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Conserved domains on  [gi|1720380882|ref|XP_030103904|]
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cyclin-dependent kinase inhibitor 3 isoform X3 [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 ...
 17-153 1.60e-90

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: 262.27  E-value: 1.60e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  17 WLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPD 96
Cdd:pfam05706  31 WLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPIAD 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720380882  97 GGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRS-CLAACLLLYLSDSISPQQAI 153
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 ...
 17-153 1.60e-90

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: 262.27  E-value: 1.60e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  17 WLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPD 96
Cdd:pfam05706  31 WLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPIAD 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720380882  97 GGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRS-CLAACLLLYLSDSISPQQAI 153
Cdd:pfam05706 111 GGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRScLVAACLLLYLSDSISPEQAI 168
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 16-176 9.05e-72

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: 214.43  E-value: 9.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  16 QWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIP 95
Cdd:cd14505     2 DWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  96 DGGTPD-IGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLAACLL-LYLSDSISPQQAIDSLRDVRGsGAIQTIKQYNY 173
Cdd:cd14505    82 DGGVPSdIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLlLELGDTLDPEQAIAAVRALRP-GAIQTPKQENF 160


                  ...
gi 1720380882 174 LHE 176
Cdd:cd14505   161 LHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
48-181 1.90e-18

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 77.70  E-value: 1.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  48 KDTEELKSYGIQDVFVFCTRGELskyrvpnLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCY 127
Cdd:COG2453    16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLVHCR 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720380882 128 GGLGRS---------ClaaclllylsDSISPQQAIDSLRDVRgSGAIQTIKQYNYLHEFRDKL 181
Cdd:COG2453    89 GGIGRTgtvaaaylvL----------LGLSAEEALARVRAAR-PGAVETPAQRAFLERFAKRL 140
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 51-180 1.44e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 47.24  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  51 EELKSYGIQDVFVFCTR----GELskyrvpnlldlyQQYGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKTLI 124
Cdd:PTZ00393  110 KEMKNYNVTDLVRTCERtyndGEI------------TSAGINVHELIFPDGDAPtvDIVSNW--LTIVNNVIKNNRAVAV 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720380882 125 HCYGGLGRSCLAACLLLYLSdSISPQQAIDSLRDvRGSGAIQTiKQYNYLHEFRDK 180
Cdd:PTZ00393  176 HCVAGLGRAPVLASIVLIEF-GMDPIDAIVFIRD-RRKGAINK-RQLQFLKAYKKK 228
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
90-176 2.25e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 41.96  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882   90 HHHPIPDGGTPDigSCWEIMEELATCLKNNRK------TLIHCYGGLGRS------CLAACLLLYLSDSISPQQAIDSLR 157
Cdd:smart00404   6 HYTGWPDHGVPE--SPDSILELLRAVKKNLNQsessgpVVVHCSAGVGRTgtfvaiDILLQQLEAEAGEVDIFDTVKELR 83

                           90
                   ....*....|....*....
gi 1720380882  158 DVRgSGAIQTIKQYNYLHE 176
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 ...
 17-153 1.60e-90

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: 262.27  E-value: 1.60e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  17 WLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPD 96
Cdd:pfam05706  31 WLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPIAD 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720380882  97 GGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRS-CLAACLLLYLSDSISPQQAI 153
Cdd:pfam05706 111 GGTPDIASCCEIMEELATCLKNNRKTLIHCYGGLGRScLVAACLLLYLSDSISPEQAI 168
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 16-176 9.05e-72

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: 214.43  E-value: 9.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  16 QWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIP 95
Cdd:cd14505     2 DWLPLSMLGNAGSLGLTPCPGCKFKDHRRDLQADLEELKDQGVDDVVTLCTDGELEELGVPDLLEQYQQAGITWHHLPIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  96 DGGTPD-IGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLAACLL-LYLSDSISPQQAIDSLRDVRGsGAIQTIKQYNY 173
Cdd:cd14505    82 DGGVPSdIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLlLELGDTLDPEQAIAAVRALRP-GAIQTPKQENF 160


                  ...
gi 1720380882 174 LHE 176
Cdd:cd14505   161 LHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
48-181 1.90e-18

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 77.70  E-value: 1.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  48 KDTEELKSYGIQDVFVFCTRGELskyrvpnLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCY 127
Cdd:COG2453    16 GGEADLKREGIDAVVSLTEEEEL-------LLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALREGKKVLVHCR 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720380882 128 GGLGRS---------ClaaclllylsDSISPQQAIDSLRDVRgSGAIQTIKQYNYLHEFRDKL 181
Cdd:COG2453    89 GGIGRTgtvaaaylvL----------LGLSAEEALARVRAAR-PGAVETPAQRAFLERFAKRL 140
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 27-176 7.76e-10

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: 54.28  E-value: 7.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  27 QFLGLCALPGCkfkdvrrNIQKDTEELKSYGIQDVFVFCtrgelskyrvpnLLDLYqqygivthhhpipdggtpdigscw 106
Cdd:cd14494     7 LRLIAGALPLS-------PLEADSRFLKQLGVTTIVDLT------------LAMVD------------------------ 43

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882 107 EIMEELATCLKNNRKTLIHCYGGLGRSCLAACLLLYLSDSISPQQAIDSLRDVRGSGAIQTIKQYNYLHE 176
Cdd:cd14494    44 RFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPGGIPQTIEQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 73-177 1.51e-09

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: 54.21  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  73 YRVPNLlDLYQQYGIVTHHHPIPDGGTP---DIGSCWEIMEElatCLKNNRKTLIHCYGGLGRSCLAACLLLYLSDSISP 149
Cdd:cd14504    37 EEPPPE-HSDTCPGLRYHHIPIEDYTPPtleQIDEFLDIVEE---ANAKNEAVLVHCLAGKGRTGTMLACYLVKTGKISA 112

                          90       100
                  ....*....|....*....|....*...
gi 1720380882 150 QQAIDSLRDVRGsGAIQTIKQYNYLHEF 177
Cdd:cd14504   113 VDAINEIRRIRP-GSIETSEQEKFVIQF 139
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 51-177 4.02e-08

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: 51.20  E-value: 4.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  51 EELKSYGIQDVF--------VFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKT 122
Cdd:cd14506    33 EQFKEKGIKTVInlqepgehASCGPGLEPESGFSYLPEAFMRAGIYFYNFGWKDYGVPSLTTILDIVKVMAFALQEGGKV 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720380882 123 LIHCYGGLGRSCLAACLLLYLSDSISPQQAIDSLRDVRgSGAIQTIKQYNYLHEF 177
Cdd:cd14506   113 AVHCHAGLGRTGVLIACYLVYALRMSADQAIRLVRSKR-PNSIQTRGQVLCVREF 166
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 51-180 1.44e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 47.24  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  51 EELKSYGIQDVFVFCTR----GELskyrvpnlldlyQQYGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKTLI 124
Cdd:PTZ00393  110 KEMKNYNVTDLVRTCERtyndGEI------------TSAGINVHELIFPDGDAPtvDIVSNW--LTIVNNVIKNNRAVAV 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720380882 125 HCYGGLGRSCLAACLLLYLSdSISPQQAIDSLRDvRGSGAIQTiKQYNYLHEFRDK 180
Cdd:PTZ00393  176 HCVAGLGRAPVLASIVLIEF-GMDPIDAIVFIRD-RRKGAINK-RQLQFLKAYKKK 228
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 45-180 2.10e-05

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: 42.98  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  45 NIQKDTEELKSYGIQDVFVFCTRgelsKYRVPNLLDLyqqyGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKT 122
Cdd:cd14500    25 NLPLYIKELKKYNVTDLVRVCEP----TYDKEPLEKA----GIKVHDWPFDDGSPPpdDVVDDW--LDLLKTRFKEEGKP 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720380882 123 L----IHCYGGLGRSCLAACLLLYLSdSISPQQAIDSLRDVRgSGAIqTIKQYNYLHEFRDK 180
Cdd:cd14500    95 GaciaVHCVAGLGRAPVLVAIALIEL-GMKPEDAVEFIRKKR-RGAI-NSKQLQFLEKYKPK 153
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
90-176 2.25e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 41.96  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882   90 HHHPIPDGGTPDigSCWEIMEELATCLKNNRK------TLIHCYGGLGRS------CLAACLLLYLSDSISPQQAIDSLR 157
Cdd:smart00404   6 HYTGWPDHGVPE--SPDSILELLRAVKKNLNQsessgpVVVHCSAGVGRTgtfvaiDILLQQLEAEAGEVDIFDTVKELR 83

                           90
                   ....*....|....*....
gi 1720380882  158 DVRgSGAIQTIKQYNYLHE 176
Cdd:smart00404  84 SQR-PGMVQTEEQYLFLYR 101
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 90-176 2.25e-05

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: 41.96  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882   90 HHHPIPDGGTPDigSCWEIMEELATCLKNNRK------TLIHCYGGLGRS------CLAACLLLYLSDSISPQQAIDSLR 157
Cdd:smart00012   6 HYTGWPDHGVPE--SPDSILELLRAVKKNLNQsessgpVVVHCSAGVGRTgtfvaiDILLQQLEAEAGEVDIFDTVKELR 83

                           90
                   ....*....|....*....
gi 1720380882  158 DVRgSGAIQTIKQYNYLHE 176
Cdd:smart00012  84 SQR-PGMVQTEEQYLFLYR 101
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 48-133 8.98e-05

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: 40.61  E-value: 8.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  48 KDTEELKSYGIQdvFVFCTRGELSKYRVPNlldlyqqyGIVTHHHPIPDGGTPDIGS----CWEIMEElatCLKNNRKTL 123
Cdd:cd14498    17 QDKELLKKLGIT--HILNVAGEPPPNKFPD--------GIKYLRIPIEDSPDEDILShfeeAIEFIEE---ALKKGGKVL 83

                          90
                  ....*....|
gi 1720380882 124 IHCYGGLGRS 133
Cdd:cd14498    84 VHCQAGVSRS 93
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
87-176 2.09e-04

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 40.72  E-value: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882   87 IVTHHHPI--PDGGTP-DIGSCWEIMEELATCLKNNRK-TLIHCYGGLGRS-----CLAACLLLYLSDSISPQQAIDSLR 157
Cdd:smart00194 158 TVTHYHYTnwPDHGVPeSPESILDLIRAVRKSQSTSTGpIVVHCSAGVGRTgtfiaIDILLQQLEAGKEVDIFEIVKELR 237

                           90
                   ....*....|....*....
gi 1720380882  158 DVRgSGAIQTIKQYNYLHE 176
Cdd:smart00194 238 SQR-PGMVQTEEQYIFLYR 255
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 69-178 2.87e-04

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 39.62  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  69 ELSKYRVPNLL---------DLYQQYGIVTHHHPIPDGGTP--DIGSCWeiMEELATCLKNNRKTL----IHCYGGLGRS 133
Cdd:PTZ00242   35 ELQRYNVTHLVrvcgptydaELLEKNGIEVHDWPFDDGAPPpkAVIDNW--LRLLDQEFAKQSTPPetiaVHCVAGLGRA 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720380882 134 CLAACLLLYLSDSISPQQAIDSLRDVRgSGAIQtIKQYNYLHEFR 178
Cdd:PTZ00242  113 PILVALALVEYGGMEPLDAVGFVREKR-KGAIN-QTQLQFLKKYK 155
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 44-133 3.19e-04

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: 39.49  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  44 RNIQkDTEELKSYGIQDVFVFCTRGELSKYRV--PNLLDLYQQYGIVTHHHPIPDGGTPD----IGSCWEIMEELatcLK 117
Cdd:cd14526    17 QNPE-DVDRLKKEGVTAVLNLQTDSDMEYWGVdiDSIRKACKESGIRYVRLPIRDFDTEDlrqkLPQAVALLYRL---LK 92

                          90
                  ....*....|....*.
gi 1720380882 118 NNRKTLIHCYGGLGRS 133
Cdd:cd14526    93 NGGTVYVHCTAGLGRA 108
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 51-180 1.13e-03

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: 38.08  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  51 EELKSYGIQDVFVFCtrgELSKYRVPnlldlYQQYGIVTHHHPIPDGGTP--DIGSCWEIMEELATCLKNNRKTLIHCYG 128
Cdd:cd18535    31 EDLKKYGATTVVRVC---EVTYDKTP-----LEKDGITVVDWPFDDGAPPpgKVVEDWLSLLKTKFCEDPGCCVAVHCVA 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720380882 129 GLGRSCLAACLLLYLSdSISPQQAIDSLRDVRgSGAIQTiKQYNYLHEFRDK 180
Cdd:cd18535   103 GLGRAPVLVALALIES-GMKYEDAIQFIRQKR-RGAINS-KQLTYLEKYRPK 151
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 87-176 1.81e-03

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: 37.65  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  87 IVTHHHPI--PDGGTPDIGScwEIMEELA----TCLKNNRKTLIHCYGGLGRS-----CLAACLLLYLSDSISPQQAIDS 155
Cdd:cd00047   103 EVTHLHYTgwPDHGVPSSPE--DLLALVRrvrkEARKPNGPIVVHCSAGVGRTgtfiaIDILLERLEAEGEVDVFEIVKA 180

                          90       100
                  ....*....|....*....|.
gi 1720380882 156 LRDVRgSGAIQTIKQYNYLHE 176
Cdd:cd00047   181 LRKQR-PGMVQTLEQYEFIYE 200
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 46-181 8.45e-03

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: 35.36  E-value: 8.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380882  46 IQKDTEELKSYGIQDVFVFCTrgelSKYRVPnlldLYQQYGIVTHHHPIPDGGTP--DIGSCW------EIMEELATCLK 117
Cdd:cd18536    27 LNKFTEELKKYGVTTLVRVCD----ATYDKA----PVEKEGIQVLDWPFDDGAPPpnQIVDDWlnllktKFREEPGCCVA 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720380882 118 nnrktlIHCYGGLGRSCLAACLLLYLSdSISPQQAIDSLRDVRgSGAIQTiKQYNYLHEFRDKL 181
Cdd:cd18536    99 ------VHCVAGLGRAPVLVALALIEC-GMKYEDAVQFIRQKR-RGAFNS-KQLLYLEKYRPKM 153
 
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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