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Conserved domains on  [gi|2462492778|ref|XP_054186006|]
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myotubularin-related protein 10 isoform X1 [Homo sapiens]

Protein Classification

protein-tyrosine phosphatase family protein; phosphatase PAP2/dual specificity phosphatase family protein( domain architecture ID 12998646)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively; bifunctional phosphatase PAP2/dual specificity phosphatase (DSP) family protein containing a C-terminal DSP domain that may dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues in target proteins, and an N-terminal PAP2 domain with similarity to yeast inositol phosphorylceramide synthase (AUR1) that catalyzes the addition of inositol phosphate to ceramide, an essential step in sphingolipid synthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 31-224 2.56e-142

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 10; Myotubularin related phosphoinositide phosphatase 10 (MTMR10) is enzymatically inactive and contains an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR10 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket.


:

Pssm-ID: 350441  Cd Length: 195  Bit Score: 407.74  E-value: 2.56e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  31 RRMPLWCWSHSNGSALVRMALIKDVLQQRKIDQRICNAITKSHPQRSDVYKSDLDKTLPNIQEVQAAFVKLKQLCVNEPF 110
Cdd:cd14593     1 RRIPLWCWNHPNGSALVRMANIKDLLQQRKIDQRICNAITRSHPLRSDVYKSDLDKTLPNIQEIQAAFVKLKQLCVNEPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 111 EETEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLVQVMLDPYFRTITGFQSLIQKE 190
Cdd:cd14593    81 EETEEKWLSSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLVQVMLDPYFRTITGFQSLIQKE 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462492778 191 WVMAGYQFLDRCNHLKRS-EKESPLFLLFLDATWQ 224
Cdd:cd14593   161 WVMAGYRFLDRCNHLKKSsKKESPLFLLFLDCVWQ 195
3-PAP pfam12578
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
 326-457 1.31e-74

Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically between 115 and 138 amino acids in length. Myotubularin is a dual-specific phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bisphosphate. 3-PAP is a catalytically inactive member of the myotubularin gene family, which coprecipitates lipid phosphatidylinositol 3-phosphate-3-phosphatase activity from lysates of human platelets.


:

Pssm-ID: 463634  Cd Length: 132  Bit Score: 232.26  E-value: 1.31e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 326 KRTKKSYSSTLRGMPSALKNGIISDQELLPRRNSLILKPKPDPAQQTDSQNSDTEQYFREWFSKPANLHGVILPRVSGTH 405
Cdd:pfam12578   1 KRRKKSYSSTLRGPPPSLKNGLFRDEEDLLRRNSLLLRLKPDCPLHRSSDSNDSEQFFRDWFSKPADLHGLLLPLLSGPH 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462492778 406 IKLWKLCYFRWVPEAQISLGGSITAFHKLSLLADEVDVLSRMLRQQRSGPLE 457
Cdd:pfam12578  81 IKLWKLCYLRWVPEAQINHGGPITAFHKLSLLADEVEALQRLLRQYRGGPSE 132
 
Name Accession Description Interval E-value
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 31-224 2.56e-142

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 10; Myotubularin related phosphoinositide phosphatase 10 (MTMR10) is enzymatically inactive and contains an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR10 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket.


Pssm-ID: 350441  Cd Length: 195  Bit Score: 407.74  E-value: 2.56e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  31 RRMPLWCWSHSNGSALVRMALIKDVLQQRKIDQRICNAITKSHPQRSDVYKSDLDKTLPNIQEVQAAFVKLKQLCVNEPF 110
Cdd:cd14593     1 RRIPLWCWNHPNGSALVRMANIKDLLQQRKIDQRICNAITRSHPLRSDVYKSDLDKTLPNIQEIQAAFVKLKQLCVNEPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 111 EETEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLVQVMLDPYFRTITGFQSLIQKE 190
Cdd:cd14593    81 EETEEKWLSSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLVQVMLDPYFRTITGFQSLIQKE 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462492778 191 WVMAGYQFLDRCNHLKRS-EKESPLFLLFLDATWQ 224
Cdd:cd14593   161 WVMAGYRFLDRCNHLKKSsKKESPLFLLFLDCVWQ 195
3-PAP pfam12578
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
 326-457 1.31e-74

Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically between 115 and 138 amino acids in length. Myotubularin is a dual-specific phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bisphosphate. 3-PAP is a catalytically inactive member of the myotubularin gene family, which coprecipitates lipid phosphatidylinositol 3-phosphate-3-phosphatase activity from lysates of human platelets.


Pssm-ID: 463634  Cd Length: 132  Bit Score: 232.26  E-value: 1.31e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 326 KRTKKSYSSTLRGMPSALKNGIISDQELLPRRNSLILKPKPDPAQQTDSQNSDTEQYFREWFSKPANLHGVILPRVSGTH 405
Cdd:pfam12578   1 KRRKKSYSSTLRGPPPSLKNGLFRDEEDLLRRNSLLLRLKPDCPLHRSSDSNDSEQFFRDWFSKPADLHGLLLPLLSGPH 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462492778 406 IKLWKLCYFRWVPEAQISLGGSITAFHKLSLLADEVDVLSRMLRQQRSGPLE 457
Cdd:pfam12578  81 IKLWKLCYLRWVPEAQINHGGPITAFHKLSLLADEVEALQRLLRQYRGGPSE 132
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 7-264 1.22e-62

Myotubularin-like phosphatase domain; This family represents the phosphatase domain within eukaryotic myotubularin-related proteins. Myotubularin is a dual-specific lipid phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bi-phosphate. Mutations in gene encoding myotubularin-related proteins have been associated with disease.


Pssm-ID: 461958 [Multi-domain]  Cd Length: 332  Bit Score: 208.10  E-value: 1.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778   7 PEYIVVPSSLADQDLKIFSHSFVGRRMPLWCWSH-SNGSALVRMA--LIkDVLQQRKI-DQRICNAITKSHPQRS----- 77
Cdd:pfam06602  41 PALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHkENGAVITRSSqpLV-GLNGKRSIeDEKLLQAIFKSSNPYSakkly 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  78 -----------------------DVYKSD----LDktLPNIQEVQAAFVKLKQLCvnEPFEETEEKWLSSLENTRWLEYV 130
Cdd:pfam06602 120 ivdarpklnamanrakgggyeneDNYPNCkkifLG--IENIHVMRDSLNKLVEAC--NDRSPSMDKWLSRLESSGWLKHI 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 131 RAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLVQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHL---KR 207
Cdd:pfam06602 196 KAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLagfTD 275

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462492778 208 SEKESPLFLLFLDATWQLLEQYPAAFEFSETYLAVLYDSTRISLFGTFLFNSPHQRV 264
Cdd:pfam06602 276 SKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKERV 332
 
Name Accession Description Interval E-value
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 31-224 2.56e-142

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 10; Myotubularin related phosphoinositide phosphatase 10 (MTMR10) is enzymatically inactive and contains an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR10 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket.


Pssm-ID: 350441  Cd Length: 195  Bit Score: 407.74  E-value: 2.56e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  31 RRMPLWCWSHSNGSALVRMALIKDVLQQRKIDQRICNAITKSHPQRSDVYKSDLDKTLPNIQEVQAAFVKLKQLCVNEPF 110
Cdd:cd14593     1 RRIPLWCWNHPNGSALVRMANIKDLLQQRKIDQRICNAITRSHPLRSDVYKSDLDKTLPNIQEIQAAFVKLKQLCVNEPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 111 EETEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLVQVMLDPYFRTITGFQSLIQKE 190
Cdd:cd14593    81 EETEEKWLSSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLVQVMLDPYFRTITGFQSLIQKE 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462492778 191 WVMAGYQFLDRCNHLKRS-EKESPLFLLFLDATWQ 224
Cdd:cd14593   161 WVMAGYRFLDRCNHLKKSsKKESPLFLLFLDCVWQ 195
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 31-224 1.38e-106

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatases 10, 11, and 12; This subgroup of enzymatically inactive phosphatase domains of myotubularins consists of MTMR10, MTMR11, MTMR12, and similar proteins. Beside the phosphatase domain, they contain an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR10, MTMR11, and MTMR12 are pseudophosphatases that lack the catalytic cysteine in their catalytic pocket. MTMR12 functions as an adapter for the catalytically active myotubularin to regulate its intracellular location.


Pssm-ID: 350385  Cd Length: 200  Bit Score: 316.98  E-value: 1.38e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  31 RRMPLWCWSHSNGSALVRMALIKDVLQQRKIDQRICNAITKSHPQRSDVYKSDLDKTLPNIQEVQAAFVKLKQLCVNEPF 110
Cdd:cd14537     1 GRPPVWCWSHPNGAALVRMAELLPTITDRTQENKMLEAIRKSHPNLKKPKVIDLDKLLPSLQDVQAAYLKLRELCTPDSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 111 EETEE---KWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLVQVMLDPYFRTITGFQSLI 187
Cdd:cd14537    81 EQFWVqdsKWYSLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQESDGRDLSCVVSSLVQLLLDPHFRTITGFQSLI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462492778 188 QKEWVMAGYQFLDRCNHL---KRSEKESPLFLLFLDATWQ 224
Cdd:cd14537   161 QKEWVALGHPFCDRLGHVkpnKTESEESPVFLLFLDCVWQ 200
3-PAP pfam12578
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
 326-457 1.31e-74

Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically between 115 and 138 amino acids in length. Myotubularin is a dual-specific phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bisphosphate. 3-PAP is a catalytically inactive member of the myotubularin gene family, which coprecipitates lipid phosphatidylinositol 3-phosphate-3-phosphatase activity from lysates of human platelets.


Pssm-ID: 463634  Cd Length: 132  Bit Score: 232.26  E-value: 1.31e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 326 KRTKKSYSSTLRGMPSALKNGIISDQELLPRRNSLILKPKPDPAQQTDSQNSDTEQYFREWFSKPANLHGVILPRVSGTH 405
Cdd:pfam12578   1 KRRKKSYSSTLRGPPPSLKNGLFRDEEDLLRRNSLLLRLKPDCPLHRSSDSNDSEQFFRDWFSKPADLHGLLLPLLSGPH 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462492778 406 IKLWKLCYFRWVPEAQISLGGSITAFHKLSLLADEVDVLSRMLRQQRSGPLE 457
Cdd:pfam12578  81 IKLWKLCYLRWVPEAQINHGGPITAFHKLSLLADEVEALQRLLRQYRGGPSE 132
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
 31-224 4.99e-72

protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. Not all members are catalytically active proteins, some function as adaptors for the active members.


Pssm-ID: 350357  Cd Length: 226  Bit Score: 228.97  E-value: 4.99e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  31 RRMPLWCWSHS-NGSALVRMALIKDVLQQR--KIDQRICNAITKSHPQRSDVYKSDLDKTL------------------- 88
Cdd:cd14507     1 GRIPVLSWRHPrNGAVICRSSQPLVGLTGSrsKEDEKLLNAIRKASPSSKKLYIVDARPKLnavanrakgggyenteyyp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  89 ---------PNIQEVQAAFVKLKQLCvnEPFEETEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGR 159
Cdd:cd14507    81 nceleflniENIHAMRDSLNKLRDAC--LSPNDEESNWLSALESSGWLEHIRLILKGAVRVADLLEKEGTSVLVHCSDGW 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462492778 160 DLSCCVASLVQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHLKR---SEKESPLFLLFLDATWQ 224
Cdd:cd14507   159 DRTSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDKnssDEERSPIFLQFLDCVWQ 226
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 31-225 6.60e-69

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 12; Myotubularin related phosphoinositide phosphatase 12 (MTMR12), also called phosphatidylinositol 3 phosphate 3-phosphatase adapter subunit (3-PAP), is enzymatically inactive and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR12 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket. It functions as an adapter for the catalytically active myotubularin to regulate its intracellular location.


Pssm-ID: 350442  Cd Length: 203  Bit Score: 220.10  E-value: 6.60e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  31 RRMPLWCWSHSNGSALVRM-ALIKDV------LQQRKIDqRICNAITKSHPQRsdVYKSDLDKTLPNIQEVQAAFVKLKQ 103
Cdd:cd14594     1 RGIPIWCWSCHNGCALLKMsALPKEQddvalqDQKSFLD-RIYKTLSRPPYES--VKTEDLSASLPSLQEIQTAYNRFKQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 104 LCVNE---PFEETEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLVQVMLDPYFRTI 180
Cdd:cd14594    78 LFLIDnstDFWDTDVKWFSSLESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462492778 181 TGFQSLIQKEWVMAGYQFLDRCNHLKRSEK-ESPLFLLFLDATWQL 225
Cdd:cd14594   158 SGFQSLIQKEWVMGGHCFLDRCNHLRQNDKeEVPVFLLFLDCVWQL 203
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 7-264 1.22e-62

Myotubularin-like phosphatase domain; This family represents the phosphatase domain within eukaryotic myotubularin-related proteins. Myotubularin is a dual-specific lipid phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bi-phosphate. Mutations in gene encoding myotubularin-related proteins have been associated with disease.


Pssm-ID: 461958 [Multi-domain]  Cd Length: 332  Bit Score: 208.10  E-value: 1.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778   7 PEYIVVPSSLADQDLKIFSHSFVGRRMPLWCWSH-SNGSALVRMA--LIkDVLQQRKI-DQRICNAITKSHPQRS----- 77
Cdd:pfam06602  41 PALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHkENGAVITRSSqpLV-GLNGKRSIeDEKLLQAIFKSSNPYSakkly 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  78 -----------------------DVYKSD----LDktLPNIQEVQAAFVKLKQLCvnEPFEETEEKWLSSLENTRWLEYV 130
Cdd:pfam06602 120 ivdarpklnamanrakgggyeneDNYPNCkkifLG--IENIHVMRDSLNKLVEAC--NDRSPSMDKWLSRLESSGWLKHI 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 131 RAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLVQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHL---KR 207
Cdd:pfam06602 196 KAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLagfTD 275

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462492778 208 SEKESPLFLLFLDATWQLLEQYPAAFEFSETYLAVLYDSTRISLFGTFLFNSPHQRV 264
Cdd:pfam06602 276 SKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKERV 332
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 31-225 1.24e-61

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 11; Myotubularin related phosphoinositide phosphatase 11 (MTMR11), also called cisplatin resistance-associated protein (hCRA) in humans, is enzymatically inactive and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR11 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket.


Pssm-ID: 350443  Cd Length: 195  Bit Score: 200.83  E-value: 1.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  31 RRMPLWCWSHSNGSALVRMALIKDVLQQRKIDQRICNAITKSHpqRSDVYKSDLDKTLPNIQEVQAAFVKLKQLCVNEP- 109
Cdd:cd14595     1 GRIPRWCWHHPGGSDLLRMAGFYTNSDPEKEDIRSVELLLQAG--HSQCVIVDTSEELPSPADIQLAYLKLRTLCLPDIs 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 110 FEETEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLVQVMLDPYFRTITGFQSLIQK 189
Cdd:cd14595    79 VSVSDEKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQK 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462492778 190 EWVMAGYQFLDRCNHLKRSEK-ESPLFLLFLDATWQL 225
Cdd:cd14595   159 EWVVAGHPFLQRLNLTRESDKeESPVFLLFLDCVWQL 195
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 7-245 9.23e-42

protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases 6, 7, and 8; This subgroup of enzymatically active phosphatase domains of myotubularins consists of MTMR6, MTMR7 and MTMR8, and related domains. Beside the phosphatase domain, they contain a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. MTMR6, MTMR7 and MTMR8 form complexes with catalytically inactive MTMR9, and display differential substrate preferences. In cells, the MTMR6/R9 complex significantly increases the cellular levels of PtdIns(5)P, the product of PI(3,5)P(2) dephosphorylation, whereas the MTMR8/R9 complex reduces cellular PtdIns(3)P levels. The MTMR6/R9 complex serves to inhibit stress-induced apoptosis while the MTMR8/R9 complex inhibits autophagy.


Pssm-ID: 350380 [Multi-domain]  Cd Length: 301  Bit Score: 151.73  E-value: 9.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778   7 PEYIVVPSSlADQDLKIFSHSFVGR-RMPLWCWSH-SNGSALVRMALIKDVLQQRKI-DQRICNAITKSHPQRSDVYKSD 83
Cdd:cd14532    31 PRELFVPTS-ASTPVLVGSSKFRSKgRLPVLSYLHkDNQAAICRCSQPLSGFSARCVeDEQLLQAIRKANPNSKFMYVVD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  84 ldkTLP-------------------------------NIQEVQAAFVKLKQLCvnEPFEETEEKWLSSLENTRWLEYVRA 132
Cdd:cd14532   110 ---TRPkinamankaagkgyenednysnikfqffgieNIHVMRSSLQKLLEVC--ELKNPSMSAFLSGLESSGWLKHIKA 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 133 FLKHSAELVYMLESKHlSVVLQEEEGRDLSCCVASLVQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHLKRSEKE- 211
Cdd:cd14532   185 VMDTSVFIAKAVSEGA-SVLVHCSDGWDRTAQTCSLASLLLDPYYRTIKGFQVLIEKEWLSFGHKFTDRCGHLQGDAKEv 263

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2462492778 212 SPLFLLFLDATWQLLEQYPAAFEFSETYLAVLYD 245
Cdd:cd14532   264 SPVFTQFLDCVWQLMQQFPRAFEFNERFLLTLHD 297
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 1-228 1.19e-36

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatases 5 and 13; This subgroup of enzymatically inactive phosphatase domains of myotubularins consists of MTMR5, also known as SET binding factor 1 (SBF1) and MTMR13, also known as SET binding factor 2 (SBF2), and similar domains. Beside the pseudophosphatase domain, they contain a variety of other domains, including a DENN and a PH-like domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR5 and MTMR13 are pseudophosphatases that lack the catalytic cysteine in their catalytic pocket. Mutations in MTMR13 causes Charcot-Marie-Tooth type 4B2, a severe childhood-onset neuromuscular disorder, characterized by demyelination and redundant loops of myelin known as myelin outfoldings, a similar phenotype as mutations in MTMR2. Mutations in the MTMR5 gene cause Charcot-Marie-tooth disease type 4B3. MTMR5 and MTMR13 interact with MTMR2 and stimulate its phosphatase activity.


Pssm-ID: 350382 [Multi-domain]  Cd Length: 274  Bit Score: 137.11  E-value: 1.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778   1 MISTC--LPEYIVVPSSLADQDLKIFSHSFVGRRMPLWCWSHSNGSA-LVRMALI--KDVLQQRKIDQRICNAITKSHPQ 75
Cdd:cd14534     9 DYSICrsYPALVVVPQSVSDESLRKVARCYRQGRFPVVTWRHPRTKAlLLRSGGFhgKGVMGMLKSANTSTSSPTVSSSE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  76 RSDV-----YKSDL------DKT-------------------LPNIQEVQAAFVKLKQLCVNEPF-EETEEKWLSSLENT 124
Cdd:cd14534    89 TSSSleqekYLSALvlyvlgEKSqmkgvkaesdpkcefipveYPEVRQVKASFKKLLRACVPSSApTEPEQSFLKAVEDS 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 125 RWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLVQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNH 204
Cdd:cd14534   169 EWLQQLQCLMQLSGAVVDLLDVQGSSVLLCLEDGWDVTTQVSSLSQLLLDPYYRTLEGFRVLVEKEWLAFGHRFSHRSNL 248

                         250       260
                  ....*....|....*....|....*.
gi 2462492778 205 LKRSEKE--SPLFLLFLDATWQLLEQ 228
Cdd:cd14534   249 TAASQSSgfAPVFLQFLDAVHQIHRQ 274
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
 90-245 3.68e-35

protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related phosphoinositide phosphatases 1 and 2; This subgroup of enzymatically active phosphatase domains of myotubularins consists of MTM1, MTMR1 and MTMR2. All contain an additional N-terminal PH-GRAM domain and C-terminal coiled-coiled domain and PDZ binding site. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively.


Pssm-ID: 350383  Cd Length: 249  Bit Score: 132.19  E-value: 3.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  90 NIQEVQAAFVKLKQLCvnepFEETEE-KWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASL 168
Cdd:cd14535    91 NIHVMRESLRKLKDIC----FPNIDDsHWLSNLESTHWLEHIKLILAGAVRIADKVESGKTSVVVHCSDGWDRTAQLTSL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 169 VQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHLKRSEKE---SPLFLLFLDATWQLLEQYPAAFEFSETYLAVLYD 245
Cdd:cd14535   167 AMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGHGDKNHSDadrSPVFLQFIDCVWQMTRQFPNAFEFNEHFLITILD 246
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 18-245 5.31e-35

protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 2; Myotubularin related phosphoinositide phosphatase 2 (MTMR2) is enzymatically active and contains an additional N-terminal PH-GRAM domain and C-terminal coiled-coiled domain and PDZ binding site. Mutations in MTMR2 causes Charcot-Marie-Tooth type 4B1, a severe childhood-onset neuromuscular disorder, characterized by demyelination and redundant loops of myelin known as myelin outfoldings, a similar phenotype as mutations in MTMR13. MTMR13, an inactive phosphatase, is believed to interact with MTMR2 and stimulate its phosphatase activity. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively.


Pssm-ID: 350438  Cd Length: 262  Bit Score: 132.08  E-value: 5.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  18 DQDLKIFShSFVGR-RMPLWCWSHSNGSALV---RMALIKDVLQQRKIDQRICNAITKSHPQRSDVYKSD---------- 83
Cdd:cd14590     1 DEELKRVA-SFRSRgRIPVLSWIHPESQATItrcSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFDarpsvnavan 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  84 --------------------LDktLPNIQEVQAAFVKLKQLcVNEPFEETEekWLSSLENTRWLEYVRAFLKHSAELVYM 143
Cdd:cd14590    80 kakgggyesedayqnaelvfLD--IHNIHVMRESLRKLKEI-VYPNIEESH--WLSNLESTHWLEHIKLILAGALRIADK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 144 LESKHLSVVLQEEEGRDLSCCVASLVQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHLKRSEKE---SPLFLLFLD 220
Cdd:cd14590   155 VESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADadrSPVFLQFID 234

                         250       260
                  ....*....|....*....|....*
gi 2462492778 221 ATWQLLEQYPAAFEFSETYLAVLYD 245
Cdd:cd14590   235 CVWQMTRQFPTAFEFNEYFLITILD 259
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
 32-245 7.41e-35

protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; Myotubularin phosphoinositide phosphatase 1 (MTM1), also called myotubularin, is enzymatically active and contains an N-terminal PH-GRAM domain and C-terminal coiled-coiled domain and PDZ binding site. Mutations in MTM1 cause X-linked myotubular myopathy. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively.


Pssm-ID: 350439  Cd Length: 249  Bit Score: 131.30  E-value: 7.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  32 RMPLWCWSH-SNGSALVRMA--LIKDVLQQRKIDQRICNAITKSHPQRSDV--------------------YKSD----- 83
Cdd:cd14591     2 RIPVLSWIHpENQAVIMRCSqpLVGMSGKRNKDDEKYLDIIREANGQTSKLtiydarpsvnavankatgggYEGDdayqn 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  84 -----LDktLPNIQEVQAAFVKLKQLcVNEPFEETEekWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEG 158
Cdd:cd14591    82 aelvfLD--IHNIHVMRESLKKLKDI-VYPNVEESH--WLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 159 RDLSCCVASLVQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHLKRSEKE---SPLFLLFLDATWQLLEQYPAAFEF 235
Cdd:cd14591   157 WDRTAQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGHGDKNHADadrSPIFLQFIDCVWQMSKQFPTAFEF 236

                         250
                  ....*....|
gi 2462492778 236 SETYLAVLYD 245
Cdd:cd14591   237 NEQFLITILD 246
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 88-245 1.74e-34

protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 1; Myotubularin-related phosphoinositide phosphatase 1 (MTMR1) is enzymatically active and contains an N-terminal PH-GRAM domain, a C-terminal coiled-coiled domain and a PDZ binding site. MTMR1 is associated with myotonic dystrophy. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively.


Pssm-ID: 350440  Cd Length: 249  Bit Score: 130.48  E-value: 1.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  88 LPNIQEVQAAFVKLKQLcVNEPFEETeeKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVAS 167
Cdd:cd14592    89 IHNIHVMRESLRKLKEI-VYPSIDEA--RWLSNVDGTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGWDRTAQLTS 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 168 LVQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHLKRSEKE---SPLFLLFLDATWQLLEQYPAAFEFSETYLAVLY 244
Cdd:cd14592   166 LAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGHGDDNHADadrSPIFLQFIDCVWQMTRQFPSAFEFNELFLITIL 245


                  .
gi 2462492778 245 D 245
Cdd:cd14592   246 D 246
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 86-224 1.49e-32

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 9; Myotubularin related phosphoinositide phosphatase 9 (MTMR9) is enzymatically inactive and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. Mutations have been associated with obesity and metabolic syndrome. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR9 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket. It forms complexes with catalytically active MTMR6, MTMR7 and MTMR8, and regulates their activities; the complexes display differential substrate preferences. The MTMR6/R9 complex serves to inhibit stress-induced apoptosis while the MTMR8/R9 complex inhibits autophagy.


Pssm-ID: 350384  Cd Length: 224  Bit Score: 124.37  E-value: 1.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  86 KTLPNIQEVQAAFVKLKQLCVNEpfEETEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCV 165
Cdd:cd14536    84 KPIERYNVLQESLIKLVEACNDQ--GHSMDKWLSKLESSNWLSHVKEILTTACLVAQCIDREGASVLVHGSEGMDSTLQV 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462492778 166 ASLVQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHL----KRSEKESPLFLLFLDATWQ 224
Cdd:cd14536   162 TSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRCAKSaysnSKQKFESPVFLLFLDCVWQ 224
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 90-245 1.93e-31

protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 8; Myotubularin related phosphoinositide phosphatase 8 (MTMR8) is enzymatically active and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. MTMR8 forms a complex with catalytically inactive MTMR9 and preferentially dephosphorylates PtdIns(3)P; the MTMR8/R9 complex inhibits autophagy. In zebrafish, it cooperates with PI3K to regulate actin filament modeling and muscle development.


Pssm-ID: 350432 [Multi-domain]  Cd Length: 308  Bit Score: 123.44  E-value: 1.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  90 NIQEVQAAFVKLKQLCvnEPFEETEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLV 169
Cdd:cd14584   150 NIHVMRSSLQKLLEVC--EMKSPSMSDFLTGLENSGWLRHIKAVMDAGVFLAKAVKEEKASVLVHCSDGWDRTAQVCSLA 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462492778 170 QVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHLKRSEKE-SPLFLLFLDATWQLLEQYPAAFEFSETYLAVLYD 245
Cdd:cd14584   228 SLLLDPFYRTIKGLMVLIEKEWISMGHKFSQRCGHLDGDPKEvSPVFTQFLECVWQLMEQFPCAFEFNEHFLLEIHD 304
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 90-245 2.13e-31

protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 6; Myotubularin related phosphoinositide phosphatase 6 is enzymatically active and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. MTMR6 forms a complex with catalytically inactive MTMR9 and preferentially dephosphorylates PtdIns(3,5)P(2); the MTMR6/R9 complex serves to inhibit stress-induced apoptosis.


Pssm-ID: 350433 [Multi-domain]  Cd Length: 302  Bit Score: 123.12  E-value: 2.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  90 NIQEVQAAFVKLKQLCVNEPFEETEekWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLV 169
Cdd:cd14585   144 NIHVMRSSLQKLLEVCGTKALSVND--FLSGLESSGWLRHIKAVLDAAVFLAKAVAVEGASVLVHCSDGWDRTAQVCSLG 221

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462492778 170 QVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHLKRSEKE-SPLFLLFLDATWQLLEQYPAAFEFSETYLAVLYD 245
Cdd:cd14585   222 SLLLDPYYRTIKGFMVLIEKDWISFGHKFSDRCGQLDGDPKEiSPVFTQFLECVWQLTEQFPRAFEFSEAFLLQIHE 298
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 88-224 5.61e-28

protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases 3 and 4; This subgroup of enzymatically active phosphatase domains of myotubularins consists of MTMR3, also known as ZFYVE10, and MTMR4, also known as ZFYVE11, and related domains. Beside the phosphatase domain, they contain a C-terminal FYVE domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively.


Pssm-ID: 350381  Cd Length: 229  Bit Score: 111.73  E-value: 5.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  88 LPNIQEVQAAFVKLKQLCVNEPFEETeekWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVAS 167
Cdd:cd14533    93 LANIHAIRKSFHSLRALCSSAPDQPN---WLSNLESTKWLHHLSGLLKAALLVVNAVDEEGRPVLVHCSDGWDRTPQIVA 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 168 LVQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHLKRSE---KESPLFLLFLDATWQ 224
Cdd:cd14533   170 LAELMLDPYYRTIEGFQVLVEREWLDFGHKFADRCGHGVNSEdinERCPVFLQWLDCVHQ 229
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 90-240 2.91e-27

protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 7; Myotubularin related phosphoinositide phosphatase 7 (MTMR7) is enzymatically active and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. In neuronal cells, MTMR7 forms a complex with catalytically inactive MTMR9 and dephosphorylates phosphatidylinositol 3-phosphate and Ins(1,3)P2.


Pssm-ID: 350431 [Multi-domain]  Cd Length: 302  Bit Score: 111.59  E-value: 2.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  90 NIQEVQAAFVKLKQLCvnEPFEETEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLV 169
Cdd:cd14583   144 NIHVMRNSLQKMLEVC--ELRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVA 221

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462492778 170 QVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHLKRSEKE-SPLFLLFLDATWQLLEQYPAAFEFSETYL 240
Cdd:cd14583   222 SLLLDPYYRTIKGFMVLIEKDWVSFGHKFNHRYGHLDGDPKEvSPVIDQFIECVWQLMEQFPCAFEFNERFL 293
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 88-224 7.59e-26

protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 3; Myotubularin related phosphoinositide phosphatase 3 (MTMR3), also known as FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1) or Zinc finger FYVE domain-containing protein 10 (ZFYVE10), is enzymatically active and contains a C-terminal FYVE domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. Together with phosphoinositide 5-kinase PIKfyve, phosphoinositide 3-phosphatase MTMR3 constitutes a phosphoinositide loop that produces PI(5)P via PI(3,5)P2 and regulates cell migration.


Pssm-ID: 350434  Cd Length: 317  Bit Score: 107.80  E-value: 7.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  88 LPNIQEVQAAFVKLKQLCVNEPfeeTEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVAS 167
Cdd:cd14586   181 MANIHSIRKSFQSLRLLCTQMP---DPANWLSALESTKWLQHLSMLLKSALLVVHAVDRDQRPVLVHCSDGWDRTPQIVA 257

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 168 LVQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHLKRSE---KESPLFLLFLDATWQ 224
Cdd:cd14586   258 LSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRCGHGENSDdlnERCPVFLQWLDCVHQ 317
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 88-224 2.24e-24

protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 4; Myotubularin related phosphoinositide phosphatase 4 (MTMR4), also known as FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2) or zinc finger FYVE domain-containing protein 11 (ZFYVE11), is enzymatically active and contains a C-terminal FYVE domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. MTMR4 localizes at the interface of early and recycling endosomes to regulate trafficking through this pathway. It plays a role in bacterial pathogenesis by stabilizing the integrity of bacteria-containing vacuoles.


Pssm-ID: 350435 [Multi-domain]  Cd Length: 308  Bit Score: 103.57  E-value: 2.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  88 LPNIQEVQAAFVKLKQLCVNEPfeeTEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVAS 167
Cdd:cd14587   172 MANIHSIRNSFQYLRAVCSQMP---DPGNWLSALESTKWLQHLSVMLKAAVLVASAVDREGRPVLVHCSDGWDRTPQIVA 248

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 168 LVQVMLDPYFRTITGFQSLIQKEWVMAGYQFLDRCNHLKRSEKES---PLFLLFLDATWQ 224
Cdd:cd14587   249 LAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHQENVEDQNeqcPVFLQWLDCVHQ 308
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 1-228 6.06e-23

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 13; Myotubularin related phosphoinositide phosphatase 13 (MTMR13), also known as SET binding factor 2 (SBF2), is enzymatically inactive and contains a variety of other domains, including a DENN and a PH-like domain. Mutations in MTMR13 causes Charcot-Marie-Tooth type 4B2, a severe childhood-onset neuromuscular disorder, characterized by demyelination and redundant loops of myelin known as myelin outfoldings, a similar phenotype as mutations in MTMR2. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR13 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket. It is believed to interact with MTMR2 and stimulate its phosphatase activity. It is also a guanine nucleotide exchange factor (GEF) which may activate RAB28, promoting the exchange of GDP to GTP and converting inactive GDP-bound Rab proteins into their active GTP-bound form.


Pssm-ID: 350437  Cd Length: 297  Bit Score: 99.23  E-value: 6.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778   1 MISTC--LPEYIVVPSSLADQDLKIFSHSFVGRRMPLWCWSHS-NGSALVR---------MALIKD-------------- 54
Cdd:cd14589     9 MYSLCrsYPGLLVVPQSVQDSSLQKVARCYRHNRLPVVCWKNSkTKAVLLRsggfhgkgvVGLFKSqnphsaapassess 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  55 -VLQQRKIDQRICNAITKSHP-----------------------QRSDVYKSDLDKTL---------PNIQEVQAAFVKL 101
Cdd:cd14589    89 sSIEQEKYLQALLNAISVHQKmngnstllqsqllkrqaalyifgEKSQLRGFKLDFALncefvpvefHDIRQVKASFKKL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 102 KQLCVNEPF-EETEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHlSVVLQEEEGRDLSCCVASLVQVMLDPYFRTI 180
Cdd:cd14589   169 MRACVPSTIpTDSEVTFLKALGESEWFLQLHRIMQLAVVISELLESGS-SVMVCLEDGWDITTQVVSLVQLLSDPFYRTL 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462492778 181 TGFQSLIQKEWVMAGYQFLDRCNHLKRSEKE--SPLFLLFLDATWQLLEQ 228
Cdd:cd14589   248 EGFQMLVEKEWLSFGHKFSQRSNLTPNSQGSgfAPIFLQFLDCVHQIHNQ 297
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 1-225 2.92e-22

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 5; Myotubularin related phosphoinositide phosphatase 5 (MTMR5), also known as SET binding factor 1 (SBF1), is enzymatically inactive and contains a variety of other domains, including a DENN and a PH-like domain. Mutations in the MTMR5 gene cause Charcot-Marie-tooth disease type 4B3. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR5 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket. It interacts with MTMR2, an active myotubularin related phosphatidylinositol phosphatase, regulates its enzymatic activity and subcellular location.


Pssm-ID: 350436 [Multi-domain]  Cd Length: 291  Bit Score: 96.96  E-value: 2.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778   1 MISTC--LPEYIVVPSSLADQDLKIFSHSFVGRRMPLWCWSHSNGSA-LVRMA---------LIKD-------------- 54
Cdd:cd14588     9 MYAVCrsYPGLLIVPQSIQDNTIQRISRCYRQNRFPVVCWRNSRTKAvLLRSGglhgkgvvgLFKSqnapaagqsqtdst 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778  55 VLQQRKIDQricnAITKSHPQRSDVY-----------------KSDLDKTLPN--------------IQEVQAAFVKLKQ 103
Cdd:cd14588    89 SLEQEKYLQ----AVINSMPRYADASgrntlsgfraalyiigdKSQLKGVKQDplqqwevvpievfdVRQVKASFKKLMK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 104 LCV-NEPFEETEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHlSVVLQEEEGRDLSCCVASLVQVMLDPYFRTITG 182
Cdd:cd14588   165 ACVpSCPSTDPSQTYLRTLEESEWLSQLHKLLQVSVLVVELLDSGS-SVLVSLEDGWDITTQVVSLVQLLSDPYYRTIEG 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2462492778 183 FQSLIQKEWVMAGYQFLDRCNHLKRSEKE--SPLFLLFLDATWQL 225
Cdd:cd14588   244 FRLLVEKEWLSFGHRFSHRGAQTLASQSSgfTPVFLQFLDCVHQI 288
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
 104-224 9.08e-21

protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. Not all members are catalytically active proteins, some function as adaptors for the active members.


Pssm-ID: 350504  Cd Length: 229  Bit Score: 90.97  E-value: 9.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462492778 104 LCVNEPFEETEEKWLSSLENTRWLEYVRAFLKHSAELVYMLESKHLSVVLQEEEGRDLSCCVASLVQVMLDPYFRTITGF 183
Cdd:cd17666   113 LKDGDDSNPSYPPLINALKKSNWLKYLAIILQGADLIAKSIHFNHSHVLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGF 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462492778 184 QSLIQKEWVMAGYQFLDRCNHlkrseKE-SPLFLLFLDATWQ 224
Cdd:cd17666   193 MVLVEKDWLSFGHRFAERSGH-----KEtSPVFHQFLDCVYQ 229
 
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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