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Conserved domains on  [gi|1958778754|ref|XP_038966808|]
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protein tyrosine phosphatase type IVA 2 isoform X1 [Rattus norvegicus]

Protein Classification

protein-tyrosine phosphatase family protein; phosphatase PAP2/dual specificity phosphatase family protein( domain architecture ID 13035231)

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; bifunctional phosphatase PAP2/dual specificity phosphatase (DSP) family protein containing a C-terminal DSP domain that may dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues in target proteins, and an N-terminal PAP2 domain with similarity to yeast inositol phosphorylceramide synthase (AUR1) that catalyzes the addition of inositol phosphate to ceramide, an essential step in sphingolipid synthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 1-155 3.86e-120

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: 335.43  E-value: 3.86e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   1 MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDD 80
Cdd:cd18536     1 MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIQVLDWPFDDGAPPPNQIVDD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958778754  81 WLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 155
Cdd:cd18536    81 WLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 155
 
Name Accession Description Interval E-value
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 1-155 3.86e-120

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: 335.43  E-value: 3.86e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   1 MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDD 80
Cdd:cd18536     1 MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIQVLDWPFDDGAPPPNQIVDD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958778754  81 WLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 155
Cdd:cd18536    81 WLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 155
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 8-157 7.12e-72

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 213.73  E-value: 7.12e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   8 EISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDWLNLLKT 87
Cdd:PTZ00242   10 QIEYVLFKFLILDAPSPSNLPLYIKELQRYNVTHLVRVCGPTYDAELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQ 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958778754  88 KFREE--PGCCVAVHCVAGLGRAPVLVALALIE-CGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 157
Cdd:PTZ00242   90 EFAKQstPPETIAVHCVAGLGRAPILVALALVEyGGMEPLDAVGFVREKRKGAINQTQLQFLKKYKPRKKAAG 162
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
32-153 2.88e-19

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 78.86  E-value: 2.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  32 EELKKYGVTTLVRVC-DATYDKAPVEKEGIHVLDWPF-DDGAPPPNQIVD--DWL-NLLKtkfREEPgccVAVHCVAGLG 106
Cdd:COG2453    19 ADLKREGIDAVVSLTeEEELLLGLLEEAGLEYLHLPIpDFGAPDDEQLQEavDFIdEALR---EGKK---VLVHCRGGIG 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958778754 107 RAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSK-QLLYLEKYRPKM 153
Cdd:COG2453    93 RTGTVAAAYLVLLGLSAEEALARVRAARPGAVETPaQRAFLERFAKRL 140
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
61-146 2.20e-12

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 60.07  E-value: 2.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   61 HVLDWPfDDGAPPPNQIVDDWLNLLKTKFREEPGCC-VAVHCVAGLGRAPVLVALALIECGMKYE-------DAVQFIRQ 132
Cdd:smart00404   6 HYTGWP-DHGVPESPDSILELLRAVKKNLNQSESSGpVVVHCSAGVGRTGTFVAIDILLQQLEAEagevdifDTVKELRS 84

                           90
                   ....*....|....*
gi 1958778754  133 KRRGAFNSK-QLLYL 146
Cdd:smart00404  85 QRPGMVQTEeQYLFL 99
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
26-146 6.95e-09

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 53.01  E-value: 6.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  26 TLNKFTEELKKYGVTTLvRVCDATYDKAPVEKEgIHVLDWPfDDGAPP-PNQIVD--DWLNLLKTKFREEPgccVAVHCV 102
Cdd:pfam00102 104 TLKKEKEDEKDYTVRTL-EVSNGGSEETRTVKH-FHYTGWP-DHGVPEsPNSLLDllRKVRKSSLDGRSGP---IVVHCS 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958778754 103 AGLGRAPVLVALALIECGMKYE------DAVQFIRQKRRGAFNSK-QLLYL 146
Cdd:pfam00102 178 AGIGRTGTFIAIDIALQQLEAEgevdifQIVKELRSQRPGMVQTLeQYIFL 228
 
Name Accession Description Interval E-value
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 1-155 3.86e-120

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: 335.43  E-value: 3.86e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   1 MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDD 80
Cdd:cd18536     1 MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIQVLDWPFDDGAPPPNQIVDD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958778754  81 WLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 155
Cdd:cd18536    81 WLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 155
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 1-163 5.71e-114

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: 320.10  E-value: 5.71e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   1 MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDD 80
Cdd:cd18537     4 MNRPAPVEITYKNMRFLITHNPTNATLNKFIEELKKYGVTTVVRVCEATYDTTLVEKEGIQVLDWPFDDGAPPSNQIVDD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  81 WLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFRDT 160
Cdd:cd18537    84 WLNLLKVKFREEPGCCIAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFKDS 163


                  ...
gi 1958778754 161 NGH 163
Cdd:cd18537   164 NGH 166
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 2-155 2.11e-109

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: 308.00  E-value: 2.11e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   2 NRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDW 81
Cdd:cd14500     1 LRPAPTLIEYKGMRFLITDAPTDSNLPLYIKELKKYNVTDLVRVCEPTYDKEPLEKAGIKVHDWPFDDGSPPPDDVVDDW 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778754  82 LNLLKTKFREE--PGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 155
Cdd:cd14500    81 LDLLKTRFKEEgkPGACIAVHCVAGLGRAPVLVAIALIELGMKPEDAVEFIRKKRRGAINSKQLQFLEKYKPKKKL 156
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 2-155 1.39e-104

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: 296.17  E-value: 1.39e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   2 NRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDW 81
Cdd:cd18535     1 NRPAPVEVCYKNMRFLITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDW 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958778754  82 LNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRL 155
Cdd:cd18535    81 LSLLKTKFCEDPGCCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRL 154
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 8-157 7.12e-72

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 213.73  E-value: 7.12e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   8 EISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDWLNLLKT 87
Cdd:PTZ00242   10 QIEYVLFKFLILDAPSPSNLPLYIKELQRYNVTHLVRVCGPTYDAELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRLLDQ 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958778754  88 KFREE--PGCCVAVHCVAGLGRAPVLVALALIE-CGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRF 157
Cdd:PTZ00242   90 EFAKQstPPETIAVHCVAGLGRAPILVALALVEyGGMEPLDAVGFVREKRKGAINQTQLQFLKKYKPRKKAAG 162
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 6-152 1.44e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 149.31  E-value: 1.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   6 PVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDWLNLL 85
Cdd:PTZ00393   84 PTKIEHGKIKILILDAPTNDLLPLYIKEMKNYNVTDLVRTCERTYNDGEITSAGINVHELIFPDGDAPTVDIVSNWLTIV 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778754  86 KTKFREEpgCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPK 152
Cdd:PTZ00393  164 NNVIKNN--RAVAVHCVAGLGRAPVLASIVLIEFGMDPIDAIVFIRDRRKGAINKRQLQFLKAYKKK 228
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 35-154 1.42e-20

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: 82.89  E-value: 1.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  35 KKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDWLNLLktkfrEEPGCCVAVHCVAGLGRAPVLVAL 114
Cdd:cd14499    55 KKLGVTTVVRLNKKLYDAKRFTDAGIRHYDLYFPDGSTPSDDIVKKFLDIC-----ENEKGAIAVHCKAGLGRTGTLIAC 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958778754 115 ALI-ECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMR 154
Cdd:cd14499   130 YLMkHYGFTAREAIAWLRICRPGSVIGPQQQFLEEKEARLW 170
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 14-148 9.88e-20

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: 79.32  E-value: 9.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  14 MRFLITHNPTNaTLNKFTEELKKYGVTTLVRVCDAtydkapvekegihvldwpfddgapppnqIVDDWLNLLKTKfrEEP 93
Cdd:cd14494     7 LRLIAGALPLS-PLEADSRFLKQLGVTTIVDLTLA----------------------------MVDRFLEVLDQA--EKP 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778754  94 GCCVAVHCVAGLGRAPVLVALALIECG-MKYEDAVQFIRQKRRG--AFNSKQLLYLEK 148
Cdd:cd14494    56 GEPVLVHCKAGVGRTGTLVACYLVLLGgMSAEEAVRIVRLIRPGgiPQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
32-153 2.88e-19

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 78.86  E-value: 2.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  32 EELKKYGVTTLVRVC-DATYDKAPVEKEGIHVLDWPF-DDGAPPPNQIVD--DWL-NLLKtkfREEPgccVAVHCVAGLG 106
Cdd:COG2453    19 ADLKREGIDAVVSLTeEEELLLGLLEEAGLEYLHLPIpDFGAPDDEQLQEavDFIdEALR---EGKK---VLVHCRGGIG 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958778754 107 RAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSK-QLLYLEKYRPKM 153
Cdd:COG2453    93 RTGTVAAAYLVLLGLSAEEALARVRAARPGAVETPaQRAFLERFAKRL 140
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 32-146 2.66e-13

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: 63.82  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  32 EELKKYGVTTLVRVCdatydkapvEKEGIHVLDWPFDDGAPPPN-----QIVDDWLNLLKTKFReepgccVAVHCVAGLG 106
Cdd:cd14505    54 GELEELGVPDLLEQY---------QQAGITWHHLPIPDGGVPSDiaqwqELLEELLSALENGKK------VLIHCKGGLG 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958778754 107 RAPVLVALALIECG--MKYEDAVQFIRQKRRGAF-NSKQLLYL 146
Cdd:cd14505   119 RTGLIAACLLLELGdtLDPEQAIAAVRALRPGAIqTPKQENFL 161
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
61-146 2.20e-12

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 60.07  E-value: 2.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   61 HVLDWPfDDGAPPPNQIVDDWLNLLKTKFREEPGCC-VAVHCVAGLGRAPVLVALALIECGMKYE-------DAVQFIRQ 132
Cdd:smart00404   6 HYTGWP-DHGVPESPDSILELLRAVKKNLNQSESSGpVVVHCSAGVGRTGTFVAIDILLQQLEAEagevdifDTVKELRS 84

                           90
                   ....*....|....*
gi 1958778754  133 KRRGAFNSK-QLLYL 146
Cdd:smart00404  85 QRPGMVQTEeQYLFL 99
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 61-146 2.20e-12

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: 60.07  E-value: 2.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   61 HVLDWPfDDGAPPPNQIVDDWLNLLKTKFREEPGCC-VAVHCVAGLGRAPVLVALALIECGMKYE-------DAVQFIRQ 132
Cdd:smart00012   6 HYTGWP-DHGVPESPDSILELLRAVKKNLNQSESSGpVVVHCSAGVGRTGTFVAIDILLQQLEAEagevdifDTVKELRS 84

                           90
                   ....*....|....*
gi 1958778754  133 KRRGAFNSK-QLLYL 146
Cdd:smart00012  85 QRPGMVQTEeQYLFL 99
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 49-166 2.16e-11

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: 59.67  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  49 TYDKAPVEKEGIHVLDWPFDD-GAPPPNQIVDdwlnLLKT-KFREEPGCCVAVHCVAGLGRAPVLVALALI-ECGMKYED 125
Cdd:cd14506    66 SYLPEAFMRAGIYFYNFGWKDyGVPSLTTILD----IVKVmAFALQEGGKVAVHCHAGLGRTGVLIACYLVyALRMSADQ 141

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958778754 126 AVQFIRQKRRGAFNSK-QLLYLEKYrpKMRLRFRDTNGHCCV 166
Cdd:cd14506   142 AIRLVRSKRPNSIQTRgQVLCVREF--AQFLLPLRNVFACPD 181
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 32-134 1.40e-10

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: 56.02  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  32 EELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPfDDGAPPPNQIVDDWLNLLKTKFREepGCCVAVHCVAGLGRAPVL 111
Cdd:cd14498    20 ELLKKLGITHILNVAGEPPPNKFPDGIKYLRIPIE-DSPDEDILSHFEEAIEFIEEALKK--GGKVLVHCQAGVSRSATI 96

                          90       100
                  ....*....|....*....|....
gi 1958778754 112 VALALI-ECGMKYEDAVQFIRQKR 134
Cdd:cd14498    97 VIAYLMkKYGWSLEEALELVKSRR 120
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
26-146 6.95e-09

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 53.01  E-value: 6.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  26 TLNKFTEELKKYGVTTLvRVCDATYDKAPVEKEgIHVLDWPfDDGAPP-PNQIVD--DWLNLLKTKFREEPgccVAVHCV 102
Cdd:pfam00102 104 TLKKEKEDEKDYTVRTL-EVSNGGSEETRTVKH-FHYTGWP-DHGVPEsPNSLLDllRKVRKSSLDGRSGP---IVVHCS 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958778754 103 AGLGRAPVLVALALIECGMKYE------DAVQFIRQKRRGAFNSK-QLLYL 146
Cdd:pfam00102 178 AGIGRTGTFIAIDIALQQLEAEgevdifQIVKELRSQRPGMVQTLeQYIFL 228
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 32-154 6.31e-08

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: 49.29  E-value: 6.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  32 EELKKYGVTTLV----RVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQiVDDWLNLLKTKFREEPgccVAVHCVAGLGR 107
Cdd:cd14529    27 ALLKKLGIKTVIdlrgADERAASEEAAAKIDGVKYVNLPLSATRPTESD-VQSFLLIMDLKLAPGP---VLIHCKHGKDR 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958778754 108 APVLVALALIECGMKYEDAV-QFIRQKRRGAFNSKQLLYLEKYRPKMR 154
Cdd:cd14529   103 TGLVSALYRIVYGGSKEEANeDYRLSNRHLEGLRSGIALDSKGGVKGR 150
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 60-146 7.01e-08

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: 49.98  E-value: 7.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  60 IHVLDWPfDDGAPPPNQIVDDWLNLLKTKFREEPGCCVaVHCVAGLGRAPVLVAL-ALIECgMKYE------DAVQFIRQ 132
Cdd:cd00047   107 LHYTGWP-DHGVPSSPEDLLALVRRVRKEARKPNGPIV-VHCSAGVGRTGTFIAIdILLER-LEAEgevdvfEIVKALRK 183

                          90
                  ....*....|....*
gi 1958778754 133 KRRGAF-NSKQLLYL 146
Cdd:cd00047   184 QRPGMVqTLEQYEFI 198
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 32-136 7.68e-08

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: 48.81  E-value: 7.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  32 EELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDWLNLLKTkfREEPGCCVAVHCVAGLGRAPVL 111
Cdd:cd14504    22 AYLNENGIRHVVTLTEEPPPEHSDTCPGLRYHHIPIEDYTPPTLEQIDEFLDIVEE--ANAKNEAVLVHCLAGKGRTGTM 99

                          90       100
                  ....*....|....*....|....*.
gi 1958778754 112 VALALIECG-MKYEDAVQFIRQKRRG 136
Cdd:cd14504   100 LACYLVKTGkISAVDAINEIRRIRPG 125
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 9-149 2.03e-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: 47.64  E-value: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   9 ISYENMRFLITHN---PTNATLNKfTEELKKYGVTTLVRVCDATYDKAPVEK--EGIHVLDwpfddgapppnqivddwln 83
Cdd:cd14524    24 VAKENVRGVITMNeeyETRFFCNS-KEEWKALGVEQLRLPTVDFTGVPSLEDleKGVDFIL------------------- 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778754  84 llktKFREEpGCCVAVHCVAGLGRAPVLVALALIEC-GMKYEDAVQFIRQKRRG-AFNSKQLLYLEKY 149
Cdd:cd14524    84 ----KHREK-GKSVYVHCKAGRGRSATIVACYLIQHkGWSPEEAQEFLRSKRPHiLLRLSQREVLEEF 146
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 13-148 3.96e-07

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: 46.82  E-value: 3.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  13 NMRFL----ITHnptnaTLNkfTEELKKYGvttLVRVCDATYDKAPVEKEGIHVLDWP-------FDDGApppnQIVDDW 81
Cdd:cd14515    18 NKAKLkklgITH-----VLN--AAEGKKNG---EVNTNAKFYKGSGIIYLGIPASDLPtfdisqyFDEAA----DFIDKA 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958778754  82 LNLLKTKfreepgccVAVHCVAGLGRAPVLV-ALALIECGMKYEDAVQFIRQKRRGAFNS---KQLLYLEK 148
Cdd:cd14515    84 LSDPGGK--------VLVHCVEGVSRSATLVlAYLMIYQNMTLEEAIRTVRKKREIRPNRgflQQLCELND 146
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 62-149 2.50e-06

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: 44.89  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  62 VLDWPFDDGAPPPNQI-------VDDWLnllktkfREEPGCCVAVHCVAGLGRAPVLVALALIECGM--KYEDAVQFIRQ 132
Cdd:cd14509    62 VAEYPFDDHNPPPLELikpfcedVDEWL-------KEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKfpSAKEALDFYGA 134

                          90       100
                  ....*....|....*....|...
gi 1958778754 133 KRrgAFNSK------QLLYLEKY 149
Cdd:cd14509   135 KR--TKNKKgvtipsQRRYVYYY 155
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 60-134 2.60e-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: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  60 IHVLDWPfDDGAPPPNQIVDDWLNLLKTK--FREEPgccVAVHCVAGLGRAPVLV----ALALIECGMKYE--DAVQFIR 131
Cdd:cd14601   111 IQYIAWP-DHGVPDDSSDFLDFVCLVRNKraGKDEP---VVVHCSAGIGRTGVLItmetAMCLIECNQPVYplDIVRTMR 186


                  ...
gi 1958778754 132 QKR 134
Cdd:cd14601   187 DQR 189
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
60-146 3.84e-06

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 45.34  E-value: 3.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   60 IHVLDWPfDDGAPPPNQIVDDWLNLLKTKFREEPGCCVaVHCVAGLGRAPVLVALALIECGMKYE------DAVQFIRQK 133
Cdd:smart00194 162 YHYTNWP-DHGVPESPESILDLIRAVRKSQSTSTGPIV-VHCSAGVGRTGTFIAIDILLQQLEAGkevdifEIVKELRSQ 239

                           90
                   ....*....|....
gi 1958778754  134 RRGAFNSK-QLLYL 146
Cdd:smart00194 240 RPGMVQTEeQYIFL 253
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 94-134 4.46e-06

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: 44.11  E-value: 4.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958778754  94 GCCVAVHCVAGLGRAP--VLVALALIeCGMKYEDAVQFIRQKR 134
Cdd:cd14526    94 GGTVYVHCTAGLGRAPatVIAYLYWV-LGYSLDEAYYLLTSKR 135
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 15-147 7.30e-06

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: 43.72  E-value: 7.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  15 RFLITHNPTNATLNKFTEElkKYGVTTLVrvcdatydkapvekEGiHVLDWPFDDGAPPP----NQIVDD---WLNllkt 87
Cdd:cd14497    33 NFLNTHHPDHYMIFNLSEE--EYDDDSKF--------------EG-RVLHYGFPDHHPPPlgllLEIVDDidsWLS---- 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778754  88 kfrEEPGCCVAVHCVAGLGRAPVLVALALIECGM--KYEDAVQFIRQKR-----RGAFNSKQLLYLE 147
Cdd:cd14497    92 ---EDPNNVAVVHCKAGKGRTGTVICAYLLYYGQysTADEALEYFAKKRfkeglPGVTIPSQLRYLQ 155
PRK12361 PRK12361
hypothetical protein; Provisional
 32-152 8.75e-06

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 44.61  E-value: 8.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  32 EELKKYGVTTLVRVCdATYD--KAPVEKEGIHVLDWP-FDDGAPPPNQIVD--DWLNLLKTKFREepgccVAVHCVAGLG 106
Cdd:PRK12361  114 EKLKSNKITAILDVT-AEFDglDWSLTEEDIDYLNIPiLDHSVPTLAQLNQaiNWIHRQVRANKS-----VVVHCALGRG 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958778754 107 RApVLVALALIECGMK---YEDAVQFIRQKRRGA-FNSKQLLYLEKYRPK 152
Cdd:PRK12361  188 RS-VLVLAAYLLCKDPdltVEEVLQQIKQIRKTArLNKRQLRALEKMLEQ 236
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
32-134 1.39e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 42.65  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   32 EELKKYGVTTLVRVCDATYDKAPVEKEGIHVldwPFDDGappPNQIVDDWLNLLKTK--FREEPGCCVAVHCVAGLGRAP 109
Cdd:smart00195  20 ALLKKLGITHVINVTNEVPNYNGSDFTYLGV---PIDDN---TETKISPYFPEAVEFieDAESKGGKVLVHCQAGVSRSA 93

                           90       100
                   ....*....|....*....|....*.
gi 1958778754  110 VLVALALIEC-GMKYEDAVQFIRQKR 134
Cdd:smart00195  94 TLIIAYLMKTrNMSLNDAYDFVKDRR 119
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 94-134 2.77e-05

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: 41.63  E-value: 2.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958778754  94 GCCVAVHCVAGLGRAPVL-VALALIECGMKYEDAVQFIRQKR 134
Cdd:cd14568    79 NKRVLVHCLAGISRSATIaIAYIMKHMRMSLDDAYRFVKEKR 120
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 6-135 3.81e-05

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


Pssm-ID: 350414 [Multi-domain]  Cd Length: 137  Bit Score: 41.15  E-value: 3.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754   6 PVEIsyenMRFLITHNPTNATlnkFTEELKKYGVTTLVRVcdaTYDKAPV--EKEGIHVLDWPfddgapppnqIVDDWL- 82
Cdd:cd14566     1 PVEI----LPFLYLGNAKDSA---NIDLLKKYNIKYILNV---TPNLPNTfeEDGGFKYLQIP----------IDDHWSq 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958778754  83 NLLK-----TKFREEP---GCCVAVHCVAGLGRA-PVLVALALIECGMKYEDAVQFIRQKRR 135
Cdd:cd14566    61 NLSAffpeaISFIDEArskKCGVLVHCLAGISRSvTVTVAYLMQKLHLSLNDAYDFVKKRKS 122
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 44-153 4.52e-05

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: 42.13  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  44 RVCDATYDKAPVEKEgIHVLDWPfDDGAPPPNQ-IVDDWLNLLKTKfrEEPGCC--VAVHCVAGLGRAPVLVALALIECG 120
Cdd:cd14554   125 KVTDARDGQSRTVRQ-FQFTDWP-EQGVPKSGEgFIDFIGQVHKTK--EQFGQEgpITVHCSAGVGRTGVFITLSIVLER 200

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958778754 121 MKYEDAVQFirqkrrgaFNSKQLLYLEkyRPKM 153
Cdd:cd14554   201 MRYEGVVDV--------FQTVKLLRTQ--RPAM 223
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 94-134 6.39e-05

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: 40.71  E-value: 6.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958778754  94 GCCVAVHCVAGLGRAPVLVALALIEC-GMKYEDAVQFIRQKR 134
Cdd:pfam00782  69 GGKVLVHCQAGISRSATLIIAYLMKTrNLSLNEAYSFVKERR 110
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 65-141 7.85e-05

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong 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. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 41.21  E-value: 7.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  65 WPfDDGAPppnQIVDDWLNLLKTKFREEPGCCVAVHCVAGLGRAPVL----VALALIECGMKYE--DAVQFIRQKRRGAF 138
Cdd:cd14538   115 WP-DHGTP---QSADPLLRFIRYMRRIHNSGPIVVHCSAGIGRTGVLitidVALGLIERDLPFDiqDIVKDLREQRQGMI 190


                  ...
gi 1958778754 139 NSK 141
Cdd:cd14538   191 QTK 193
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 72-134 2.97e-04

dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; Serine/threonine/tyrosine-interacting protein (STYX), also called protein tyrosine phosphatase-like protein, is a catalytically inactive member of the protein tyrosine phosphatase family that plays an integral role in regulating pathways by competing with active phosphatases for binding to MAPKs. It acts as a nuclear anchor for MAPKs, affecting their nucleocytoplasmic shuttling.


Pssm-ID: 350372 [Multi-domain]  Cd Length: 151  Bit Score: 39.24  E-value: 2.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958778754  72 PPPNQIVDDWLNllktkfreePGCCVAVHCVAGLGRAPVLVALALIEC-GMKYEDAVQFIRQKR 134
Cdd:cd14522    76 PTVKEFIDDCLQ---------TGGKVLVHGNAGISRSAALVIAYIMETyGLSYRDAFAYVQQRR 130
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 60-142 3.46e-04

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: 39.35  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  60 IHVLDWPfDDGAPPPNQIVDDWLNLLKTKFREEPgccVAVHCVAGLGRAPVL----VALALIECGMKYE--DAVQFIRQK 133
Cdd:cd14596   109 LQFTTWP-DHGTPQSSDQLVKFICYMRKVHNTGP---IVVHCSAGIGRAGVLicvdVLLSLIEKDLSFNikDIVREMRQQ 184


                  ....*....
gi 1958778754 134 RRGAFNSKQ 142
Cdd:cd14596   185 RYGMIQTKD 193
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 64-153 3.79e-04

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which 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 that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains 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). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 39.71  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  64 DWPfDDGAPPPNQIVDDWLNLL-KTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYE---DAVQFIRQKR--RGA 137
Cdd:cd14628   190 DWP-EQGVPKSGEGFIDFIGQVhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEgvvDIFQTVKMLRtqRPA 268

                          90
                  ....*....|....*.
gi 1958778754 138 FNSKQLLYLEKYRPKM 153
Cdd:cd14628   269 MVQTEDQYQFCYRAAL 284
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 32-134 4.50e-04

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


Pssm-ID: 350413 [Multi-domain]  Cd Length: 138  Bit Score: 38.52  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  32 EELKKYGVTTLVRV---CDA------TYDKAPVEKEGIHVLDWPFDDGApppnqivdDWLNLLKTKfreepGCCVAVHCV 102
Cdd:cd14565    20 EVLKALGITAVLNVsrnCPNhfedhfQYKSIPVEDSHNADISSWFEEAI--------GFIDKVKAS-----GGRVLVHCQ 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958778754 103 AGLGRAPVlVALA-LIEC-GMKYEDAVQFIRQKR 134
Cdd:cd14565    87 AGISRSAT-ICLAyLMTTrRVRLNEAFDYVKQRR 119
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 64-131 4.52e-04

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which 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. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains 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). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 39.33  E-value: 4.52e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958778754  64 DWPfDDGAPPPNQIVDDWLNLL-KTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIR 131
Cdd:cd14627   191 DWP-EQGVPKSGEGFIDFIGQVhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQ 258
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 94-134 4.76e-04

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


Pssm-ID: 350362 [Multi-domain]  Cd Length: 136  Bit Score: 38.23  E-value: 4.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958778754  94 GCCVAVHCVAGLGR-APVLVALALIECGMKYEDAVQFIRQKR 134
Cdd:cd14512    79 NGGVLVHCLAGISRsATIAIAYLMKRMRMSLDEAYDFVKEKR 120
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 64-131 7.15e-04

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which 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. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains 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). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 38.94  E-value: 7.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958778754  64 DWPfDDGAPPPNQIVDDWLNLL-KTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIR 131
Cdd:cd14629   191 DWP-EQGVPKTGEGFIDFIGQVhKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQ 258
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 97-134 9.86e-04

dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and similar proteins; Dual specificity protein phosphatase 22 (DUSP22, also known as VHX) and 15 (DUSP15, also known as VHY) function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). They 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. The both contain N-terminal myristoylation recognition sequences and myristoylation regulates their subcellular location. DUSP22 negatively regulates the estrogen receptor-alpha-mediated signaling pathway and the IL6-leukemia inhibitory factor (LIF)-STAT3-mediated signaling pathway. DUSP15 has been identified as a regulator of oligodendrocyte differentiation. DUSP22 is a single domain protein containing only the catalytic dual specificity phosphatase domain while DUSP15 contains a short C-terminal tail.


Pssm-ID: 350369 [Multi-domain]  Cd Length: 136  Bit Score: 37.34  E-value: 9.86e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958778754  97 VAVHCVAGLGRAPVLVALALIE-CGMKYEDAVQFIRQKR 134
Cdd:cd14519    80 VLVHCLAGVSRSVTIVAAYLMTvTDLGWRDALKAVRAAR 118
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
 28-147 1.03e-03

dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 isoform A (DUSP13A), also called branching-enzyme interacting DSP or muscle-restricted DSP (MDSP), 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. DUSP13A 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. DUSP13A also functions as a regulator of apoptosis signal-regulating kinase 1 (ASK1), a MAPK kinase kinase, by interacting with its N-terminal domain and inducing ASK1-mediated apoptosis through the activation of caspase-3. This function is independent of phosphatase activity.


Pssm-ID: 350428 [Multi-domain]  Cd Length: 145  Bit Score: 37.43  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  28 NKFteELKKYGVTTLV------RVCDATYD--KAPVEKEGIHVLDWPFDDGAP---PPNQIVDDWLNllktkfreEPGCC 96
Cdd:cd14580    18 NRF--GLWKLGITHVLnaahgkLFCQGGDDfyGTSVDYYGVPANDLPDFDISPyfySAAEFIHRALN--------TPGAK 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958778754  97 VAVHCVAGLGRAPVLV-ALALIECGMKYEDAVQFIRQKRRGAFNS---KQLLYLE 147
Cdd:cd14580    88 VLVHCAVGVSRSATLVlAYLMIYHQLSLVQAIKTVKERRWIFPNRgflKQLRKLD 142
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 61-127 2.21e-03

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ 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 (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 37.10  E-value: 2.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778754  61 HVLDWPfDDGAPPPNQIVDDWLNLLKTKFREEP-GCCVAVHCVAGLGRAPVLVALALIECGMKYEDAV 127
Cdd:cd14615   131 HFTSWP-DHGVPETTDLLINFRHLVREYMKQNPpNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVV 197
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 65-134 4.05e-03

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: 36.37  E-value: 4.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778754  65 WPfDDGAPPPNQIVDDWLNLLKTKFRE-EPgccVAVHCVAGLGRAPVLVALALIECGMKYE------DAVQFIRQKR 134
Cdd:cd14600   179 WP-DHGVPDDSSDFLEFVNYVRSKRVEnEP---VLVHCSAGIGRTGVLVTMETAMCLTERNqpvyplDIVRKMRDQR 251
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 65-119 5.40e-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: 35.77  E-value: 5.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778754  65 WPfDDGAPppnqivDDWLNLLKTKFR--------EEPgccVAVHCVAGLGRAPVLV----ALALIEC 119
Cdd:cd14541   116 WP-DHGVP------DDSSDFLDFVKRvrqnrvgmVEP---TVVHCSAGIGRTGVLItmetAMCLIEA 172
DSP_DUSP8 cd14645
dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual ...
 95-134 6.10e-03

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


Pssm-ID: 350493 [Multi-domain]  Cd Length: 151  Bit Score: 35.37  E-value: 6.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958778754  95 CCVAVHCVAGLGR-APVLVALALIECGMKYEDAVQFIRQKR 134
Cdd:cd14645    91 CRVIVHCLAGISRsATIAIAYIMKTMGLSSDDAYRFVKDRR 131
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 35-136 6.14e-03

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: 36.01  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  35 KKYGVTTLvRVCDATYDKAPVEKEGIHVLDWPfDDGAPPPNQIVDDWLNLLKTKFREEPGCC-VAVHCVAGLGRAPVLVA 113
Cdd:cd14606   136 TEYKLRTL-QVSPLDNGELIREIWHYQYLSWP-DHGVPSEPGGVLSFLDQINQRQESLPHAGpIIVHCSAGIGRTGTIIV 213

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958778754 114 LALI---------ECGMKYEDAVQFIRQKRRG 136
Cdd:cd14606   214 IDMLmenistkglDCDIDIQKTIQMVRAQRSG 245
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 61-136 8.22e-03

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 35.52  E-value: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778754  61 HVLDWPfDDGAPPPNQIVDDWLNLLKTKF--REEPGCCVaVHCVAGLGR-APVLVALALIE--------CGMKYEDAVQF 129
Cdd:cd14544   146 QYLSWP-DHGVPSDPGGVLNFLEDVNQRQesLPHAGPIV-VHCSAGIGRtGTFIVIDMLLDqikrkgldCDIDIQKTIQM 223


                  ....*..
gi 1958778754 130 IRQKRRG 136
Cdd:cd14544   224 VRSQRSG 230
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 73-134 8.24e-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: 35.33  E-value: 8.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778754  73 PPNQIVDDWLNLLKtKFREE---PGCCVAVHCVAGLGRAPVLVALALIEC-GMKYEDAVQFIRQKR 134
Cdd:cd17665    90 PDDKTIQSFKDAVK-DFLEKnkdNDKLIGVHCTHGLNRTGYLICRYLIDVdGMSPDDAIEAFEQAR 154
DUSP13B cd14577
dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 ...
 97-148 9.70e-03

dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 isoform B (DUSP13B), also called testis- and skeletal-muscle-specific DSP (TMDP) or dual specificity phosphatase SKRP4, 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. DUSP13B 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. DUSP13B inactivates MAPK activation in the order of selectivity, JNK = p38 > ERK in cells. It may play a role in protection from external stress during spermatogenesis.


Pssm-ID: 350425 [Multi-domain]  Cd Length: 163  Bit Score: 34.78  E-value: 9.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778754  97 VAVHCVAGLGRAPVLV-ALALIECGMKYEDAVQFIRQKRRGAFNS---KQLLYLEK 148
Cdd:cd14577   106 VLVHCAMGISRSATLVlAFLMICEDLTLVDAIQTVRAHRDICPNSgflRQLRELDN 161
 
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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