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Conserved domains on  [gi|528492142|ref|XP_005155316|]
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putative tyrosine-protein phosphatase TPTE isoform X1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 188-364 1.21e-136

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


:

Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 392.11  E-value: 1.21e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 188 SENKRRYQKDGFDLDLTYVTERVIAMSFPSSGKQALYRNPIREVVRFLDTKHMDHYKVFNLCSEKGYDPKFFHYRVERVM 267
Cdd:cd14510    1 SENKRRYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLCSERGYDPKYFHNRVERVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 268 IDDHNVPSLDDMLRYTACVRDWMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQFESAQESLDYFGERRTDKSMSSKFQ 347
Cdd:cd14510   81 IDDHNVPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSSKFQ 160

                        170
                 ....*....|....*..
gi 528492142 348 GVETPSQSRYVGYYEIM 364
Cdd:cd14510  161 GVETPSQSRYVGYFEKL 177
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 373-510 1.27e-39

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


:

Pssm-ID: 463081  Cd Length: 133  Bit Score: 140.11  E-value: 1.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142  373 PPRKSLKIKSIRIHSIAGVGKGNGSDLKLKIIVKHELVFQcvcaKQHNCTVFPDTGSNAVVISLQDGPIVTGDVKVMFeS 452
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVFS----TSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEF-Y 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528492142  453 SAGLPKGYEDCPFYFWFNTSFVENYRLFLSREELDNPHKPKTWDIYKEDFGVTLSFTE 510
Cdd:pfam10409  76 HKGSDLLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDKKDKRFPKDFKVELLFSE 133
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 55-175 3.08e-11

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


:

Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 63.44  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142   55 SFGFRVFGLVLIILDIIMVIVDlSLSEKSRDVGGALETVSLVISFFFLIDVLLRVYVEGFKV-YFSSKLNIVDaCIVVIT 133
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALE-TYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKKrYFRSPWNILD-FVVVLP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 528492142  134 LVVTMIYAFSDfsgaslIPRVVTFLRSLRILilvRIFRLASQ 175
Cdd:pfam00520  79 SLISLVLSSVG------SLSGLRVLRLLRLL---RLLRLIRR 111
 
Name Accession Description Interval E-value
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 188-364 1.21e-136

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


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 392.11  E-value: 1.21e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 188 SENKRRYQKDGFDLDLTYVTERVIAMSFPSSGKQALYRNPIREVVRFLDTKHMDHYKVFNLCSEKGYDPKFFHYRVERVM 267
Cdd:cd14510    1 SENKRRYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLCSERGYDPKYFHNRVERVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 268 IDDHNVPSLDDMLRYTACVRDWMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQFESAQESLDYFGERRTDKSMSSKFQ 347
Cdd:cd14510   81 IDDHNVPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSSKFQ 160

                        170
                 ....*....|....*..
gi 528492142 348 GVETPSQSRYVGYYEIM 364
Cdd:cd14510  161 GVETPSQSRYVGYFEKL 177
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 373-510 1.27e-39

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 140.11  E-value: 1.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142  373 PPRKSLKIKSIRIHSIAGVGKGNGSDLKLKIIVKHELVFQcvcaKQHNCTVFPDTGSNAVVISLQDGPIVTGDVKVMFeS 452
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVFS----TSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEF-Y 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528492142  453 SAGLPKGYEDCPFYFWFNTSFVENYRLFLSREELDNPHKPKTWDIYKEDFGVTLSFTE 510
Cdd:pfam10409  76 HKGSDLLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDKKDKRFPKDFKVELLFSE 133
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
206-362 2.65e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 64.22  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 206 VTERVIAMSFPSSGKQALYRNPIREVVrfldtkhmdhykvfNLCSEKGYDPKFF---HYRVERVMIDDHNVPSLDDMLRY 282
Cdd:COG2453    4 IPGLLAGGPLPGGGEADLKREGIDAVV--------------SLTEEEELLLGLLeeaGLEYLHLPIPDFGAPDDEQLQEA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 283 TACVRDWMAADSRnvIAIHCKGGKGRTGTMVCTWLIDSDQfeSAQESLDYFGERRTdksmsskfQGVETPSQSRYVGYYE 362
Cdd:COG2453   70 VDFIDEALREGKK--VLVHCRGGIGRTGTVAAAYLVLLGL--SAEEALARVRAARP--------GAVETPAQRAFLERFA 137
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 55-175 3.08e-11

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 63.44  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142   55 SFGFRVFGLVLIILDIIMVIVDlSLSEKSRDVGGALETVSLVISFFFLIDVLLRVYVEGFKV-YFSSKLNIVDaCIVVIT 133
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALE-TYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKKrYFRSPWNILD-FVVVLP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 528492142  134 LVVTMIYAFSDfsgaslIPRVVTFLRSLRILilvRIFRLASQ 175
Cdd:pfam00520  79 SLISLVLSSVG------SLSGLRVLRLLRLL---RLLRLIRR 111
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
270-365 4.20e-09

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 53.90  E-value: 4.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142   270 DHNVP-SLDDMLRYTACVRDWM-AADSRNVIAIHCKGGKGRTGTMVCTWLIdSDQFESAQESLDYFGerrTDKSM-SSKF 346
Cdd:smart00404  12 DHGVPeSPDSILELLRAVKKNLnQSESSGPVVVHCSAGVGRTGTFVAIDIL-LQQLEAEAGEVDIFD---TVKELrSQRP 87

                           90
                   ....*....|....*....
gi 528492142   347 QGVETPSQSRYVgYYEIMK 365
Cdd:smart00404  88 GMVQTEEQYLFL-YRALLE 105
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 234-337 8.66e-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: 42.25  E-value: 8.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142  234 FLDTKHMDHykVFNLCSEKGYDPKFFHY-RVErvMIDDHNVPSLDDMLRYTACVRDwmAADSRNVIAIHCKGGKGRTGTM 312
Cdd:pfam00782  13 FLSKLGITA--VINVTREVDLYNSGILYlRIP--VEDNHETNISKYLEEAVEFIDD--ARQKGGKVLVHCQAGISRSATL 86

                          90       100
                  ....*....|....*....|....*
gi 528492142  313 VCTWLIDSDQFeSAQESLDYFGERR 337
Cdd:pfam00782  87 IIAYLMKTRNL-SLNEAYSFVKERR 110
 
Name Accession Description Interval E-value
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 188-364 1.21e-136

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


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 392.11  E-value: 1.21e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 188 SENKRRYQKDGFDLDLTYVTERVIAMSFPSSGKQALYRNPIREVVRFLDTKHMDHYKVFNLCSEKGYDPKFFHYRVERVM 267
Cdd:cd14510    1 SENKRRYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLCSERGYDPKYFHNRVERVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 268 IDDHNVPSLDDMLRYTACVRDWMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQFESAQESLDYFGERRTDKSMSSKFQ 347
Cdd:cd14510   81 IDDHNVPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSSKFQ 160

                        170
                 ....*....|....*..
gi 528492142 348 GVETPSQSRYVGYYEIM 364
Cdd:cd14510  161 GVETPSQSRYVGYFEKL 177
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 202-364 3.39e-74

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: 231.32  E-value: 3.39e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 202 DLTYVTERVIAMSFPSSGKQALYRNPIREVVRFLDTKHMDHYKVFNLCSEKGYDPKFFHYRVERVMIDDHNVPSLDDMLR 281
Cdd:cd14509    1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 282 YTACVRDWMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQFESAQESLDYFGERRTDKSmsskfQGVETPSQSRYVGYY 361
Cdd:cd14509   81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNK-----KGVTIPSQRRYVYYY 155


                 ...
gi 528492142 362 EIM 364
Cdd:cd14509  156 SRL 158
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 202-362 5.19e-64

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: 205.12  E-value: 5.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 202 DLTYVTERVIAMSFPSSGK-QALYRNPIREVVRFLDTKHMDHYKVFNLCSEKGYDPKFFHYRVERVMIDDHNVPSLDDML 280
Cdd:cd14497    1 DLSYITPRIIAMSFPATGYpESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDDSKFEGRVLHYGFPDHHPPPLGLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 281 RYTACVRDWMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQFESAQESLDYFGERRtdksMSSKFQGVETPSQSRYVGY 360
Cdd:cd14497   81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKR----FKEGLPGVTIPSQLRYLQY 156


                 ..
gi 528492142 361 YE 362
Cdd:cd14497  157 FE 158
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 373-510 1.27e-39

C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (pfam00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane.


Pssm-ID: 463081  Cd Length: 133  Bit Score: 140.11  E-value: 1.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142  373 PPRKSLKIKSIRIHSIAGVGKGNGSDLKLKIIVKHELVFQcvcaKQHNCTVFPDTGSNAVVISLQDGPIVTGDVKVMFeS 452
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVFS----TSGKYKKLKEYQQDDCVILFPKGIPVQGDVLVEF-Y 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528492142  453 SAGLPKGYEDCPFYFWFNTSFVENYRLFLSREELDNPHKPKTWDIYKEDFGVTLSFTE 510
Cdd:pfam10409  76 HKGSDLLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDKKDKRFPKDFKVELLFSE 133
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 202-361 2.91e-39

protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular proteins (tensin-1, -2, -3 and -4) act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Dysregulation of tensin expression has been implicated in human cancer. Tensin-1, -2, and -3 contain an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. In addition, tensin-2 contains a zinc finger N-terminal to its PTP domain. Tensin-4 is not included in this model as it does not contain a PTP-like domain.


Pssm-ID: 350358 [Multi-domain]  Cd Length: 159  Bit Score: 139.83  E-value: 2.91e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 202 DLTYVTERVIAMSFPSSGKQALYRNPIREVVRFLDTKHMDHYKVFNLcSEKGYDPKFFHYRVERVMIDDHNVPSLDDMLR 281
Cdd:cd14508    1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNL-SERRHDLRSLNPKVLDFGWPELHAPPLEKLCS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 282 YTACVRDWMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQFESAQESLDYFGERRTdksMSSKFQGVETPSQSRYVGYY 361
Cdd:cd14508   80 ICKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRF---YDDKVGPLGQPSQKRYVGYF 156
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 200-360 7.71e-36

protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily contains proteins similar to auxilin, characterized by also containing a J domain. It includes auxilin, also called auxilin-1, and cyclin-G-associated kinase (GAK), also called auxilin-2. Auxilin-1 and -2 facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, while auxilin-1 which is nerve-specific. Both proteins contain a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. In addition, GAK contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2.


Pssm-ID: 350361 [Multi-domain]  Cd Length: 164  Bit Score: 130.93  E-value: 7.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 200 DLDLTYVTERVIAMSFPSSG-KQALYRNPIREVVRFLDTKHMDHYKVFNLcSEKGYDPKFFHYRVERVMIDDHNVPSLDD 278
Cdd:cd14511    8 DLDISYITSRIIVMPFPAEGiESTYRKNNIEDVRAFLDSRHPQKYSVYNL-SPRSYPTLRLPSRVVECSWPYRRAPSLHA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 279 MlrYTACvRD---WMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQFESAQESLDYFGERRTDKSMSskfqgvetPSQS 355
Cdd:cd14511   87 L--YALC-RDiyqWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKRCPPGLS--------PSEL 155


                 ....*
gi 528492142 356 RYVGY 360
Cdd:cd14511  156 RYLYY 160
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 202-361 4.05e-34

protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. It plays an essential role in TGF-beta-induced myofibroblast differentiation and myofibroblast-mediated formation of extracellular fibronectin and collagen matrix. It also positively regulates RhoA activity through its interaction with DLC1, a RhoGAP-containing tumor suppressor; the tensin-1-DLC1-RhoA signaling axis is critical in regulating cellular functions that lead to angiogenesis. Tensin-1 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350408 [Multi-domain]  Cd Length: 159  Bit Score: 126.25  E-value: 4.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 202 DLTYVTERVIAMSFPSSGKQALYRNPIREVVRFLDTKHMDHYKVFNLcSEKGYDPKFFHYRVERVMIDDHNVPSLDDMLR 281
Cdd:cd14560    1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNL-SERRHDISKLHPKVLDFGWPDLHAPALEKICS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 282 YTACVRDWMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQFESAQESLDYFGERRTdksMSSKFQGVETPSQSRYVGYY 361
Cdd:cd14560   80 ICKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRF---YEDKVVPVGQPSQKRYVHYF 156
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 202-360 1.51e-32

protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called tensin-like SH2 domain-containing protein 1 (TENS1) or tumor endothelial marker (TEM6). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-3 contributes to cell migration, anchorage-independent growth, tumorigenesis, and metastasis of cancer cells. It cooperates with Dock5, an exchange factor for the small GTPase Rac, for osteoclast activity to ensure the correct organization of podosomes. Tensin-3 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350409 [Multi-domain]  Cd Length: 159  Bit Score: 121.98  E-value: 1.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 202 DLTYVTERVIAMSFPSSGKQALYRNPIREVVRFLDTKHMDHYKVFNLcSEKGYDPKFFHYRVERVMIDDHNVPSLDDMLR 281
Cdd:cd14561    1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNL-SEKRYELTKLNPKIMDVGWPDLHAPPLDKMCT 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528492142 282 YTACVRDWMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQFESAQESLDYFGERrtdKSMSSKFQGVETPSQSRYVGY 360
Cdd:cd14561   80 ICKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMK---KFYDDKVSALMQPSQKRYVQF 155
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 202-361 1.22e-28

protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called tensin-like C1 domain-containing phosphatase (TENC1) or C1 domain-containing phosphatase and tensin homolog (C1-TEN). It is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. Tensin-2 is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It also modulates cell contractility and remodeling of collagen fibers through the DLC1, a RhoGAP that binds to tensins in focal adhesions. Tensin-2 may have phosphatase activity; it reduces AKT1 phosphorylation. It contains an N-terminal region with a zinc finger, a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350410 [Multi-domain]  Cd Length: 159  Bit Score: 111.19  E-value: 1.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 202 DLTYVTERVIAMSFPSSGKQALYRNPIREVVRFLDTKHMDHYKVFNLcSEKGYDPKFFHYRVERVMIDDHNVPSLDDMLR 281
Cdd:cd14562    1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNL-SEKRHDITRLNPKVQDFGWPDLHAPPLDKICS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 282 YTACVRDWMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQFESAQESLDYFGERR--TDKsMSSKFQgvetPSQSRYVG 359
Cdd:cd14562   80 ICKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKfcEDK-VATSLQ----PSQRRYIS 154


                 ..
gi 528492142 360 YY 361
Cdd:cd14562  155 YF 156
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 200-360 1.33e-28

protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated kinase (GAK), also called auxilin-2, contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor.


Pssm-ID: 350412 [Multi-domain]  Cd Length: 163  Bit Score: 111.15  E-value: 1.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 200 DLDLTYVTERVIAMSFPSSGKQALYRNPIREVVRFLDTKHMDHYKVFNLCsEKGYDPKFFHYRVERVMIDDHNVPSLDDM 279
Cdd:cd14564    8 DLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLS-QRTYRPSRFHNRVSECGWPARRAPNLQNL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 280 LRYTACVRDWMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQFESAQESLDYFGERRTDKSMSskfqgvetPSQSRYVG 359
Cdd:cd14564   87 YSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPPGIW--------PSHKRYIE 158


                 .
gi 528492142 360 Y 360
Cdd:cd14564  159 Y 159
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 200-360 3.60e-27

N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 or DnaJ homolog subfamily C member 6 (DNAJC6), is a J-domain containing protein that recruits the ATP-dependent chaperone Hsc70 to newly budded clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles, driving the clathrin assembly#disassembly cycle. Mutations in the DNAJC6 gene, encoding auxilin, are associated with early-onset Parkinson's disease. Auxilin contains an N-terminal protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN, a phosphoinositide 3-phosphatase, and a C-terminal region with clathrin-binding and J domains.


Pssm-ID: 350411 [Multi-domain]  Cd Length: 163  Bit Score: 107.27  E-value: 3.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 200 DLDLTYVTERVIAMSFPSSGKQALYRNPIREVVRFLDTKHMDHYKVFNLcSEKGYDPKFFHYRVERVMIDDHNVPSLDDM 279
Cdd:cd14563    8 ELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNL-SQKSYRSAKFHNRVSECSWPVRQAPSLHNL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 280 LRYTACVRDWMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQFESAQESLDYFGERRTDKSMSskfqgvetPSQSRYVG 359
Cdd:cd14563   87 FAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGIGLW--------PSHRRYIG 158


                 .
gi 528492142 360 Y 360
Cdd:cd14563  159 Y 159
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
206-362 2.65e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 64.22  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 206 VTERVIAMSFPSSGKQALYRNPIREVVrfldtkhmdhykvfNLCSEKGYDPKFF---HYRVERVMIDDHNVPSLDDMLRY 282
Cdd:COG2453    4 IPGLLAGGPLPGGGEADLKREGIDAVV--------------SLTEEEELLLGLLeeaGLEYLHLPIPDFGAPDDEQLQEA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 283 TACVRDWMAADSRnvIAIHCKGGKGRTGTMVCTWLIDSDQfeSAQESLDYFGERRTdksmsskfQGVETPSQSRYVGYYE 362
Cdd:COG2453   70 VDFIDEALREGKK--VLVHCRGGIGRTGTVAAAYLVLLGL--SAEEALARVRAARP--------GAVETPAQRAFLERFA 137
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 55-175 3.08e-11

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 63.44  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142   55 SFGFRVFGLVLIILDIIMVIVDlSLSEKSRDVGGALETVSLVISFFFLIDVLLRVYVEGFKV-YFSSKLNIVDaCIVVIT 133
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALE-TYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKKrYFRSPWNILD-FVVVLP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 528492142  134 LVVTMIYAFSDfsgaslIPRVVTFLRSLRILilvRIFRLASQ 175
Cdd:pfam00520  79 SLISLVLSSVG------SLSGLRVLRLLRLL---RLLRLIRR 111
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 209-328 2.52e-10

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: 58.44  E-value: 2.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 209 RVIAMSFPSSGK--QALYRNPIREVVrfldtkhmdhykvfNLCSEKGYDPKFFHYRV--ERVMIDDHNVPSLDDMLRYTA 284
Cdd:cd14504    8 KLAGMAFPRLPEhyAYLNENGIRHVV--------------TLTEEPPPEHSDTCPGLryHHIPIEDYTPPTLEQIDEFLD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 528492142 285 CVRDwmaADSRN-VIAIHCKGGKGRTGTMVCTWLIDSdQFESAQE 328
Cdd:cd14504   74 IVEE---ANAKNeAVLVHCLAGKGRTGTMLACYLVKT-GKISAVD 114
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
270-365 4.20e-09

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 53.90  E-value: 4.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142   270 DHNVP-SLDDMLRYTACVRDWM-AADSRNVIAIHCKGGKGRTGTMVCTWLIdSDQFESAQESLDYFGerrTDKSM-SSKF 346
Cdd:smart00404  12 DHGVPeSPDSILELLRAVKKNLnQSESSGPVVVHCSAGVGRTGTFVAIDIL-LQQLEAEAGEVDIFD---TVKELrSQRP 87

                           90
                   ....*....|....*....
gi 528492142   347 QGVETPSQSRYVgYYEIMK 365
Cdd:smart00404  88 GMVQTEEQYLFL-YRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 270-365 4.20e-09

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 53.90  E-value: 4.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142   270 DHNVP-SLDDMLRYTACVRDWM-AADSRNVIAIHCKGGKGRTGTMVCTWLIdSDQFESAQESLDYFGerrTDKSM-SSKF 346
Cdd:smart00012  12 DHGVPeSPDSILELLRAVKKNLnQSESSGPVVVHCSAGVGRTGTFVAIDIL-LQQLEAEAGEVDIFD---TVKELrSQRP 87

                           90
                   ....*....|....*....
gi 528492142   347 QGVETPSQSRYVgYYEIMK 365
Cdd:smart00012  88 GMVQTEEQYLFL-YRALLE 105
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 249-337 6.72e-07

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: 49.20  E-value: 6.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 249 CSEKGYDPKFFH---YRVERVMIDDHNVPSLDDMLRYTACVRD--WMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQF 323
Cdd:cd17665   62 NTTRYYDPRDLTnhgVYYKKITCPGHQVPDDKTIQSFKDAVKDflEKNKDNDKLIGVHCTHGLNRTGYLICRYLIDVDGM 141

                         90
                 ....*....|....
gi 528492142 324 eSAQESLDYFGERR 337
Cdd:cd17665  142 -SPDDAIEAFEQAR 154
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 206-358 2.01e-06

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: 46.57  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 206 VTERVIAMSFPSSgkqalyrnPIREVVRFLDTKHMDHykVFNLCsekgydpkffhyrvervmiddhnvpslDDMLRYTAC 285
Cdd:cd14494    5 DPLRLIAGALPLS--------PLEADSRFLKQLGVTT--IVDLT---------------------------LAMVDRFLE 47

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528492142 286 VRDwmAADSRN-VIAIHCKGGKGRTGTMVCTWLIdSDQFESAQESLDYFGERRTDKSmsskfqgVETPSQSRYV 358
Cdd:cd14494   48 VLD--QAEKPGePVLVHCKAGVGRTGTLVACYLV-LLGGMSAEEAVRIVRLIRPGGI-------PQTIEQLDFL 111
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 251-318 6.20e-06

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: 46.68  E-value: 6.20e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528492142 251 EKGYDPKFF------HYRvervMI-DDHNVPSLDDMLRYTAcvrdwMAADSRNVIAIHCKGGKGRTGTMVCTWLI 318
Cdd:cd14499   67 KKLYDAKRFtdagirHYD----LYfPDGSTPSDDIVKKFLD-----ICENEKGAIAVHCKAGLGRTGTLIACYLM 132
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 245-337 2.18e-05

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


Pssm-ID: 350376 [Multi-domain]  Cd Length: 136  Bit Score: 44.19  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 245 VFNLCSEKGYDPKFFHYRVERVMidDHNVPSLDDMLRytACvrDWM---AADSRNVIaIHCKGGKGRTGTMVCTWLIDSD 321
Cdd:cd14527   30 VLDLTAELPRPRKRQAYRCVPLL--DLVAPTPEQLER--AV--AWIeelRAQGGPVL-VHCALGYGRSATVVAAWLLAYG 102

                         90
                 ....*....|....*.
gi 528492142 322 QFESAQESLDYFGERR 337
Cdd:cd14527  103 RAKSVAEAEALIRAAR 118
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
215-318 2.18e-05

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 46.11  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142   215 FPSSGKQALYRNPIRevVRFLDTKHMDHY--KVFNLCSEKGYDPKF---FHYrvervmID--DHNVP-SLDDMLRYTACV 286
Cdd:smart00194 115 WPDEEGEPLTYGDIT--VTLKSVEKVDDYtiRTLEVTNTGCSETRTvthYHY------TNwpDHGVPeSPESILDLIRAV 186

                           90       100       110
                   ....*....|....*....|....*....|..
gi 528492142   287 RDWMAADSRNVIaIHCKGGKGRTGTMVCTWLI 318
Cdd:smart00194 187 RKSQSTSTGPIV-VHCSAGVGRTGTFIAIDIL 217
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 206-330 6.17e-05

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: 43.02  E-value: 6.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 206 VTERVI--AMSFPSSGKQALYRnpirEVVRFldtkhmdhykVFNLCSEkgYDPKFF-----HYRVERV------MIDDHN 272
Cdd:cd14524    5 IDDTVIlgALPFRSMTVALVAK----ENVRG----------VITMNEE--YETRFFcnskeEWKALGVeqlrlpTVDFTG 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 273 VPSLDDMLRYTACVRDWMAADSRnvIAIHCKGGKGRTGTMVCTWLIDSDQ--FESAQESL 330
Cdd:cd14524   69 VPSLEDLEKGVDFILKHREKGKS--VYVHCKAGRGRSATIVACYLIQHKGwsPEEAQEFL 126
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 234-337 8.66e-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: 42.25  E-value: 8.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142  234 FLDTKHMDHykVFNLCSEKGYDPKFFHY-RVErvMIDDHNVPSLDDMLRYTACVRDwmAADSRNVIAIHCKGGKGRTGTM 312
Cdd:pfam00782  13 FLSKLGITA--VINVTREVDLYNSGILYlRIP--VEDNHETNISKYLEEAVEFIDD--ARQKGGKVLVHCQAGISRSATL 86

                          90       100
                  ....*....|....*....|....*
gi 528492142  313 VCTWLIDSDQFeSAQESLDYFGERR 337
Cdd:pfam00782  87 IIAYLMKTRNL-SLNEAYSFVKERR 110
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 270-334 1.67e-04

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 43.11  E-value: 1.67e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528492142 270 DHNVPSL-DDMLRYTACVRDWMAADSRNVIaIHCKGGKGRTGTMVC-TWLIdsDQFESaQESLDYFG 334
Cdd:cd14548  136 DHGVPEApDSLLRFVRLVRDYIKQEKGPTI-VHCSAGVGRTGTFIAlDRLL--QQIES-EDYVDIFG 198
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 246-334 2.72e-04

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 42.60  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 246 FNLCSEKGYDP----KFFHYRVervmIDDHNVP-SLDDMLRYTACVRDWM-AADSRNVIAIHCKGGKGRTGTMVctwLID 319
Cdd:cd14617  116 FKICSEEQLDAprlvRHFHYTV----WPDHGVPeTTQSLIQFVRTVRDYInRTPGSGPTVVHCSAGVGRTGTFI---ALD 188

                         90
                 ....*....|....*..
gi 528492142 320 S--DQFESaQESLDYFG 334
Cdd:cd14617  189 RilQQLDS-KDSVDIYG 204
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 215-314 3.36e-04

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: 41.89  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 215 FPSSGKQALYRNPIRevVRFLDTKHMDHYKV--FNLCSEKGYDPKF---FHYRvervMIDDHNVPS-LDDMLRYTACVRD 288
Cdd:cd00047   60 WPEEGGKPLEYGDIT--VTLVSEEELSDYTIrtLELSPKGCSESREvthLHYT----GWPDHGVPSsPEDLLALVRRVRK 133

                         90       100
                 ....*....|....*....|....*.
gi 528492142 289 WMAADSRNVIaIHCKGGKGRTGTMVC 314
Cdd:cd00047  134 EARKPNGPIV-VHCSAGVGRTGTFIA 158
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 204-337 3.46e-04

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: 41.95  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 204 TYVTERVIAMSFPSsgkqalyrnpirevvrfldTKHMDHYK------------VFNL--------CSEKGYDPKFFHYRV 263
Cdd:cd14506    9 SWITDDILAMARPS-------------------TELIDKYGiieqfkekgiktVINLqepgehasCGPGLEPESGFSYLP 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 264 ERVM----------IDDHNVPSLDDMLRYTACVRdwMAADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQFeSAQESLDYF 333
Cdd:cd14506   70 EAFMragiyfynfgWKDYGVPSLTTILDIVKVMA--FALQEGGKVAVHCHAGLGRTGVLIACYLVYALRM-SADQAIRLV 146


                 ....
gi 528492142 334 GERR 337
Cdd:cd14506  147 RSKR 150
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 221-311 4.31e-04

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: 41.09  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 221 QALYRNPIREVVRFLDTKHMDHYKVFNL---CSEKGYdpKFFHYRVErvmidDHNVPsldDMLRYTACVRDWMAA---DS 294
Cdd:cd14505   37 EELKDQGVDDVVTLCTDGELEELGVPDLleqYQQAGI--TWHHLPIP-----DGGVP---SDIAQWQELLEELLSaleNG 106

                         90
                 ....*....|....*..
gi 528492142 295 RNVIaIHCKGGKGRTGT 311
Cdd:cd14505  107 KKVL-IHCKGGLGRTGL 122
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 273-350 5.76e-04

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: 40.44  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 273 VPSLDDMLRYTACVRDwmaADSRNVIAIHCKGGKGRTGTMVCTWLI-----DSDQFESAQESLDYFGERRTDKSMSSKFQ 347
Cdd:cd14529   70 RPTESDVQSFLLIMDL---KLAPGPVLIHCKHGKDRTGLVSALYRIvyggsKEEANEDYRLSNRHLEGLRSGIALDSKGG 146


                 ...
gi 528492142 348 GVE 350
Cdd:cd14529  147 VKG 149
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 270-358 5.95e-04

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: 41.47  E-value: 5.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 270 DHNVPS-LDDMLRYTACVRDWMAADSRNVIaIHCKGGKGRTG------TMVCtwLIDSDQfesAQESLDYFGERRTDKSM 342
Cdd:cd14601  118 DHGVPDdSSDFLDFVCLVRNKRAGKDEPVV-VHCSAGIGRTGvlitmeTAMC--LIECNQ---PVYPLDIVRTMRDQRAM 191

                         90
                 ....*....|....*.
gi 528492142 343 SskfqgVETPSQSRYV 358
Cdd:cd14601  192 M-----IQTPSQYRFV 202
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 95-155 9.51e-04

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 40.72  E-value: 9.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528492142   95 LVISFFFLIDVLLRVYVEGFKV------YFSSKLNIVDACIVVITLVVTMIYAFSDFSGASLIPRVV 155
Cdd:pfam08016  11 LLCEIVFVVFFLYFVVEEILKIrkhrpsYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVE 77
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 231-320 1.01e-03

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 40.41  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 231 VVRFLDTKHMDHYKVFNLCSEKGYDPKFFHYRVERVMID-------DHNVPslDDMLRYTACVRDWMAADSRNV--IAIH 301
Cdd:cd14549   72 QVTLLSTEVLATYTVRTFSLKNLKLKKVKGRSSERVVYQyhytqwpDHGVP--DYTLPVLSFVRKSSAANPPGAgpIVVH 149

                         90
                 ....*....|....*....
gi 528492142 302 CKGGKGRTGTMVctwLIDS 320
Cdd:cd14549  150 CSAGVGRTGTYI---VIDS 165
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 259-319 1.07e-03

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


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 40.48  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528492142 259 FHYrverVMIDDHNVP-SLDDMLRYTACVRDWMAADSRNVIaIHCKGGKGRTGTmVCTwlID 319
Cdd:cd14542  106 FHY----TAWPDHGVPsSVDPILDLVRLVRDYQGSEDVPIC-VHCSAGCGRTGT-ICA--ID 159
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 270-334 1.67e-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: 40.18  E-value: 1.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528492142 270 DHNVPSLDDML-RYTACVRDWMAADSRNV-IAIHCKGGKGRTGTMVCtwlIDS--DQFESaQESLDYFG 334
Cdd:cd14615  137 DHGVPETTDLLiNFRHLVREYMKQNPPNSpILVHCSAGVGRTGTFIA---IDRliYQIEN-ENVVDVYG 201
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 231-315 2.73e-03

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


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 39.30  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142 231 VVRFLDTKHMDHYKVFNLCSEKGYDPKF-FHYRVERVMidDHNVP-SLDDMLRYTACVRDW-MAADSRNVIAIHCKGGKG 307
Cdd:cd14547   98 EVTVQSVKETDGYTVRKLTLKYGGEKRYlKHYWYTSWP--DHKTPeAAQPLLSLVQEVEEArQTEPHRGPIVVHCSAGIG 175


                 ....*...
gi 528492142 308 RTGTMVCT 315
Cdd:cd14547  176 RTGCFIAT 183
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
245-337 2.85e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 38.03  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528492142   245 VFNLCSEKgYDPKFFHYRVERVMIDDHnvpSLDDMLRYTACVRDWM--AADSRNVIAIHCKGGKGRTGTMVCTWLIDSDQ 322
Cdd:smart00195  30 VINVTNEV-PNYNGSDFTYLGVPIDDN---TETKISPYFPEAVEFIedAESKGGKVLVHCQAGVSRSATLIIAYLMKTRN 105

                           90
                   ....*....|....*
gi 528492142   323 FeSAQESLDYFGERR 337
Cdd:smart00195 106 M-SLNDAYDFVKDRR 119
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 270-314 5.45e-03

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: 38.12  E-value: 5.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 528492142 270 DHNVP-SLDDMLRYTACVRdwMAADSRNVIaIHCKGGKGRTGTMVC 314
Cdd:cd14538  117 DHGTPqSADPLLRFIRYMR--RIHNSGPIV-VHCSAGIGRTGVLIT 159
 
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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