100
                 ....*....|....*....|.
gi 568988872 161 -----RGsGAIQTIKQYNYLH 176
Cdd:cd14547  204 qlrldRG-GMVQTAEQYEFVH 223
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 58-155 1.92e-03

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 37.18  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  58 IQDVFVFCTRGELSKYRVPNLLDLYQQ-----YGIVTHHhPIPDGGTPDIGSCWEIMEELATCLKNNRKTL--IHCYGGL 130
Cdd:cd14509   27 IDDVQRFLETKHKGHYKVYNLCSERSYdpskfNGRVAEY-PFDDHNPPPLELIKPFCEDVDEWLKEDEKNVaaVHCKAGK 105

                         90       100
                 ....*....|....*....|....*
gi 568988872 131 GRSCLVAACLLLYLSDSISPQQAID 155
Cdd:cd14509  106 GRTGVMICCYLLYLGKFPSAKEALD 130
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 88-176 1.99e-03

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 38.00  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  88 VTHHH--PIPDGGTPDIGSCW----EIMEELATCLKNNRKTLIHCYGGLGRSCLVAAclLLYLSDSISPQQAID------ 155
Cdd:cd14618  129 VKHLHytAWPDHGIPESTSSLmafrELVREHVQATKGKGPTLVHCSAGVGRSGTFIA--LDRLLRQLKEEKVVDvfntvy 206

                         90       100
                 ....*....|....*....|.
gi 568988872 156 SLRDVRGSgAIQTIKQYNYLH 176
Cdd:cd14618  207 ILRMHRYL-MIQTLSQYIFLH 226
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 95-176 2.32e-03

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 37.92  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988872  95 PDGGTPD-----IGSCWEIMEELATCLKNNRKTLIHCYGGLGRS-CLVAACLllyLSDSISPQQAIDSLRDV------RG 162
Cdd:cd14613  163 PDQKTPDnapplLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTgCFIATSI---CCKQLRNEGVVDILRTTcqlrldRG 239

                         90
                 ....*....|....
gi 568988872 163 sGAIQTIKQYNYLH 176
Cdd:cd14613  240 -GMIQTCEQYQFVH 252
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 122-177 7.46e-03

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: 36.15  E-value: 7.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568988872 122 TLIHCYGGLGRS-CLV----AACLLLYlSDSISPQQAIDSLRDVRGSgAIQTIKQYNYLHE 177
Cdd:cd14541  146 TVVHCSAGIGRTgVLItmetAMCLIEA-NEPVYPLDIVRTMRDQRAM-LIQTPSQYRFVCE 204
 
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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