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Conserved domains on  [gi|167535754|ref|XP_001749550|]
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uncharacterized protein MONBRDRAFT_29099 [Monosiga brevicollis MX1]

Protein Classification

myotubularin family protein( domain architecture ID 10535076)

myotubularin family protein similar to myotubularin, a protein tyrosine phosphatase that dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
5-276 3.72e-112

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: 327.51  E-value: 3.72e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754    5 RSVSKYRQNGRFPMLCFLHPKTKMPLLRSGQPLAGSSGKRKYEDEQMLRMVLSTADV---KQGLILDTRTSSVASTHRSK 81
Cdd:pfam06602  56 KKAAKFRSKGRIPVLSYRHKENGAVITRSSQPLVGLNGKRSIEDEKLLQAIFKSSNPysaKKLYIVDARPKLNAMANRAK 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754   82 GGGLEVIDKYYGWSRKMLDIAAWPILADSLSKLLEACQDPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQP 161
Cdd:pfam06602 136 GGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACNDRSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSS 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  162 VVVHGSHGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPL-TRHNKTERAPVFLLFLDCVYQSYF 240
Cdd:pfam06602 216 VLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLaGFTDSKERSPVFLQFLDCVWQLLR 295
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 167535754  241 QFCAAFEFNESFLMELYMQSYSCVFGTFVGDCEAMR 276
Cdd:pfam06602 296 QFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKER 331
 
Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
5-276 3.72e-112

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: 327.51  E-value: 3.72e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754    5 RSVSKYRQNGRFPMLCFLHPKTKMPLLRSGQPLAGSSGKRKYEDEQMLRMVLSTADV---KQGLILDTRTSSVASTHRSK 81
Cdd:pfam06602  56 KKAAKFRSKGRIPVLSYRHKENGAVITRSSQPLVGLNGKRSIEDEKLLQAIFKSSNPysaKKLYIVDARPKLNAMANRAK 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754   82 GGGLEVIDKYYGWSRKMLDIAAWPILADSLSKLLEACQDPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQP 161
Cdd:pfam06602 136 GGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACNDRSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSS 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  162 VVVHGSHGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPL-TRHNKTERAPVFLLFLDCVYQSYF 240
Cdd:pfam06602 216 VLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLaGFTDSKERSPVFLQFLDCVWQLLR 295
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 167535754  241 QFCAAFEFNESFLMELYMQSYSCVFGTFVGDCEAMR 276
Cdd:pfam06602 296 QFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKER 331
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
14-237 6.07e-87

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: 259.58  E-value: 6.07e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  14 GRFPMLCFLHPKTKMPLLRSGQPLAGSSGKRKYEDEQMLRMVLSTAdvKQGLILDTRTSSVASTHRSKGGGLEVIDKYYG 93
Cdd:cd14536    1 GRFPVLSYYHKKNGMVLMRSSQPLTGPNGKRCKEDEKLLNAVLGGG--KRGYIIDTRSKNVAQQARAKGGGFEPEAHYPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  94 WSRKMLDIAAWPILADSLSKLLEACQDPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHGSHGTDIT 173
Cdd:cd14536   79 WRRIHKPIERYNVLQESLIKLVEACNDQGHSMDKWLSKLESSNWLSHVKEILTTACLVAQCIDREGASVLVHGSEGMDST 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167535754 174 CIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPL---TRHNKTErAPVFLLFLDCVYQ 237
Cdd:cd14536  159 LQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRCAKSaysNSKQKFE-SPVFLLFLDCVWQ 224
 
Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
5-276 3.72e-112

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: 327.51  E-value: 3.72e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754    5 RSVSKYRQNGRFPMLCFLHPKTKMPLLRSGQPLAGSSGKRKYEDEQMLRMVLSTADV---KQGLILDTRTSSVASTHRSK 81
Cdd:pfam06602  56 KKAAKFRSKGRIPVLSYRHKENGAVITRSSQPLVGLNGKRSIEDEKLLQAIFKSSNPysaKKLYIVDARPKLNAMANRAK 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754   82 GGGLEVIDKYYGWSRKMLDIAAWPILADSLSKLLEACQDPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQP 161
Cdd:pfam06602 136 GGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACNDRSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSS 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  162 VVVHGSHGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPL-TRHNKTERAPVFLLFLDCVYQSYF 240
Cdd:pfam06602 216 VLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLaGFTDSKERSPVFLQFLDCVWQLLR 295
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 167535754  241 QFCAAFEFNESFLMELYMQSYSCVFGTFVGDCEAMR 276
Cdd:pfam06602 296 QFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKER 331
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
14-237 6.07e-87

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: 259.58  E-value: 6.07e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  14 GRFPMLCFLHPKTKMPLLRSGQPLAGSSGKRKYEDEQMLRMVLSTAdvKQGLILDTRTSSVASTHRSKGGGLEVIDKYYG 93
Cdd:cd14536    1 GRFPVLSYYHKKNGMVLMRSSQPLTGPNGKRCKEDEKLLNAVLGGG--KRGYIIDTRSKNVAQQARAKGGGFEPEAHYPQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  94 WSRKMLDIAAWPILADSLSKLLEACQDPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHGSHGTDIT 173
Cdd:cd14536   79 WRRIHKPIERYNVLQESLIKLVEACNDQGHSMDKWLSKLESSNWLSHVKEILTTACLVAQCIDREGASVLVHGSEGMDST 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167535754 174 CIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPL---TRHNKTErAPVFLLFLDCVYQ 237
Cdd:cd14536  159 LQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRCAKSaysNSKQKFE-SPVFLLFLDCVWQ 224
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
14-237 4.52e-77

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: 234.75  E-value: 4.52e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  14 GRFPMLCFLHPKTKMPLLRSGQPLAGSSGKRKYEDEQMLRMVLSTADV-KQGLILDTRTSSVASTHRSKGGGLEVIDKYY 92
Cdd:cd14507    1 GRIPVLSWRHPRNGAVICRSSQPLVGLTGSRSKEDEKLLNAIRKASPSsKKLYIVDARPKLNAVANRAKGGGYENTEYYP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  93 GWSRKMLDIAAWPILADSLSKLLEACQDPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHGSHGTDI 172
Cdd:cd14507   81 NCELEFLNIENIHAMRDSLNKLRDACLSPNDEESNWLSALESSGWLEHIRLILKGAVRVADLLEKEGTSVLVHCSDGWDR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167535754 173 TCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWS-PLTRHNKTERAPVFLLFLDCVYQ 237
Cdd:cd14507  161 TSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGhGDKNSSDEERSPIFLQFLDCVWQ 226
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
8-262 3.66e-65

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: 206.81  E-value: 3.66e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754   8 SKYRQNGRFPMLCFLHPKTKMPLLRSGQPLAGSSGkRKYEDEQMLRMVLSTADVKQGL-ILDTRTSSVASTHRSKGGGLE 86
Cdd:cd14532   49 SKFRSKGRLPVLSYLHKDNQAAICRCSQPLSGFSA-RCVEDEQLLQAIRKANPNSKFMyVVDTRPKINAMANKAAGKGYE 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  87 VIDKYYGWSRKMLDIAAWPILADSLSKLLEACQDPSLDASKFLEKLNASNWLSTVRDALSAAL---QAVTclehEQQPVV 163
Cdd:cd14532  128 NEDNYSNIKFQFFGIENIHVMRSSLQKLLEVCELKNPSMSAFLSGLESSGWLKHIKAVMDTSVfiaKAVS----EGASVL 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 164 VHGSHGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPLTRHNKtERAPVFLLFLDCVYQSYFQFC 243
Cdd:cd14532  204 VHCSDGWDRTAQTCSLASLLLDPYYRTIKGFQVLIEKEWLSFGHKFTDRCGHLQGDAK-EVSPVFTQFLDCVWQLMQQFP 282
                        250
                 ....*....|....*....
gi 167535754 244 AAFEFNESFLMELYMQSYS 262
Cdd:cd14532  283 RAFEFNERFLLTLHDHVYS 301
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
14-254 1.23e-64

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: 203.83  E-value: 1.23e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  14 GRFPMLCFLHPKTKMPLLRSGQPLAGSSGKRKYEDEQMLRMVL-STADVKQGLILDTRTSSVASTHRSKGGGLEVIDKYY 92
Cdd:cd14535    1 NRIPVLSWIHPESQATITRCSQPLVGVSGKRSKDDEKYLQLIMdANAQSHKLFIMDARPSVNAVANKAKGGGYESEDAYQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  93 GWSRKMLDIAAWPILADSLSKLLEACQdPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHGSHGTDI 172
Cdd:cd14535   81 NAELVFLDIHNIHVMRESLRKLKDICF-PNIDDSHWLSNLESTHWLEHIKLILAGAVRIADKVESGKTSVVVHCSDGWDR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 173 TCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWS-PLTRHNKTERAPVFLLFLDCVYQSYFQFCAAFEFNES 251
Cdd:cd14535  160 TAQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGhGDKNHSDADRSPVFLQFIDCVWQMTRQFPNAFEFNEH 239

                 ...
gi 167535754 252 FLM 254
Cdd:cd14535  240 FLI 242
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
5-261 1.60e-60

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: 193.71  E-value: 1.60e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754   5 RSVSKYRQNGRFPMLCFLHPKTKMPLLRSGQPLAGSSGKRKYEDEQMLRMVL-STADVKQGLILDTRTSSVASTHRSKGG 83
Cdd:cd14590    5 KRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMdSNAQSHKIFIFDARPSVNAVANKAKGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  84 GLEVIDKYYGWSRKMLDIAAWPILADSLSKLLEACQdPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVV 163
Cdd:cd14590   85 GYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVY-PNIEESHWLSNLESTHWLEHIKLILAGALRIADKVESGKTSVV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 164 VHGSHGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPLTR-HNKTERAPVFLLFLDCVYQSYFQF 242
Cdd:cd14590  164 VHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKnHADADRSPVFLQFIDCVWQMTRQF 243
                        250
                 ....*....|....*....
gi 167535754 243 CAAFEFNESFLMELYMQSY 261
Cdd:cd14590  244 PTAFEFNEYFLITILDHLY 262
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
14-256 1.69e-60

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: 193.27  E-value: 1.69e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  14 GRFPMLCFLHPKTKMPLLRSGQPLAGSSGKRKYEDEQMLRMVL-STADVKQGLILDTRTSSVASTHRSKGGGLEVIDKYY 92
Cdd:cd14592    1 GRVPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYLQTIMdANAQSHKLIIFDARQNSVADTNKTKGGGYESESAYP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  93 GWSRKMLDIAAWPILADSLSKLLEACQdPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHGSHGTDI 172
Cdd:cd14592   81 NAELVFLEIHNIHVMRESLRKLKEIVY-PSIDEARWLSNVDGTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGWDR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 173 TCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPLT-RHNKTERAPVFLLFLDCVYQSYFQFCAAFEFNES 251
Cdd:cd14592  160 TAQLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGHGDdNHADADRSPIFLQFIDCVWQMTRQFPSAFEFNEL 239

                 ....*
gi 167535754 252 FLMEL 256
Cdd:cd14592  240 FLITI 244
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
15-254 1.06e-55

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: 180.99  E-value: 1.06e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  15 RFPMLCFLHPKTKMPLLRSGQPLAGSSGKRKYEDEQMLRMVLSTADVKQGL-ILDTRTSSVASTHRSKGGGLEVIDKYYG 93
Cdd:cd14591    2 RIPVLSWIHPENQAVIMRCSQPLVGMSGKRNKDDEKYLDIIREANGQTSKLtIYDARPSVNAVANKATGGGYEGDDAYQN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  94 WSRKMLDIAAWPILADSLSKLLEACQdPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHGSHGTDIT 173
Cdd:cd14591   82 AELVFLDIHNIHVMRESLKKLKDIVY-PNVEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWDRT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 174 CIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPLTR-HNKTERAPVFLLFLDCVYQSYFQFCAAFEFNESF 252
Cdd:cd14591  161 AQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGHGDKnHADADRSPIFLQFIDCVWQMSKQFPTAFEFNEQF 240

                 ..
gi 167535754 253 LM 254
Cdd:cd14591  241 LI 242
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
8-262 4.84e-54

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: 178.20  E-value: 4.84e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754   8 SKYRQNGRFPMLCFLHPKTKMPLLRSGQPLAGSSGkRKYEDEQMLRMVLSTADVKQGL-ILDTRTSSVASTHRSKGGGLE 86
Cdd:cd14585   49 SKFRSKGRFPVLSYYHQEKKAAICRCSQPLSGFSA-RCLEDEHMLQAISKANPNNRYMyVMDTRPKLNAMANRAAGKGYE 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  87 VIDKYYGWSRKMLDIAAWPILADSLSKLLEACQDPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHG 166
Cdd:cd14585  128 NEDNYSNIRFQFVGIENIHVMRSSLQKLLEVCGTKALSVNDFLSGLESSGWLRHIKAVLDAAVFLAKAVAVEGASVLVHC 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 167 SHGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPLTRHNKtERAPVFLLFLDCVYQSYFQFCAAF 246
Cdd:cd14585  208 SDGWDRTAQVCSLGSLLLDPYYRTIKGFMVLIEKDWISFGHKFSDRCGQLDGDPK-EISPVFTQFLECVWQLTEQFPRAF 286
                        250
                 ....*....|....*.
gi 167535754 247 EFNESFLMELYMQSYS 262
Cdd:cd14585  287 EFSEAFLLQIHEHIHS 302
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
8-262 1.30e-52

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: 174.68  E-value: 1.30e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754   8 SKYRQNGRFPMLCFLHPKTKMPLLRSGQPLAGSSGkRKYEDEQMLRMVLSTADVKQGL-ILDTRTSSVASTHRSKGGGLE 86
Cdd:cd14584   55 SKFRSRGRFPVLSYLYKENNAAICRCSQPLSGFSA-RCVEDEQMLQAISKANPGSPFMyVVDTRPKLNAMANRAAGKGYE 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  87 VIDKYYGWSRKMLDIAAWPILADSLSKLLEACQDPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHG 166
Cdd:cd14584  134 NEDNYSNIRFQFIGIENIHVMRSSLQKLLEVCEMKSPSMSDFLTGLENSGWLRHIKAVMDAGVFLAKAVKEEKASVLVHC 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 167 SHGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPLTRHNKtERAPVFLLFLDCVYQSYFQFCAAF 246
Cdd:cd14584  214 SDGWDRTAQVCSLASLLLDPFYRTIKGLMVLIEKEWISMGHKFSQRCGHLDGDPK-EVSPVFTQFLECVWQLMEQFPCAF 292
                        250
                 ....*....|....*.
gi 167535754 247 EFNESFLMELYMQSYS 262
Cdd:cd14584  293 EFNEHFLLEIHDHVFS 308
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
8-262 8.87e-52

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: 172.45  E-value: 8.87e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754   8 SKYRQNGRFPMLCFLHPKTKMPLLRSGQPLAGSSGkRKYEDEQMLRMVLSTADVKQGL-ILDTRTSSVASTHRSKGGGLE 86
Cdd:cd14583   49 SKFRSRGRFPVLSYYCKDNNASICRSSQPLSGFSA-RCLEDEQMLQAIRKANPGSDFMyVVDTRPKLNAMANRAAGKGYE 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  87 VIDKYYGWSRKMLDIAAWPILADSLSKLLEACQDPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHG 166
Cdd:cd14583  128 NEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHC 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 167 SHGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPLTRHNKtERAPVFLLFLDCVYQSYFQFCAAF 246
Cdd:cd14583  208 SDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKFNHRYGHLDGDPK-EVSPVIDQFIECVWQLMEQFPCAF 286
                        250
                 ....*....|....*.
gi 167535754 247 EFNESFLMELYMQSYS 262
Cdd:cd14583  287 EFNERFLIHIHHHIYS 302
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
14-237 3.16e-49

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: 163.34  E-value: 3.16e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  14 GRFPMLCFLHPKTKMPLLRSGQPLAGSSGKRKYEDEQMLRMVL----STADVKQGLILDTRTSSVASTHRSKGGGLEVID 89
Cdd:cd14533    2 KRIPSVVWRHQRNGAVIARCSQPEVGWLGWRNAEDENLLQAIAeacaSNASPKKLLIVDARSYAAAVANRAKGGGCECPE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  90 KYYGWSRKMLDIAAWPILADSLSKLLEACQDPSlDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHGSHG 169
Cdd:cd14533   82 YYPNCEVVFMNLANIHAIRKSFHSLRALCSSAP-DQPNWLSNLESTKWLHHLSGLLKAALLVVNAVDEEGRPVLVHCSDG 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167535754 170 TDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRW---SPLTRHNktERAPVFLLFLDCVYQ 237
Cdd:cd14533  161 WDRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFGHKFADRCghgVNSEDIN--ERCPVFLQWLDCVHQ 229
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
14-237 4.72e-45

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: 152.60  E-value: 4.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  14 GRFPMLCFLHPKTKMPLLRSGQPLAGSSGKRKYEDEQMLRMVLSTADV------KQGLILDTRTSSVASTHRSKGGGLEV 87
Cdd:cd17666    1 QRIPVLTYLHKANGCSITRSSQPLVGLKQNRSIQDEKLVSEIFNTSINeiyispQKNLIVDARPTTNAMAQVALGAGTEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  88 IDKY-YGWSRKM-LDIAAWPILADSLSKLLEACQD----PSLDASKfLEKLNASNWLSTVRDALSAALQAVTCLEHEQQP 161
Cdd:cd17666   81 MDNYkYKTAKKIyLGIDNIHVMRDSLNKVTEALKDgddsNPSYPPL-INALKKSNWLKYLAIILQGADLIAKSIHFNHSH 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167535754 162 VVVHGSHGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRwsplTRHNKTerAPVFLLFLDCVYQ 237
Cdd:cd17666  160 VLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFAER----SGHKET--SPVFHQFLDCVYQ 229
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
20-237 1.61e-37

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: 135.55  E-value: 1.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  20 CFLHPKTKMPllrSGQPLAGSSGKRKYEDEQMLRMVLSTADVKQG------LILDTRTSSVASTHRSKGGGLEVIDKYYG 93
Cdd:cd14587   88 CALDPGTRAP---GGSPSKGNSDGSDASDTDFDSSLTACSAVESGaapqklLILDARSYTAAVANRAKGGGCECEEYYPN 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  94 WSRKMLDIAAWPILADSLSKLLEAC-QDPslDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHGSHGTDI 172
Cdd:cd14587  165 CEVMFMGMANIHSIRNSFQYLRAVCsQMP--DPGNWLSALESTKWLQHLSVMLKAAVLVASAVDREGRPVLVHCSDGWDR 242
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167535754 173 TCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWS-PLTRHNKTERAPVFLLFLDCVYQ 237
Cdd:cd14587  243 TPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGhQENVEDQNEQCPVFLQWLDCVHQ 308
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
6-237 1.69e-36

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: 132.84  E-value: 1.69e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754   6 SVSKYRQNGRFPMLCFLHPKTKMPLLRSGQPLAGSSGKRKYEDEQMLRMV-----------------------------L 56
Cdd:cd14586   40 SVASFRSWKRIPAVVYRHQSNGAVIARCGQPEVSWWGWRNADDEHLVQSVakacasdssscksvlmtgncsrdfpnggdL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  57 STADVKQG-----------------LILDTRTSSVASTHRSKGGGLEVIDKYYGWSRKMLDIAAWPILADSLSKLLEAC- 118
Cdd:cd14586  120 SDVEFDSSmsnasgveslaiqpqklLILDARSYAAAVANRAKGGGCECPEYYPNCEVVFMGMANIHSIRKSFQSLRLLCt 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 119 QDPslDASKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHGSHGTDITCIVVALAQLYMDPYFRTLEGFCKLV 198
Cdd:cd14586  200 QMP--DPANWLSALESTKWLQHLSMLLKSALLVVHAVDRDQRPVLVHCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLV 277
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 167535754 199 EKEWLHAGHPFASRWSpltrHNK-----TERAPVFLLFLDCVYQ 237
Cdd:cd14586  278 ETEWLDFGHKFADRCG----HGEnsddlNERCPVFLQWLDCVHQ 317
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
5-241 9.40e-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: 129.79  E-value: 9.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754   5 RSVSK-YRQNgRFPMLCFLHPKTKMPLLRSGQP-LAGSSGKRKYEDEQMLRMVLSTADVKQGLILDTRTSSV---ASTHR 79
Cdd:cd14534   32 RKVARcYRQG-RFPVVTWRHPRTKALLLRSGGFhGKGVMGMLKSANTSTSSPTVSSSETSSSLEQEKYLSALvlyVLGEK 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  80 SKGGGLEvIDKYYGWSRKMLDIAAWPILADSLSKLLEAC---QDPSLDASKFLEKLNASNWLSTVRDALSAALQAVTCLE 156
Cdd:cd14534  111 SQMKGVK-AESDPKCEFIPVEYPEVRQVKASFKKLLRACvpsSAPTEPEQSFLKAVEDSEWLQQLQCLMQLSGAVVDLLD 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 157 HEQQPVVVHGSHGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPLTRHNKTERAPVFLLFLDCVY 236
Cdd:cd14534  190 VQGSSVLLCLEDGWDVTTQVSSLSQLLLDPYYRTLEGFRVLVEKEWLAFGHRFSHRSNLTAASQSSGFAPVFLQFLDAVH 269

                 ....*
gi 167535754 237 QSYFQ 241
Cdd:cd14534  270 QIHRQ 274
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
105-237 3.20e-35

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: 126.30  E-value: 3.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 105 PILAD---SLSKLLEACQDPSLDA-----SKFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHGSHGTDITCIV 176
Cdd:cd14537   59 PSLQDvqaAYLKLRELCTPDSSEQfwvqdSKWYSLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQESDGRDLSCVV 138
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167535754 177 VALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWS-PLTRHNKTERAPVFLLFLDCVYQ 237
Cdd:cd14537  139 SSLVQLLLDPHFRTITGFQSLIQKEWVALGHPFCDRLGhVKPNKTESEESPVFLLFLDCVWQ 200
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
127-237 5.93e-32

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: 117.63  E-value: 5.93e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 127 KFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHGSHGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAG 206
Cdd:cd14594   93 KWFSSLESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQSLIQKEWVMGG 172
                         90       100       110
                 ....*....|....*....|....*....|.
gi 167535754 207 HPFASRWSPLtRHNKTERAPVFLLFLDCVYQ 237
Cdd:cd14594  173 HCFLDRCNHL-RQNDKEEVPVFLLFLDCVWQ 202
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
10-241 2.86e-31

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: 118.53  E-value: 2.86e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  10 YRQNgRFPMLCFLHPKTKMPLLRSG---------------QPLAGSS--GKRKYEDEQMLRMVLST----ADVKQGLILD 68
Cdd:cd14588   38 YRQN-RFPVVCWRNSRTKAVLLRSGglhgkgvvglfksqnAPAAGQSqtDSTSLEQEKYLQAVINSmpryADASGRNTLS 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  69 T-RTSSVASTHRSKGGGLEViDKYYGWSRKMLDIAAWPILADSLSKLLEAC--QDPSLDAS-KFLEKLNASNWLSTVRDA 144
Cdd:cd14588  117 GfRAALYIIGDKSQLKGVKQ-DPLQQWEVVPIEVFDVRQVKASFKKLMKACvpSCPSTDPSqTYLRTLEESEWLSQLHKL 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 145 LSAALQAVTCLEHEQQpVVVHGSHGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPLTRHNKTER 224
Cdd:cd14588  196 LQVSVLVVELLDSGSS-VLVSLEDGWDITTQVVSLVQLLSDPYYRTIEGFRLLVEKEWLSFGHRFSHRGAQTLASQSSGF 274
                        250
                 ....*....|....*..
gi 167535754 225 APVFLLFLDCVYQSYFQ 241
Cdd:cd14588  275 TPVFLQFLDCVHQIHLQ 291
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
10-241 6.54e-27

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: 106.93  E-value: 6.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  10 YRQNgRFPMLCFLHPKTKMPLLRSG-------------------QPlAGSSGKRKYEDEQMLRMVLSTADVK-------- 62
Cdd:cd14589   38 YRHN-RLPVVCWKNSKTKAVLLRSGgfhgkgvvglfksqnphsaAP-ASSESSSSIEQEKYLQALLNAISVHqkmngnst 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  63 --QGLILDTRTSSVASTHRSKGGGLEViDKYYGWSRKMLDIAAWPILADSLSKLLEAC---QDPSLDASKFLEKLNASNW 137
Cdd:cd14589  116 llQSQLLKRQAALYIFGEKSQLRGFKL-DFALNCEFVPVEFHDIRQVKASFKKLMRACvpsTIPTDSEVTFLKALGESEW 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 138 LSTVRDALSAALQAVTCLEHEQQpVVVHGSHGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPLT 217
Cdd:cd14589  195 FLQLHRIMQLAVVISELLESGSS-VMVCLEDGWDITTQVVSLVQLLSDPFYRTLEGFQMLVEKEWLSFGHKFSQRSNLTP 273
                        250       260
                 ....*....|....*....|....
gi 167535754 218 RHNKTERAPVFLLFLDCVYQSYFQ 241
Cdd:cd14589  274 NSQGSGFAPIFLQFLDCVHQIHNQ 297
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
110-237 1.22e-26

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: 103.43  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 110 SLSKLLEACQDPSLDAS--KFLEKLNASNWLSTVRDALSAALQAVTCLEHEQQPVVVHGSHGTDITCIVVALAQLYMDPY 187
Cdd:cd14593   67 AFVKLKQLCVNEPFEETeeKWLSSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLVQVMLDPY 146
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 167535754 188 FRTLEGFCKLVEKEWLHAGHPFASRWSPLTRHNKTErAPVFLLFLDCVYQ 237
Cdd:cd14593  147 FRTITGFQSLIQKEWVMAGYRFLDRCNHLKKSSKKE-SPLFLLFLDCVWQ 195
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
14-237 1.13e-25

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: 101.06  E-value: 1.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  14 GRFPMLCFLHPKTKmPLLRSGQPLAGSSGKRkyEDEQMLRMVLStADVKQGLILDTRTSsvasthrskggglevidkyyg 93
Cdd:cd14595    1 GRIPRWCWHHPGGS-DLLRMAGFYTNSDPEK--EDIRSVELLLQ-AGHSQCVIVDTSEE--------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754  94 wsrkmldiaaWPILAD---SLSKLLEAC-QDPSLDASKFLEKLNASN--WLSTVRDALSAALQAVTCLEHEQQPVVVHGS 167
Cdd:cd14595   56 ----------LPSPADiqlAYLKLRTLClPDISVSVSDEKWLSNLEGtrWLDHVRACLRKASEVSCLLAERHRSVILQES 125
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167535754 168 HGTDITCIVVALAQLYMDPYFRTLEGFCKLVEKEWLHAGHPFASRWSPlTRHNKTERAPVFLLFLDCVYQ 237
Cdd:cd14595  126 EDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEWVVAGHPFLQRLNL-TRESDKEESPVFLLFLDCVWQ 194
 
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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