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Conserved domains on  [gi|767951332|ref|XP_011542995|]
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myotubularin-related protein 7 isoform X3 [Homo sapiens]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 8-196 1.59e-153

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


The actual alignment was detected with superfamily member cd14583:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 302  Bit Score: 436.31  E-value: 1.59e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   8 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 87
Cdd:cd14583  114 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  88 KAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIE 167
Cdd:cd14583  194 KAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKFNHRYGHLDGDPKEVSPVIDQFIE 273

                        170       180
                 ....*....|....*....|....*....
gi 767951332 168 CVWQLMEQFPCAFEFNERFLIHIQHHIYS 196
Cdd:cd14583  274 CVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
 
Name Accession Description Interval E-value
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 8-196 1.59e-153

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: 436.31  E-value: 1.59e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   8 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 87
Cdd:cd14583  114 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  88 KAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIE 167
Cdd:cd14583  194 KAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKFNHRYGHLDGDPKEVSPVIDQFIE 273

                        170       180
                 ....*....|....*....|....*....
gi 767951332 168 CVWQLMEQFPCAFEFNERFLIHIQHHIYS 196
Cdd:cd14583  274 CVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 8-211 1.27e-150

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: 429.98  E-value: 1.27e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332    8 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 87
Cdd:pfam06602 127 LNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACNDRSPSMDKWLSRLESSGWLKHIKAILDGACLIA 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   88 KAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDG--DPKEISPVIDQF 165
Cdd:pfam06602 207 QAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGftDSKERSPVFLQF 286

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 767951332  166 IECVWQLMEQFPCAFEFNERFLIHIQHHIYSCQFGNFLCNSQKERR 211
Cdd:pfam06602 287 LDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKERV 332
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
91-195 3.29e-07

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 48.51  E-value: 3.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332    91 SEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTlkgfmvliekdwisfghkfnhrygnldgdpkeisPVIDQFiECVW 170
Cdd:smart00404  36 SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA----------------------------------GEVDIF-DTVK 80

                           90       100
                   ....*....|....*....|....*
gi 767951332   171 QLMEQFPCAFEFNERFLIHIQHHIY 195
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
 
Name Accession Description Interval E-value
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 8-196 1.59e-153

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: 436.31  E-value: 1.59e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   8 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 87
Cdd:cd14583  114 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  88 KAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIE 167
Cdd:cd14583  194 KAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKFNHRYGHLDGDPKEVSPVIDQFIE 273

                        170       180
                 ....*....|....*....|....*....
gi 767951332 168 CVWQLMEQFPCAFEFNERFLIHIQHHIYS 196
Cdd:cd14583  274 CVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 8-211 1.27e-150

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: 429.98  E-value: 1.27e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332    8 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 87
Cdd:pfam06602 127 LNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACNDRSPSMDKWLSRLESSGWLKHIKAILDGACLIA 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   88 KAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDG--DPKEISPVIDQF 165
Cdd:pfam06602 207 QAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGftDSKERSPVFLQF 286

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 767951332  166 IECVWQLMEQFPCAFEFNERFLIHIQHHIYSCQFGNFLCNSQKERR 211
Cdd:pfam06602 287 LDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKERV 332
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 8-196 4.14e-147

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: 419.82  E-value: 4.14e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   8 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 87
Cdd:cd14532  114 INAMANKAAGKGYENEDNYSNIKFQFFGIENIHVMRSSLQKLLEVCELKNPSMSAFLSGLESSGWLKHIKAVMDTSVFIA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  88 KAVSEeGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIE 167
Cdd:cd14532  194 KAVSE-GASVLVHCSDGWDRTAQTCSLASLLLDPYYRTIKGFQVLIEKEWLSFGHKFTDRCGHLQGDAKEVSPVFTQFLD 272

                        170       180
                 ....*....|....*....|....*....
gi 767951332 168 CVWQLMEQFPCAFEFNERFLIHIQHHIYS 196
Cdd:cd14532  273 CVWQLMQQFPRAFEFNERFLLTLHDHVYS 301
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 8-196 6.69e-136

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: 391.93  E-value: 6.69e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   8 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 87
Cdd:cd14584  120 LNAMANRAAGKGYENEDNYSNIRFQFIGIENIHVMRSSLQKLLEVCEMKSPSMSDFLTGLENSGWLRHIKAVMDAGVFLA 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  88 KAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIE 167
Cdd:cd14584  200 KAVKEEKASVLVHCSDGWDRTAQVCSLASLLLDPFYRTIKGLMVLIEKEWISMGHKFSQRCGHLDGDPKEVSPVFTQFLE 279

                        170       180
                 ....*....|....*....|....*....
gi 767951332 168 CVWQLMEQFPCAFEFNERFLIHIQHHIYS 196
Cdd:cd14584  280 CVWQLMEQFPCAFEFNEHFLLEIHDHVFS 308
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 8-196 2.33e-125

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: 365.02  E-value: 2.33e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   8 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 87
Cdd:cd14585  114 LNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVCGTKALSVNDFLSGLESSGWLRHIKAVLDAAVFLA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  88 KAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIE 167
Cdd:cd14585  194 KAVAVEGASVLVHCSDGWDRTAQVCSLGSLLLDPYYRTIKGFMVLIEKDWISFGHKFSDRCGQLDGDPKEISPVFTQFLE 273

                        170       180
                 ....*....|....*....|....*....
gi 767951332 168 CVWQLMEQFPCAFEFNERFLIHIQHHIYS 196
Cdd:cd14585  274 CVWQLTEQFPRAFEFSEAFLLQIHEHIHS 302
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
 8-171 2.52e-92

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: 277.89  E-value: 2.52e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   8 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 87
Cdd:cd14507   61 LNAVANRAKGGGYENTEYYPNCELEFLNIENIHAMRDSLNKLRDACLSPNDEESNWLSALESSGWLEHIRLILKGAVRVA 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  88 KAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLD--GDPKEISPVIDQF 165
Cdd:cd14507  141 DLLEKEGTSVLVHCSDGWDRTSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDknSSDEERSPIFLQF 220


                 ....*.
gi 767951332 166 IECVWQ 171
Cdd:cd14507  221 LDCVWQ 226
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
 7-195 4.71e-82

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: 252.37  E-value: 4.71e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   7 NLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCelkSPSMSDFLW--GLENSGWLRHIKAIMDAGI 84
Cdd:cd14535   60 SVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKDIC---FPNIDDSHWlsNLESTHWLEHIKLILAGAV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  85 FIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNldGDPK----EISP 160
Cdd:cd14535  137 RIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGH--GDKNhsdaDRSP 214

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767951332 161 VIDQFIECVWQLMEQFPCAFEFNERFLIHIQHHIY 195
Cdd:cd14535  215 VFLQFIDCVWQMTRQFPNAFEFNEHFLITILDHLY 249
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
 7-195 9.92e-74

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: 231.07  E-value: 9.92e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   7 NLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCelkSPSMSDFLW--GLENSGWLRHIKAIMDAGI 84
Cdd:cd14591   60 SVNAVANKATGGGYEGDDAYQNAELVFLDIHNIHVMRESLKKLKDIV---YPNVEESHWlsSLESTHWLEHIKLVLTGAI 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  85 FIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEI--SPVI 162
Cdd:cd14591  137 QVADKVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGHGDKNHADAdrSPIF 216

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767951332 163 DQFIECVWQLMEQFPCAFEFNERFLIHIQHHIY 195
Cdd:cd14591  217 LQFIDCVWQMSKQFPTAFEFNEQFLITILDHLY 249
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 7-195 1.60e-71

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: 225.68  E-value: 1.60e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   7 NLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCelkSPSMSDFLW--GLENSGWLRHIKAIMDAGI 84
Cdd:cd14590   73 SVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIV---YPNIEESHWlsNLESTHWLEHIKLILAGAL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  85 FIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEI--SPVI 162
Cdd:cd14590  150 RIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADAdrSPVF 229

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767951332 163 DQFIECVWQLMEQFPCAFEFNERFLIHIQHHIY 195
Cdd:cd14590  230 LQFIDCVWQMTRQFPTAFEFNEYFLITILDHLY 262
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
 9-171 6.44e-68

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: 215.39  E-value: 6.44e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   9 NAMANRAAGKGYENEDNYSN--IKFQFIGIENIHVMRNSLQKMLEV------CELKSPSMSDflwGLENSGWLRHIKAIM 80
Cdd:cd17666   67 NAMAQVALGAGTENMDNYKYktAKKIYLGIDNIHVMRDSLNKVTEAlkdgddSNPSYPPLIN---ALKKSNWLKYLAIIL 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  81 DAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNldgdpKEISP 160
Cdd:cd17666  144 QGADLIAKSIHFNHSHVLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFAERSGH-----KETSP 218

                        170
                 ....*....|.
gi 767951332 161 VIDQFIECVWQ 171
Cdd:cd17666  219 VFHQFLDCVYQ 229
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 3-195 1.33e-65

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: 210.22  E-value: 1.33e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   3 IFYLNLNAMA--NRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCelkSPSMSDFLW--GLENSGWLRHIKA 78
Cdd:cd14592   54 IFDARQNSVAdtNKTKGGGYESESAYPNAELVFLEIHNIHVMRESLRKLKEIV---YPSIDEARWlsNVDGTHWLEYIRM 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  79 IMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGD--PK 156
Cdd:cd14592  131 LLAGAVRIADKIESGKTSVVVHCSDGWDRTAQLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGHGDDNhaDA 210

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767951332 157 EISPVIDQFIECVWQLMEQFPCAFEFNERFLIHIQHHIY 195
Cdd:cd14592  211 DRSPIFLQFIDCVWQMTRQFPSAFEFNELFLITILDHLY 249
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 10-171 5.32e-54

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: 182.15  E-value: 5.32e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  10 AMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCElKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKA 89
Cdd:cd14587  146 AVANRAKGGGCECEEYYPNCEVMFMGMANIHSIRNSFQYLRAVCS-QMPDPGNWLSALESTKWLQHLSVMLKAAVLVASA 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  90 VSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDG--DPKEISPVIDQFIE 167
Cdd:cd14587  225 VDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHQENveDQNEQCPVFLQWLD 304


                 ....
gi 767951332 168 CVWQ 171
Cdd:cd14587  305 CVHQ 308
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 10-171 7.54e-54

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: 178.75  E-value: 7.54e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  10 AMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCElKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKA 89
Cdd:cd14533   67 AVANRAKGGGCECPEYYPNCEVVFMNLANIHAIRKSFHSLRALCS-SAPDQPNWLSNLESTKWLHHLSGLLKAALLVVNA 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  90 VSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDG--DPKEISPVIDQFIE 167
Cdd:cd14533  146 VDEEGRPVLVHCSDGWDRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFGHKFADRCGHGVNseDINERCPVFLQWLD 225


                 ....
gi 767951332 168 CVWQ 171
Cdd:cd14533  226 CVHQ 229
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 10-171 1.60e-45

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: 159.80  E-value: 1.60e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  10 AMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCElKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKA 89
Cdd:cd14586  155 AVANRAKGGGCECPEYYPNCEVVFMGMANIHSIRKSFQSLRLLCT-QMPDPANWLSALESTKWLQHLSMLLKSALLVVHA 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  90 VSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHR--YGNLDGDPKEISPVIDQFIE 167
Cdd:cd14586  234 VDRDQRPVLVHCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRcgHGENSDDLNERCPVFLQWLD 313


                 ....
gi 767951332 168 CVWQ 171
Cdd:cd14586  314 CVHQ 317
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 10-171 4.49e-45

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: 155.96  E-value: 4.49e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  10 AMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKA 89
Cdd:cd14536   60 AQQARAKGGGFEPEAHYPQWRRIHKPIERYNVLQESLIKLVEACNDQGHSMDKWLSKLESSNWLSHVKEILTTACLVAQC 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  90 VSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHR-----YGNldGDPKEISPVIDQ 164
Cdd:cd14536  140 IDREGASVLVHGSEGMDSTLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRcaksaYSN--SKQKFESPVFLL 217


                 ....*..
gi 767951332 165 FIECVWQ 171
Cdd:cd14536  218 FLDCVWQ 224
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 6-175 1.03e-38

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: 140.58  E-value: 1.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   6 LNLNAMANRAAGKGYENEdnySNIKFQFIGIE--NIHVMRNSLQKMLEVCELKSPSMSD---FLWGLENSGWLRHIKAIM 80
Cdd:cd14534  102 LVLYVLGEKSQMKGVKAE---SDPKCEFIPVEypEVRQVKASFKKLLRACVPSSAPTEPeqsFLKAVEDSEWLQQLQCLM 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  81 DagifIAKAVSE----EGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRyGNLDGDPK 156
Cdd:cd14534  179 Q----LSGAVVDlldvQGSSVLLCLEDGWDVTTQVSSLSQLLLDPYYRTLEGFRVLVEKEWLAFGHRFSHR-SNLTAASQ 253

                        170       180
                 ....*....|....*....|.
gi 767951332 157 E--ISPVIDQFIECVWQLMEQ 175
Cdd:cd14534  254 SsgFAPVFLQFLDAVHQIHRQ 274
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 34-175 1.79e-30

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: 118.92  E-value: 1.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  34 IGIENIHVMRNSLQKMLEVC---ELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKAVsEEGASVLVHCSDGWDRTAQ 110
Cdd:cd14588  147 IEVFDVRQVKASFKKLMKACvpsCPSTDPSQTYLRTLEESEWLSQLHKLLQVSVLVVELL-DSGSSVLVSLEDGWDITTQ 225

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767951332 111 VCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGN-LDGDPKEISPVIDQFIECVWQLMEQ 175
Cdd:cd14588  226 VVSLVQLLSDPYYRTIEGFRLLVEKEWLSFGHRFSHRGAQtLASQSSGFTPVFLQFLDCVHQIHLQ 291
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 32-175 2.04e-30

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: 118.87  E-value: 2.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  32 QFIGIE--NIHVMRNSLQKMLEVC---ELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKaVSEEGASVLVHCSDGWD 106
Cdd:cd14589  149 EFVPVEfhDIRQVKASFKKLMRACvpsTIPTDSEVTFLKALGESEWFLQLHRIMQLAVVISE-LLESGSSVMVCLEDGWD 227

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332 107 RTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYG-NLDGDPKEISPVIDQFIECVWQLMEQ 175
Cdd:cd14589  228 ITTQVVSLVQLLSDPFYRTLEGFQMLVEKEWLSFGHKFSQRSNlTPNSQGSGFAPIFLQFLDCVHQIHNQ 297
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 36-171 6.40e-26

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: 103.96  E-value: 6.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  36 IENIHVmrnSLQKMLEVCELKSPS---MSDFLW--GLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQ 110
Cdd:cd14537   61 LQDVQA---AYLKLRELCTPDSSEqfwVQDSKWysLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQESDGRDLSCV 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767951332 111 VCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNL--DGDPKEISPVIDQFIECVWQ 171
Cdd:cd14537  138 VSSLVQLLLDPHFRTITGFQSLIQKEWVALGHPFCDRLGHVkpNKTESEESPVFLLFLDCVWQ 200
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 59-172 7.03e-23

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: 95.28  E-value: 7.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  59 SMSDFLWGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWI 138
Cdd:cd14595   82 SDEKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEWV 161

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767951332 139 SFGHKFNHRYGNLDGDPKEISPVIDQFIECVWQL 172
Cdd:cd14595  162 VAGHPFLQRLNLTRESDKEESPVFLLFLDCVWQL 195
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 61-172 2.59e-18

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: 82.97  E-value: 2.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  61 SDFLW--GLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWI 138
Cdd:cd14594   90 TDVKWfsSLESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQSLIQKEWV 169

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767951332 139 SFGHKFNHRYGNLDGDPKEISPVIDQFIECVWQL 172
Cdd:cd14594  170 MGGHCFLDRCNHLRQNDKEEVPVFLLFLDCVWQL 203
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 38-171 3.72e-17

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: 79.17  E-value: 3.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332  38 NIHVMRNSLQKMLEVCELKSPSMSDFLW--GLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVA 115
Cdd:cd14593   60 NIQEIQAAFVKLKQLCVNEPFEETEEKWlsSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLV 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767951332 116 SLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIECVWQ 171
Cdd:cd14593  140 QVMLDPYFRTITGFQSLIQKEWVMAGYRFLDRCNHLKKSSKKESPLFLLFLDCVWQ 195
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
91-195 3.29e-07

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 48.51  E-value: 3.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332    91 SEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTlkgfmvliekdwisfghkfnhrygnldgdpkeisPVIDQFiECVW 170
Cdd:smart00404  36 SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA----------------------------------GEVDIF-DTVK 80

                           90       100
                   ....*....|....*....|....*
gi 767951332   171 QLMEQFPCAFEFNERFLIHIQHHIY 195
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 91-195 3.29e-07

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 48.51  E-value: 3.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332    91 SEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTlkgfmvliekdwisfghkfnhrygnldgdpkeisPVIDQFiECVW 170
Cdd:smart00012  36 SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA----------------------------------GEVDIF-DTVK 80

                           90       100
                   ....*....|....*....|....*
gi 767951332   171 QLMEQFPCAFEFNERFLIHIQHHIY 195
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 1-119 5.29e-05

dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is composed of dual specificity protein phosphatase 3 (DUSP3, also known as VHR), 13B (DUSP13B, also known as TMDP), 26 (DUSP26, also known as MPK8), 13A (DUSP13A, also known as MDSP), dual specificity phosphatase and pro isomerase domain containing 1 (DUPD1), and inactive DUSP27. In general, DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Members of this family are atypical DUSPs; they contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Inactive DUSP27 contains a dual specificity phosphatase-like domain with the active site cysteine substituted to serine.


Pssm-ID: 350365 [Multi-domain]  Cd Length: 148  Bit Score: 42.97  E-value: 5.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951332   1 MEIFYLN-------LNAMANRAAGKGYENEDNYSNIKFQFIGIEnihvmrnslqkmleVCELKSPSMSDFLWglensgwl 73
Cdd:cd14515   17 KNKAKLKklgithvLNAAEGKKNGEVNTNAKFYKGSGIIYLGIP--------------ASDLPTFDISQYFD-------- 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767951332  74 rhikaimDAGIFIAKAVSEEGASVLVHCSDGWDRTAqVCSVASLLL 119
Cdd:cd14515   75 -------EAADFIDKALSDPGGKVLVHCVEGVSRSA-TLVLAYLMI 112
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 56-113 1.75e-04

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 40.80  E-value: 1.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767951332  56 KSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCS 113
Cdd:cd14494   18 PLEADSRFLKQLGVTTIVDLTLAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVA 75
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
 82-153 5.36e-04

dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 isoform A (DUSP13A), also called branching-enzyme interacting DSP or muscle-restricted DSP (MDSP), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP13A is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP13A also functions as a regulator of apoptosis signal-regulating kinase 1 (ASK1), a MAPK kinase kinase, by interacting with its N-terminal domain and inducing ASK1-mediated apoptosis through the activation of caspase-3. This function is independent of phosphatase activity.


Pssm-ID: 350428 [Multi-domain]  Cd Length: 145  Bit Score: 40.12  E-value: 5.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951332  82 AGIFIAKAVSEEGASVLVHCSDGWDRTAQVCsVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDG 153
Cdd:cd14580   73 AAEFIHRALNTPGAKVLVHCAVGVSRSATLV-LAYLMIYHQLSLVQAIKTVKERRWIFPNRGFLKQLRKLDQ 143
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 81-119 5.58e-03

dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also called vaccinia H1-related phosphatase (VHR), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP3 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It favors bisphosphorylated substrates over monophosphorylated ones, and prefers pTyr peptides over pSer/pThr peptides. Reported physiological substrates includes MAPKs ERK1/2, JNK, and p38, as well as STAT5, EGFR, and ErbB2. DUSP3 has been linked to breast and prostate cancer, and may also play a role in thrombosis.


Pssm-ID: 350427 [Multi-domain]  Cd Length: 168  Bit Score: 37.44  E-value: 5.58e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767951332  81 DAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCsVASLLL 119
Cdd:cd14579   95 EAADFIDKALAQKNGRVLVHCREGYSRSPTLV-IAYLML 132
 
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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