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Conserved domains on  [gi|269784764|ref|NP_954866|]
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transmembrane phosphatase with tensin homology [Mus musculus]

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 ...
 344-520 9.23e-123

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: 361.68  E-value: 9.23e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 344 SGNKRRYKKDGFDLDLTYVTERIIAMSFPSSGRESFYRNPIKEVVRFLDTKHPNHYQVYNLCSERAYDPKHFHYRVRRIM 423
Cdd:cd14510    1 SENKRRYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLCSERGYDPKYFHNRVERVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 424 IDDHNVPTLEEMLLFSKEVNNWMAQDPENVVAIHCKGGKGRTGTMVCACLIASEIVLNAKESLYFFGERRTDKSNSSKFQ 503
Cdd:cd14510   81 IDDHNVPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSSKFQ 160

                        170
                 ....*....|....*..
gi 269784764 504 GIETPSQNRYVKYFEKL 520
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 ...
 529-663 9.58e-40

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: 142.42  E-value: 9.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764  529 PPKKVLVIKRLVVYSIHGVGKGDGSDLEVQIIMWQETVFSFCNSRNCMIFHDpeTDRAIINVFHCPALYDDVKVKFLSPN 608
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVFSTSGKYKKLKEYQ--QDDCVILFPKGIPVQGDVLVEFYHKG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 269784764  609 LPKYYDDCPFFFWFHTSFIKNNRLYLPRNELDNTHKPKTWKIYGEKFAVEVDFGE 663
Cdd:pfam10409  79 SDLLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDKKDKRFPKDFKVELLFSE 133
 
Name Accession Description Interval E-value
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 344-520 9.23e-123

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: 361.68  E-value: 9.23e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 344 SGNKRRYKKDGFDLDLTYVTERIIAMSFPSSGRESFYRNPIKEVVRFLDTKHPNHYQVYNLCSERAYDPKHFHYRVRRIM 423
Cdd:cd14510    1 SENKRRYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLCSERGYDPKYFHNRVERVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 424 IDDHNVPTLEEMLLFSKEVNNWMAQDPENVVAIHCKGGKGRTGTMVCACLIASEIVLNAKESLYFFGERRTDKSNSSKFQ 503
Cdd:cd14510   81 IDDHNVPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSSKFQ 160

                        170
                 ....*....|....*..
gi 269784764 504 GIETPSQNRYVKYFEKL 520
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 ...
 529-663 9.58e-40

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: 142.42  E-value: 9.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764  529 PPKKVLVIKRLVVYSIHGVGKGDGSDLEVQIIMWQETVFSFCNSRNCMIFHDpeTDRAIINVFHCPALYDDVKVKFLSPN 608
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVFSTSGKYKKLKEYQ--QDDCVILFPKGIPVQGDVLVEFYHKG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 269784764  609 LPKYYDDCPFFFWFHTSFIKNNRLYLPRNELDNTHKPKTWKIYGEKFAVEVDFGE 663
Cdd:pfam10409  79 SDLLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDKKDKRFPKDFKVELLFSE 133
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
362-519 1.05e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 65.76  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 362 VTERIIAMSFPSSGRESFYRNPIKEVVrfldtkhpnhyqvyNLCSERAYDPKHF---HYRVRRIMIDDHNVPTLEEMLLF 438
Cdd:COG2453    4 IPGLLAGGPLPGGGEADLKREGIDAVV--------------SLTEEEELLLGLLeeaGLEYLHLPIPDFGAPDDEQLQEA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 439 SKEVNNWMAQDpeNVVAIHCKGGKGRTGTMVCACLIASEivLNAKESLYFFGERRTdksnsskfQGIETPSQNRYVKYFE 518
Cdd:COG2453   70 VDFIDEALREG--KKVLVHCRGGIGRTGTVAAAYLVLLG--LSAEEALARVRAARP--------GAVETPAQRAFLERFA 137


                 .
gi 269784764 519 K 519
Cdd:COG2453  138 K 138
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
413-478 1.51e-07

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 50.05  E-value: 1.51e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 269784764   413 KHFHYRVrrimIDDHNVPTL-EEMLLFSKEVNNWMAQDPEN-VVAIHCKGGKGRTGTMVCACLIASEI 478
Cdd:smart00404   3 KHYHYTG----WPDHGVPESpDSILELLRAVKKNLNQSESSgPVVVHCSAGVGRTGTFVAIDILLQQL 66
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
400-480 4.80e-04

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 42.23  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764  400 QVYNLCSERAYDPKHFHYrvrrimID--DHNVP-TLEEMLLFSKEVNNWMAQDPENVVAIHCKGGKGRTGTmvcacLIAS 476
Cdd:pfam00102 121 EVSNGGSEETRTVKHFHY------TGwpDHGVPeSPNSLLDLLRKVRKSSLDGRSGPIVVHCSAGIGRTGT-----FIAI 189


                  ....
gi 269784764  477 EIVL 480
Cdd:pfam00102 190 DIAL 193
 
Name Accession Description Interval E-value
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 344-520 9.23e-123

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: 361.68  E-value: 9.23e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 344 SGNKRRYKKDGFDLDLTYVTERIIAMSFPSSGRESFYRNPIKEVVRFLDTKHPNHYQVYNLCSERAYDPKHFHYRVRRIM 423
Cdd:cd14510    1 SENKRRYQKDGFDLDLTYVTDRVIAMSFPSSGKQAFYRNPIEEVVRFLDTKHPDHYKVYNLCSERGYDPKYFHNRVERVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 424 IDDHNVPTLEEMLLFSKEVNNWMAQDPENVVAIHCKGGKGRTGTMVCACLIASEIVLNAKESLYFFGERRTDKSNSSKFQ 503
Cdd:cd14510   81 IDDHNVPTLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERRTDKSVSSKFQ 160

                        170
                 ....*....|....*..
gi 269784764 504 GIETPSQNRYVKYFEKL 520
Cdd:cd14510  161 GVETPSQSRYVGYFEKL 177
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 358-520 5.19e-76

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: 240.18  E-value: 5.19e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 358 DLTYVTERIIAMSFPSSGRESFYRNPIKEVVRFLDTKHPNHYQVYNLCSERAYDPKHFHYRVRRIMIDDHNVPTLEEMLL 437
Cdd:cd14509    1 DLTYITPNIIAMGFPAEGVEGVYRNPIDDVQRFLETKHKGHYKVYNLCSERSYDPSKFNGRVAEYPFDDHNPPPLELIKP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 438 FSKEVNNWMAQDPENVVAIHCKGGKGRTGTMVCACLIASEIVLNAKESLYFFGERRTDKSnsskfQGIETPSQNRYVKYF 517
Cdd:cd14509   81 FCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKEALDFYGAKRTKNK-----KGVTIPSQRRYVYYY 155


                 ...
gi 269784764 518 EKL 520
Cdd:cd14509  156 SRL 158
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 358-520 2.38e-62

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: 204.35  E-value: 2.38e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 358 DLTYVTERIIAMSFPSSG-RESFYRNPIKEVVRFLDTKHPNHYQVYNLCSERAYDPKHFHYRVRRIMIDDHNVPTLEEML 436
Cdd:cd14497    1 DLSYITPRIIAMSFPATGyPESLYRNSIDDVANFLNTHHPDHYMIFNLSEEEYDDDSKFEGRVLHYGFPDHHPPPLGLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 437 LFSKEVNNWMAQDPENVVAIHCKGGKGRTGTMVCACLIASEIVLNAKESLYFFGERRTDKsnssKFQGIETPSQNRYVKY 516
Cdd:cd14497   81 EIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICAYLLYYGQYSTADEALEYFAKKRFKE----GLPGVTIPSQLRYLQY 156


                 ....
gi 269784764 517 FEKL 520
Cdd:cd14497  157 FERL 160
PTP_tensin cd14508
protein tyrosine phosphatase-like domain of tensins; The tensin family of intracellular ...
 358-520 7.08e-40

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: 143.68  E-value: 7.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 358 DLTYVTERIIAMSFPSSGRESFYRNPIKEVVRFLDTKHPNHYQVYNLcSERAYDPKHFHYRVRRIMIDDHNVPTLEEMLL 437
Cdd:cd14508    1 DLTYITERIIALSFPSTCSEQTYRHNLREAAHLLQSKHGDNYMVFNL-SERRHDLRSLNPKVLDFGWPELHAPPLEKLCS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 438 FSKEVNNWMAQDPENVVAIHCKGGKGRTGTMVCACLIASEIVLNAKESLYFFGERRTdksNSSKFQGIETPSQNRYVKYF 517
Cdd:cd14508   80 ICKNMDSWLNADPQNVVVLHCKGGKGRLGVVVSAYMHYSKISATADQALDRFAMKRF---YDDKVGPLGQPSQKRYVGYF 156


                 ...
gi 269784764 518 EKL 520
Cdd:cd14508  157 SGL 159
PTEN_C2 pfam10409
C2 domain of PTEN tumour-suppressor protein; This is the C2 domain-like domain, in greek key ...
 529-663 9.58e-40

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: 142.42  E-value: 9.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764  529 PPKKVLVIKRLVVYSIHGVGKGDGSDLEVQIIMWQETVFSFCNSRNCMIFHDpeTDRAIINVFHCPALYDDVKVKFLSPN 608
Cdd:pfam10409   1 PPPKPLTLHSIILHGIPNFKSGGGCRPYIRIYQNKKKVFSTSGKYKKLKEYQ--QDDCVILFPKGIPVQGDVLVEFYHKG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 269784764  609 LPKYYDDCPFFFWFHTSFIKNNRLYLPRNELDNTHKPKTWKIYGEKFAVEVDFGE 663
Cdd:pfam10409  79 SDLLSEEKMFRFWFNTSFIEDNTLTLPKNELDKADKDKKDKRFPKDFKVELLFSE 133
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 356-517 2.70e-39

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: 142.11  E-value: 2.70e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 356 DLDLTYVTERIIAMSFPSSGRESFYR-NPIKEVVRFLDTKHPNHYQVYNLcSERAYDPKHFHYRVRRIMIDDHNVPTLEE 434
Cdd:cd14511    8 DLDISYITSRIIVMPFPAEGIESTYRkNNIEDVRAFLDSRHPQKYSVYNL-SPRSYPTLRLPSRVVECSWPYRRAPSLHA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 435 MLLFSKEVNNWMAQDPENVVAIHCKGGKGRTGTMVCACLIASEIVLNAKESLYFFGERRTdksnsskfqGIE-TPSQNRY 513
Cdd:cd14511   87 LYALCRDIYQWLNKDPKNVIVIHCTDGKAASATVVCALLVYCGLFKTPEDALQMFAVKRC---------PPGlSPSELRY 157


                 ....
gi 269784764 514 VKYF 517
Cdd:cd14511  158 LYYF 161
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 358-520 1.06e-35

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: 132.03  E-value: 1.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 358 DLTYVTERIIAMSFPSSGRESFYRNPIKEVVRFLDTKHPNHYQVYNLcSERAYDPKHFHYRVRRIMIDDHNVPTLEEMLL 437
Cdd:cd14560    1 DLVYITERIISVSFPSTAEEPSFRSNLKEVAQMLKSKHGDNYLLFNL-SERRHDISKLHPKVLDFGWPDLHAPALEKICS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 438 FSKEVNNWMAQDPENVVAIHCKGGKGRTGTMVCACLIASEIVLNAKESLYFFGERRTdksNSSKFQGIETPSQNRYVKYF 517
Cdd:cd14560   80 ICKAMDTWLNADPHNVVVIHNKGNRGRTGVVIAAYMHYSNISASADQALDRFAMKRF---YEDKVVPVGQPSQKRYVHYF 156


                 ...
gi 269784764 518 EKL 520
Cdd:cd14560  157 SGL 159
PTP_GAK cd14564
protein tyrosine phosphatase-like domain of cyclin-G-associated kinase; cyclin-G-associated ...
 356-516 1.93e-35

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: 131.56  E-value: 1.93e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 356 DLDLTYVTERIIAMSFPSSGRESFYRNPIKEVVRFLDTKHPNHYQVYNLCsERAYDPKHFHYRVRRIMIDDHNVPTLEEM 435
Cdd:cd14564    8 DLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDSRHPGHYAVYNLS-QRTYRPSRFHNRVSECGWPARRAPNLQNL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 436 LLFSKEVNNWMAQDPENVVAIHCKGGKGRTGTMVCACLIASEIVLNAKESLYFFGERRTDKsnsskfqGIeTPSQNRYVK 515
Cdd:cd14564   87 YSICKNMHLWLKQDQKNICIVHCLDGRAASAVVVCSFLCFCRLFTTAEAAVYMFSMKRCPP-------GI-WPSHKRYIE 158


                 .
gi 269784764 516 Y 516
Cdd:cd14564  159 Y 159
PTP_tensin-3 cd14561
protein tyrosine phosphatase-like domain of tensin-3; Tensin-3 (TNS3) is also called ...
 358-520 3.97e-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: 3.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 358 DLTYVTERIIAMSFPSSGRESFYRNPIKEVVRFLDTKHPNHYQVYNLcSERAYDPKHFHYRVRRIMIDDHNVPTLEEMLL 437
Cdd:cd14561    1 DLTYITERIIAVSFPADCSEETYLHNLQDVTRMLKSKHGDNYLVLNL-SEKRYELTKLNPKIMDVGWPDLHAPPLDKMCT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 438 FSKEVNNWMAQDPENVVAIHCKGGKGRTGTMVCACLIASEIVLNAKESLYFFGERrtdKSNSSKFQGIETPSQNRYVKYF 517
Cdd:cd14561   80 ICKAMESWLNSDPLHVVVIHCRGGKGRIGVVISSYMHFTNVSASADQALDRFAMK---KFYDDKVSALMQPSQKRYVQFL 156


                 ...
gi 269784764 518 EKL 520
Cdd:cd14561  157 SGL 159
PTP_tensin-2 cd14562
protein tyrosine phosphatase-like domain of tensin-2; Tensin-2 (TNS2) is also called ...
 358-520 4.72e-32

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: 121.59  E-value: 4.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 358 DLTYVTERIIAMSFPSSGRESFYRNPIKEVVRFLDTKHPNHYQVYNLcSERAYDPKHFHYRVRRIMIDDHNVPTLEEMLL 437
Cdd:cd14562    1 DLTYITERIISVFFPPALEEQRYRGNLREVAQMLKSKHEDKYLLFNL-SEKRHDITRLNPKVQDFGWPDLHAPPLDKICS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 438 FSKEVNNWMAQDPENVVAIHCKGGKGRTGTMVCACLIASEIVLNAKESLYFFGERR--TDKSNSSKfqgieTPSQNRYVK 515
Cdd:cd14562   80 ICKAMETWLNADPQHVVVLHCKGNKGKTGVIVAAYMHYSKISAGADQALSTLAMRKfcEDKVATSL-----QPSQRRYIS 154


                 ....*
gi 269784764 516 YFEKL 520
Cdd:cd14562  155 YFGGL 159
PTP_auxilin_N cd14563
N-terminal protein tyrosine phosphatase-like domain of auxilin; Auxilin, also called auxilin-1 ...
 356-516 3.09e-29

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: 113.82  E-value: 3.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 356 DLDLTYVTERIIAMSFPSSGRESFYRNPIKEVVRFLDTKHPNHYQVYNLcSERAYDPKHFHYRVRRIMIDDHNVPTLEEM 435
Cdd:cd14563    8 ELDISYITSRIIVMSYPAEGVELGFRNHIEDVRSFLDSRHLDHYTVFNL-SQKSYRSAKFHNRVSECSWPVRQAPSLHNL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 436 LLFSKEVNNWMAQDPENVVAIHCKGGKGRTGTMVCACLIASEIVLNAKESLYFFGERRTDKsnsskfqgIETPSQNRYVK 515
Cdd:cd14563   87 FAVCKNMHNWLQQNPKNVCVIHCMDGRAASAVLVSAMFCFCHLFSNPVPAMQLLNAKRPGI--------GLWPSHRRYIG 158


                 .
gi 269784764 516 Y 516
Cdd:cd14563  159 Y 159
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
362-519 1.05e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 65.76  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 362 VTERIIAMSFPSSGRESFYRNPIKEVVrfldtkhpnhyqvyNLCSERAYDPKHF---HYRVRRIMIDDHNVPTLEEMLLF 438
Cdd:COG2453    4 IPGLLAGGPLPGGGEADLKREGIDAVV--------------SLTEEEELLLGLLeeaGLEYLHLPIPDFGAPDDEQLQEA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 439 SKEVNNWMAQDpeNVVAIHCKGGKGRTGTMVCACLIASEivLNAKESLYFFGERRTdksnsskfQGIETPSQNRYVKYFE 518
Cdd:COG2453   70 VDFIDEALREG--KKVLVHCRGGIGRTGTVAAAYLVLLG--LSAEEALARVRAARP--------GAVETPAQRAFLERFA 137


                 .
gi 269784764 519 K 519
Cdd:COG2453  138 K 138
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 365-475 4.26e-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: 52.66  E-value: 4.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 365 RIIAMSFPSSGRESFY--RNPIKEVVRFldTKHPNHYQVYNlcseraydpkHFHYRVRRIMIDDHNVPTLEEMLLFSKEV 442
Cdd:cd14504    8 KLAGMAFPRLPEHYAYlnENGIRHVVTL--TEEPPPEHSDT----------CPGLRYHHIPIEDYTPPTLEQIDEFLDIV 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 269784764 443 NnwmaQDPEN--VVAIHCKGGKGRTGTMVcACLIA 475
Cdd:cd14504   76 E----EANAKneAVLVHCLAGKGRTGTML-ACYLV 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
413-478 1.51e-07

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 50.05  E-value: 1.51e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 269784764   413 KHFHYRVrrimIDDHNVPTL-EEMLLFSKEVNNWMAQDPEN-VVAIHCKGGKGRTGTMVCACLIASEI 478
Cdd:smart00404   3 KHYHYTG----WPDHGVPESpDSILELLRAVKKNLNQSESSgPVVVHCSAGVGRTGTFVAIDILLQQL 66
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 413-478 1.51e-07

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: 50.05  E-value: 1.51e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 269784764   413 KHFHYRVrrimIDDHNVPTL-EEMLLFSKEVNNWMAQDPEN-VVAIHCKGGKGRTGTMVCACLIASEI 478
Cdd:smart00012   3 KHYHYTG----WPDHGVPESpDSILELLRAVKKNLNQSESSgPVVVHCSAGVGRTGTFVAIDILLQQL 66
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 362-474 1.54e-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: 47.34  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 362 VTERIIAMSFPSSGRESFyrnpikevVRFLDTKHpnhyqvynlcseraydpkHFHYrvrrIMIDDHNVptlEEMLLFSKE 441
Cdd:cd14494    5 DPLRLIAGALPLSPLEAD--------SRFLKQLG------------------VTTI----VDLTLAMV---DRFLEVLDQ 51

                         90       100       110
                 ....*....|....*....|....*....|...
gi 269784764 442 VNNwmaqdPENVVAIHCKGGKGRTGTMVCACLI 474
Cdd:cd14494   52 AEK-----PGEPVLVHCKAGVGRTGTLVACYLV 79
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 418-473 5.89e-06

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: 46.87  E-value: 5.89e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 269784764 418 RVRRIMIDDHNVPTLEEmllFSKEVNNWMAQ---DPENVVaIHCKGGKGRTGTmVCACL 473
Cdd:cd14505   74 TWHHLPIPDGGVPSDIA---QWQELLEELLSaleNGKKVL-IHCKGGLGRTGL-IAACL 127
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
371-478 1.36e-05

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 47.27  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764   371 FPSSGRESFYRNPIKevVRFLDTKHPNHYQVYNLCSERAYDP-----KHFHYrvrrimID--DHNVP-TLEEMLLFSKEV 442
Cdd:smart00194 115 WPDEEGEPLTYGDIT--VTLKSVEKVDDYTIRTLEVTNTGCSetrtvTHYHY------TNwpDHGVPeSPESILDLIRAV 186

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 269784764   443 NNWMAQDPENVVaIHCKGGKGRTGTMVCACLIASEI 478
Cdd:smart00194 187 RKSQSTSTGPIV-VHCSAGVGRTGTFIAIDILLQQL 221
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 430-474 1.53e-05

N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as RNA guanylyltransferase and 5'-phosphatase (RNGTT) or mammalian mRNA capping enzyme (Mce1) in mammals, is a bifunctional enzyme that catalyzes the first two steps of cap formation: (1) by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end using the polynucleotide 5'-phosphatase activity (EC 3.1.3.33) of the N-terminal triphosphatase domain; and (2) by transferring the GMP moiety of GTP to the 5'-diphosphate terminus through the C-terminal mRNA guanylyltransferase domain (EC 2.7.7.50). The enzyme is also referred to as CEL-1 in Caenorhabditis elegans.


Pssm-ID: 350502  Cd Length: 167  Bit Score: 45.75  E-value: 1.53e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 269784764 430 PTLEEMLLFSKEVNNWMAQDPENVVAIHCKGGKGRTGTMVCACLI 474
Cdd:cd17664   90 PSPEQTETFIRLCENFIEKNPLELIGVHCTHGFNRTGFLICAYLV 134
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 405-474 1.88e-05

RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes baculovirus RNA 5'-triphosphatase, dual specificity protein phosphatase 11 (DUSP11), and the RNA triphosphatase domains of metazoan and plant mRNA capping enzymes. RNA/polynucleotide 5'-triphosphatase (EC 3.1.3.33) catalyzes the removal of the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end. mRNA capping enzyme is a bifunctional enzyme that catalyzes the first two steps of cap formation. DUSP11 has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity.


Pssm-ID: 350352 [Multi-domain]  Cd Length: 167  Bit Score: 45.34  E-value: 1.88e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784764 405 CSERAYDPKHFHYRVRR---IMIDDHNVPTLEEMLLFSKEVNN-WMAQDPENVVAIHCKGGKGRTGTMVCACLI 474
Cdd:cd14502   61 NTDRYYDPNDLDDDGYVyykKVCVRKEPPDAEEVNKFIELVDKfLAEDNPDKLIAVHCTHGFNRTGFMIVSYLV 134
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 402-490 2.09e-05

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: 46.45  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 402 YNLCSERAYDP----KHFHYRVrrimIDDHNVP-TLEEMLLFSKEVNNWMAQDPEN-VVAIHCKGGKGRTGTMVCACLIA 475
Cdd:cd14617  116 FKICSEEQLDAprlvRHFHYTV----WPDHGVPeTTQSLIQFVRTVRDYINRTPGSgPTVVHCSAGVGRTGTFIALDRIL 191

                         90
                 ....*....|....*
gi 269784764 476 SEivLNAKESLYFFG 490
Cdd:cd14617  192 QQ--LDSKDSVDIYG 204
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 360-518 3.81e-05

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: 45.03  E-value: 3.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 360 TYVTERIIAMSFPSSGR-------ESFYRNPIKEVVRF-LDTKHPNHYQVYNLCSERAYDPKHFHYR---VRRIMIDDHN 428
Cdd:cd14506    9 SWITDDILAMARPSTELidkygiiEQFKEKGIKTVINLqEPGEHASCGPGLEPESGFSYLPEAFMRAgiyFYNFGWKDYG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 429 VPTLEEMLLFSKEVNnwMAQDPENVVAIHCKGGKGRTGTMVCACLIASEIVlNAKESLYFFGERRTDksnsskfqGIETP 508
Cdd:cd14506   89 VPSLTTILDIVKVMA--FALQEGGKVAVHCHAGLGRTGVLIACYLVYALRM-SADQAIRLVRSKRPN--------SIQTR 157

                        170
                 ....*....|
gi 269784764 509 SQNRYVKYFE 518
Cdd:cd14506  158 GQVLCVREFA 167
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 405-474 9.79e-05

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: 43.42  E-value: 9.79e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784764 405 CSERAYDPKHFH---YRVRRIMIDDHNVPTLEEMLLFSKEVNN--WMAQDPENVVAIHCKGGKGRTGTMVCACLI 474
Cdd:cd17665   62 NTTRYYDPRDLTnhgVYYKKITCPGHQVPDDKTIQSFKDAVKDflEKNKDNDKLIGVHCTHGLNRTGYLICRYLI 136
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 407-474 1.07e-04

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: 43.21  E-value: 1.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784764 407 ERAYDPKHF------HYRvrriMI-DDHNVPTLEEMLLFSKEVNNwmaqdPENVVAIHCKGGKGRTGTMVCACLI 474
Cdd:cd14499   67 KKLYDAKRFtdagirHYD----LYfPDGSTPSDDIVKKFLDICEN-----EKGAIAVHCKAGLGRTGTLIACYLM 132
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 371-471 1.54e-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: 43.43  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 371 FPSSGRESFYRNPIKevVRFLDTKHPNHYQVYNL------CSErAYDPKHFHYrvrrIMIDDHNVPT-LEEMLLFSKEVN 443
Cdd:cd00047   60 WPEEGGKPLEYGDIT--VTLVSEEELSDYTIRTLelspkgCSE-SREVTHLHY----TGWPDHGVPSsPEDLLALVRRVR 132

                         90       100
                 ....*....|....*....|....*...
gi 269784764 444 NWMAQDPENVVaIHCKGGKGRTGTMVCA 471
Cdd:cd00047  133 KEARKPNGPIV-VHCSAGVGRTGTFIAI 159
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 387-478 1.84e-04

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


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 43.54  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 387 VVRFLDTKHPNHYQVYNLCSERAYDPKH-FHYRVRRIMidDHNVPTLEEMLL-FSKEVNNW-MAQDPENVVAIHCKGGKG 463
Cdd:cd14547   98 EVTVQSVKETDGYTVRKLTLKYGGEKRYlKHYWYTSWP--DHKTPEAAQPLLsLVQEVEEArQTEPHRGPIVVHCSAGIG 175

                         90
                 ....*....|....*
gi 269784764 464 RTGtmvcaCLIASEI 478
Cdd:cd14547  176 RTG-----CFIATSI 185
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 401-484 2.20e-04

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: 41.88  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 401 VYNLCSERAYDPKHFHYRVRRIMidDHNVPTLEEMLLFSKEVNNWMAQdpENVVAIHCKGGKGRTGTMVCACLIASEIVL 480
Cdd:cd14527   30 VLDLTAELPRPRKRQAYRCVPLL--DLVAPTPEQLERAVAWIEELRAQ--GGPVLVHCALGYGRSATVVAAWLLAYGRAK 105


                 ....
gi 269784764 481 NAKE 484
Cdd:cd14527  106 SVAE 109
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 413-469 2.82e-04

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: 42.88  E-value: 2.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 269784764 413 KHFHYrvrrIMIDDHNVPTLEEMLL-FSKEVNNWMAQDPENV-VAIHCKGGKGRTGTMV 469
Cdd:cd14615  128 RHFHF----TSWPDHGVPETTDLLInFRHLVREYMKQNPPNSpILVHCSAGVGRTGTFI 182
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 426-514 3.78e-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: 42.24  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 426 DHNVPT-LEEMLLFSKEVNNWMAQDPENVVaIHCKGGKGRTG---TMVCA-CLIaseivlNAKESLYFFGERRTDKSNSS 500
Cdd:cd14601  118 DHGVPDdSSDFLDFVCLVRNKRAGKDEPVV-VHCSAGIGRTGvliTMETAmCLI------ECNQPVYPLDIVRTMRDQRA 190

                         90
                 ....*....|....
gi 269784764 501 KFqgIETPSQNRYV 514
Cdd:cd14601  191 MM--IQTPSQYRFV 202
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
400-480 4.80e-04

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 42.23  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764  400 QVYNLCSERAYDPKHFHYrvrrimID--DHNVP-TLEEMLLFSKEVNNWMAQDPENVVAIHCKGGKGRTGTmvcacLIAS 476
Cdd:pfam00102 121 EVSNGGSEETRTVKHFHY------TGwpDHGVPeSPNSLLDLLRKVRKSSLDGRSGPIVVHCSAGIGRTGT-----FIAI 189


                  ....
gi 269784764  477 EIVL 480
Cdd:pfam00102 190 DIAL 193
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 385-469 7.82e-04

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 41.98  E-value: 7.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 385 KEVVRFLDTKH-------PNHYQVYNLCSERAYDPKH-FHYRvrRIMIDDHNVPTLEEMLLFSkevnNWMAQDPENV-VA 455
Cdd:cd14495  117 KKVVSIPLGKDkkkspsqPKTVKVESVRTEEELVKKKgAHYV--RIAATDHVWPDDEEIDAFV----AFYRSLPADAwLH 190

                         90
                 ....*....|....*
gi 269784764 456 IHCKGGKGRTGT-MV 469
Cdd:cd14495  191 FHCRAGKGRTTTfMV 205
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 413-485 1.28e-03

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-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. PTPRH 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 localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 41.03  E-value: 1.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784764 413 KHFHYRVrrimIDDHNVP-TLEEMLLFSKEVNNWMAQDPEN-VVAIHCKGGKGRTGTmvcacLIASEIVLNAKES 485
Cdd:cd14619  130 RHFHFTA----WPDHGVPsSTDTLLAFRRLLRQWLDQTMSGgPTVVHCSAGVGRTGT-----LIALDVLLQQLQS 195
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 413-469 2.09e-03

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: 40.03  E-value: 2.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 269784764 413 KHFHYRVrrimIDDHNVPTLEEMLL-FSKEVNNWMAQDPENVVaIHCKGGKGRTGTMV 469
Cdd:cd14548  127 RQFHFTA----WPDHGVPEAPDSLLrFVRLVRDYIKQEKGPTI-VHCSAGVGRTGTFI 179
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 403-493 2.10e-03

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


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 38.68  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784764 403 NLCSER--AYDPKHFHYRvrRIMIDDHNVptlEEMLLFSKEVNNWM--AQDPENVVAIHCKGGKGRTGTMVCACLIASEI 478
Cdd:cd14498   32 NVAGEPppNKFPDGIKYL--RIPIEDSPD---EDILSHFEEAIEFIeeALKKGGKVLVHCQAGVSRSATIVIAYLMKKYG 106

                         90
                 ....*....|....*
gi 269784764 479 vLNAKESLYFFGERR 493
Cdd:cd14498  107 -WSLEEALELVKSRR 120
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 423-476 8.07e-03

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: 37.24  E-value: 8.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 269784764 423 MIDDHNVPTLEEMLLFSKEVNNWMAQDpeNVVAIHCKGGKGRTGTMVCACLIAS 476
Cdd:cd14524   63 TVDFTGVPSLEDLEKGVDFILKHREKG--KSVYVHCKAGRGRSATIVACYLIQH 114
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
405-473 8.28e-03

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 38.53  E-value: 8.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784764 405 CSERAYDPKHFHYRVRRimidDHNVPTLEEMLLFSKEVNNWM--AQDPENVVAIHCKGGKGRTGTMVcACL 473
Cdd:COG5599  162 TGQKKIEIPVLHVKNWP----DHGAISAEALKNLADLIDKKEkiKDPDKLLPVVHCRAGVGRTGTLI-ACL 227
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 413-474 8.60e-03

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 37.29  E-value: 8.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269784764  413 KHFHYRVRRIMIDDHNVPTLEE--MLLfskevnNWMAQDPE-NVVAIHCKGGKGRTGT-MVCACLI 474
Cdd:pfam14566  97 EGPGVDYRRIPITDEKAPLEEDfdALI------SIVKDAPEdTALVFNCQMGRGRTTTaMVIADLV 156
 
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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