NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568954917|ref|XP_006509530|]
View 

myotubularin-related protein 7 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
1-212 1.71e-172

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: 421693  Cd Length: 302  Bit Score: 485.23  E-value: 1.71e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   1 MLQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFL 80
Cdd:cd14583   91 MLQAIRKANPGSDFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELRSPSMGDFL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  81 WGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKF 160
Cdd:cd14583  171 WGLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKF 250
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568954917 161 NHRYGNLDGDPKEISPVIDQFIECVWQLTEQFPCAFEFNERFLTHIQHHVYS 212
Cdd:cd14583  251 NHRYGHLDGDPKEVSPVIDQFIECVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
 
Name Accession Description Interval E-value
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
1-212 1.71e-172

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  Cd Length: 302  Bit Score: 485.23  E-value: 1.71e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   1 MLQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFL 80
Cdd:cd14583   91 MLQAIRKANPGSDFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELRSPSMGDFL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  81 WGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKF 160
Cdd:cd14583  171 WGLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKF 250
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568954917 161 NHRYGNLDGDPKEISPVIDQFIECVWQLTEQFPCAFEFNERFLTHIQHHVYS 212
Cdd:cd14583  251 NHRYGHLDGDPKEVSPVIDQFIECVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
1-227 6.76e-164

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: 399535  Cd Length: 330  Bit Score: 464.26  E-value: 6.76e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917    1 MLQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFL 80
Cdd:pfam06602 102 LLNAIFKSNPYSKKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACNDRSSSMDKWL 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   81 WGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKF 160
Cdd:pfam06602 182 SRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKF 261
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568954917  161 NHRYGNLDG--DPKEISPVIDQFIECVWQLTEQFPCAFEFNERFLTHIQHHVYSCQFGNFLCNSQKERR 227
Cdd:pfam06602 262 ADRCGHLAYfsDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLDHLYSCQFGTFLCNSEKERV 330
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
107-143 2.04e-06

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: 46.20  E-value: 2.04e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568954917   107 SEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLK 143
Cdd:smart00012  36 SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE 72
 
Name Accession Description Interval E-value
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
1-212 1.71e-172

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  Cd Length: 302  Bit Score: 485.23  E-value: 1.71e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   1 MLQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFL 80
Cdd:cd14583   91 MLQAIRKANPGSDFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELRSPSMGDFL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  81 WGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKF 160
Cdd:cd14583  171 WGLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKF 250
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568954917 161 NHRYGNLDGDPKEISPVIDQFIECVWQLTEQFPCAFEFNERFLTHIQHHVYS 212
Cdd:cd14583  251 NHRYGHLDGDPKEVSPVIDQFIECVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
1-212 2.12e-166

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  Cd Length: 301  Bit Score: 469.52  E-value: 2.12e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   1 MLQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFL 80
Cdd:cd14532   91 LLQAIRKANPNSKFMYVVDTRPKINAMANKAAGKGYENEDNYSNIKFQFFGIENIHVMRSSLQKLLEVCELKNPSMSAFL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  81 WGLENSGWLRHIKAIMDAGIFIAKAVSeEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKF 160
Cdd:cd14532  171 SGLESSGWLKHIKAVMDTSVFIAKAVS-EGASVLVHCSDGWDRTAQTCSLASLLLDPYYRTIKGFQVLIEKEWLSFGHKF 249
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568954917 161 NHRYGNLDGDPKEISPVIDQFIECVWQLTEQFPCAFEFNERFLTHIQHHVYS 212
Cdd:cd14532  250 TDRCGHLQGDAKEVSPVFTQFLDCVWQLMQQFPRAFEFNERFLLTLHDHVYS 301
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
1-227 6.76e-164

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: 399535  Cd Length: 330  Bit Score: 464.26  E-value: 6.76e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917    1 MLQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFL 80
Cdd:pfam06602 102 LLNAIFKSNPYSKKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACNDRSSSMDKWL 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   81 WGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKF 160
Cdd:pfam06602 182 SRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKF 261
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568954917  161 NHRYGNLDG--DPKEISPVIDQFIECVWQLTEQFPCAFEFNERFLTHIQHHVYSCQFGNFLCNSQKERR 227
Cdd:pfam06602 262 ADRCGHLAYfsDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLDHLYSCQFGTFLCNSEKERV 330
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
1-212 1.81e-154

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  Cd Length: 308  Bit Score: 439.69  E-value: 1.81e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   1 MLQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFL 80
Cdd:cd14584   97 MLQAISKANPGSPFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIRFQFIGIENIHVMRSSLQKLLEVCEMKSPSMSDFL 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  81 WGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKF 160
Cdd:cd14584  177 TGLENSGWLRHIKAVMDAGVFLAKAVKEEKASVLVHCSDGWDRTAQVCSLASLLLDPFYRTIKGLMVLIEKEWISMGHKF 256
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568954917 161 NHRYGNLDGDPKEISPVIDQFIECVWQLTEQFPCAFEFNERFLTHIQHHVYS 212
Cdd:cd14584  257 SQRCGHLDGDPKEVSPVFTQFLECVWQLMEQFPCAFEFNEHFLLEIHDHVFS 308
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
1-212 5.17e-141

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  Cd Length: 302  Bit Score: 405.08  E-value: 5.17e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   1 MLQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFL 80
Cdd:cd14585   91 MLQAISKANPNNRYMYVMDTRPKLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVCGTKALSVNDFL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  81 WGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKF 160
Cdd:cd14585  171 SGLESSGWLRHIKAVLDAAVFLAKAVAVEGASVLVHCSDGWDRTAQVCSLGSLLLDPYYRTIKGFMVLIEKDWISFGHKF 250
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568954917 161 NHRYGNLDGDPKEISPVIDQFIECVWQLTEQFPCAFEFNERFLTHIQHHVYS 212
Cdd:cd14585  251 SDRCGQLDGDPKEISPVFTQFLECVWQLTEQFPRAFEFSEAFLLQIHEHIHS 302
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
1-187 3.99e-105

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: 311.02  E-value: 3.99e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   1 MLQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFL 80
Cdd:cd14507   38 LLNAIRKASPSSKKLYIVDARPKLNAVANRAKGGGYENTEYYPNCELEFLNIENIHAMRDSLNKLRDACLSPNDEESNWL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  81 WGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKF 160
Cdd:cd14507  118 SALESSGWLEHIRLILKGAVRVADLLEKEGTSVLVHCSDGWDRTSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKF 197
                        170       180
                 ....*....|....*....|....*....
gi 568954917 161 NHRYGNLD--GDPKEISPVIDQFIECVWQ 187
Cdd:cd14507  198 ADRCGHGDknSSDEERSPIFLQFLDCVWQ 226
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
2-211 2.46e-90

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: 273.94  E-value: 2.46e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   2 LQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCelkSPSMSDFLW 81
Cdd:cd14535   39 LQLIMDANAQSHKLFIMDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKDIC---FPNIDDSHW 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  82 --GLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHK 159
Cdd:cd14535  116 lsNLESTHWLEHIKLILAGAVRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHK 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568954917 160 FNHRYGNldGDPK----EISPVIDQFIECVWQLTEQFPCAFEFNERFLTHIQHHVY 211
Cdd:cd14535  196 FAQRIGH--GDKNhsdaDRSPVFLQFIDCVWQMTRQFPNAFEFNEHFLITILDHLY 249
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
2-211 1.13e-79

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: 246.86  E-value: 1.13e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   2 LQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCelkSPSMSDFLW 81
Cdd:cd14591   39 LDIIREANGQTSKLTIYDARPSVNAVANKATGGGYEGDDAYQNAELVFLDIHNIHVMRESLKKLKDIV---YPNVEESHW 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  82 --GLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHK 159
Cdd:cd14591  116 lsSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHK 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568954917 160 FNHRYGNLDGDPKEI--SPVIDQFIECVWQLTEQFPCAFEFNERFLTHIQHHVY 211
Cdd:cd14591  196 FASRIGHGDKNHADAdrSPIFLQFIDCVWQMSKQFPTAFEFNEQFLITILDHLY 249
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
2-211 2.42e-79

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: 246.48  E-value: 2.42e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   2 LQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCelkSPSMSDFLW 81
Cdd:cd14590   52 LQAIMDSNAQSHKIFIFDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIV---YPNIEESHW 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  82 --GLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHK 159
Cdd:cd14590  129 lsNLESTHWLEHIKLILAGALRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHR 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568954917 160 FNHRYGNLDGDPKEI--SPVIDQFIECVWQLTEQFPCAFEFNERFLTHIQHHVY 211
Cdd:cd14590  209 FQLRVGHGDKNHADAdrSPVFLQFIDCVWQMTRQFPTAFEFNEYFLITILDHLY 262
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
17-187 4.61e-73

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: 228.87  E-value: 4.61e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  17 VVDTRPKLNAMANRAAGKGYENEDNYSN--IKFQFIGIENIHVMRNSLQKMLEV------CELKSPSMSDflwGLENSGW 88
Cdd:cd17666   59 IVDARPTTNAMAQVALGAGTENMDNYKYktAKKIYLGIDNIHVMRDSLNKVTEAlkdgddSNPSYPPLIN---ALKKSNW 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  89 LRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNld 168
Cdd:cd17666  136 LKYLAIILQGADLIAKSIHFNHSHVLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFAERSGH-- 213
                        170
                 ....*....|....*....
gi 568954917 169 gdpKEISPVIDQFIECVWQ 187
Cdd:cd17666  214 ---KETSPVFHQFLDCVYQ 229
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
2-211 1.27e-69

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: 221.01  E-value: 1.27e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   2 LQAIRKANPGSDFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCelkSPSMSDFLW 81
Cdd:cd14592   39 LQTIMDANAQSHKLIIFDARQNSVADTNKTKGGGYESESAYPNAELVFLEIHNIHVMRESLRKLKEIV---YPSIDEARW 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  82 --GLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHK 159
Cdd:cd14592  116 lsNVDGTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGWDRTAQLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHR 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568954917 160 FNHRYGNLDGD--PKEISPVIDQFIECVWQLTEQFPCAFEFNERFLTHIQHHVY 211
Cdd:cd14592  196 FALRVGHGDDNhaDADRSPIFLQFIDCVWQMTRQFPSAFEFNELFLITILDHLY 249
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
1-187 8.09e-58

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: 189.54  E-value: 8.09e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   1 MLQAIRKANPGSD---FIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCElKSPSMS 77
Cdd:cd14533   39 LLQAIAEACASNAspkKLLIVDARSYAAAVANRAKGGGCECPEYYPNCEVVFMNLANIHAIRKSFHSLRALCS-SAPDQP 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  78 DFLWGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFG 157
Cdd:cd14533  118 NWLSNLESTKWLHHLSGLLKAALLVVNAVDEEGRPVLVHCSDGWDRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFG 197
                        170       180       190
                 ....*....|....*....|....*....|..
gi 568954917 158 HKFNHRYGNLDG--DPKEISPVIDQFIECVWQ 187
Cdd:cd14533  198 HKFADRCGHGVNseDINERCPVFLQWLDCVHQ 229
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
17-187 2.27e-56

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  Cd Length: 308  Bit Score: 188.70  E-value: 2.27e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  17 VVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCElKSPSMSDFLWGLENSGWLRHIKAIM 96
Cdd:cd14587  137 ILDARSYTAAVANRAKGGGCECEEYYPNCEVMFMGMANIHSIRNSFQYLRAVCS-QMPDPGNWLSALESTKWLQHLSVML 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  97 DAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDG--DPKEI 174
Cdd:cd14587  216 KAAVLVASAVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHQENveDQNEQ 295
                        170
                 ....*....|...
gi 568954917 175 SPVIDQFIECVWQ 187
Cdd:cd14587  296 CPVFLQWLDCVHQ 308
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
16-187 8.88e-49

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: 165.97  E-value: 8.88e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  16 YVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAI 95
Cdd:cd14536   50 YIIDTRSKNVAQQARAKGGGFEPEAHYPQWRRIHKPIERYNVLQESLIKLVEACNDQGHSMDKWLSKLESSNWLSHVKEI 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  96 MDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHR-----YGNldGD 170
Cdd:cd14536  130 LTTACLVAQCIDREGASVLVHGSEGMDSTLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRcaksaYSN--SK 207
                        170
                 ....*....|....*..
gi 568954917 171 PKEISPVIDQFIECVWQ 187
Cdd:cd14536  208 QKFESPVFLLFLDCVWQ 224
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
15-187 1.37e-47

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: 165.58  E-value: 1.37e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  15 IYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCElKSPSMSDFLWGLENSGWLRHIKA 94
Cdd:cd14586  144 LLILDARSYAAAVANRAKGGGCECPEYYPNCEVVFMGMANIHSIRKSFQSLRLLCT-QMPDPANWLSALESTKWLQHLSM 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  95 IMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHR--YGNLDGDPK 172
Cdd:cd14586  223 LLKSALLVVHAVDRDQRPVLVHCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRcgHGENSDDLN 302
                        170
                 ....*....|....*
gi 568954917 173 EISPVIDQFIECVWQ 187
Cdd:cd14586  303 ERCPVFLQWLDCVHQ 317
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
24-191 1.96e-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  Cd Length: 274  Bit Score: 140.19  E-value: 1.96e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  24 LNAMANRAAGKGYENEdnySNIKFQFIGIE--NIHVMRNSLQKMLEVCELKSPSMSD---FLWGLENSGWLRHIKAIMDa 98
Cdd:cd14534  104 LYVLGEKSQMKGVKAE---SDPKCEFIPVEypEVRQVKASFKKLLRACVPSSAPTEPeqsFLKAVEDSEWLQQLQCLMQ- 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  99 gifIAKAVSE----EGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRyGNLDGDPKE- 173
Cdd:cd14534  180 ---LSGAVVDlldvQGSSVLLCLEDGWDVTTQVSSLSQLLLDPYYRTLEGFRVLVEKEWLAFGHRFSHR-SNLTAASQSs 255
                        170
                 ....*....|....*....
gi 568954917 174 -ISPVIDQFIECVWQLTEQ 191
Cdd:cd14534  256 gFAPVFLQFLDAVHQIHRQ 274
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
50-191 5.15e-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  Cd Length: 291  Bit Score: 120.46  E-value: 5.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  50 IGIENIHVMRNSLQKMLEVC---ELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKAVsEEGASVLVHCSDGWDRTAQ 126
Cdd:cd14588  147 IEVFDVRQVKASFKKLMKACvpsCPSTDPSQTYLRTLEESEWLSQLHKLLQVSVLVVELL-DSGSSVLVSLEDGWDITTQ 225
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568954917 127 VCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGN-LDGDPKEISPVIDQFIECVWQLTEQ 191
Cdd:cd14588  226 VVSLVQLLSDPYYRTIEGFRLLVEKEWLSFGHRFSHRGAQtLASQSSGFTPVFLQFLDCVHQIHLQ 291
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
48-191 5.68e-31

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: 120.41  E-value: 5.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  48 QFIGIE--NIHVMRNSLQKMLEVC---ELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKaVSEEGASVLVHCSDGWD 122
Cdd:cd14589  149 EFVPVEfhDIRQVKASFKKLMRACvpsTIPTDSEVTFLKALGESEWFLQLHRIMQLAVVISE-LLESGSSVMVCLEDGWD 227
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917 123 RTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYG-NLDGDPKEISPVIDQFIECVWQLTEQ 191
Cdd:cd14589  228 ITTQVVSLVQLLSDPFYRTLEGFQMLVEKEWLSFGHKFSQRSNlTPNSQGSGFAPIFLQFLDCVHQIHNQ 297
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
1-187 3.57e-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: 104.73  E-value: 3.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917   1 MLQAIRKANPGSDFIYVVDTrpklnamanraagkgyenEDNYSNIKfqfigieNIHVmrnSLQKMLEVCELKSPS---MS 77
Cdd:cd14537   35 MLEAIRKSHPNLKKPKVIDL------------------DKLLPSLQ-------DVQA---AYLKLRELCTPDSSEqfwVQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  78 DFLW--GLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWIS 155
Cdd:cd14537   87 DSKWysLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQESDGRDLSCVVSSLVQLLLDPHFRTITGFQSLIQKEWVA 166
                        170       180       190
                 ....*....|....*....|....*....|....
gi 568954917 156 FGHKFNHRYGNL--DGDPKEISPVIDQFIECVWQ 187
Cdd:cd14537  167 LGHPFCDRLGHVkpNKTESEESPVFLLFLDCVWQ 200
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
75-188 8.65e-22

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: 92.59  E-value: 8.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  75 SMSDFLWGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWI 154
Cdd:cd14595   82 SDEKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEWV 161
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568954917 155 SFGHKFNHRYGNLDGDPKEISPVIDQFIECVWQL 188
Cdd:cd14595  162 VAGHPFLQRLNLTRESDKEESPVFLLFLDCVWQL 195
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
77-188 7.75e-19

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: 84.51  E-value: 7.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  77 SDFLW--GLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWI 154
Cdd:cd14594   90 TDVKWfsSLESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQSLIQKEWV 169
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568954917 155 SFGHKFNHRYGNLDGDPKEISPVIDQFIECVWQL 188
Cdd:cd14594  170 MGGHCFLDRCNHLRQNDKEEVPVFLLFLDCVWQL 203
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
54-187 2.50e-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: 79.94  E-value: 2.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  54 NIHVMRNSLQKMLEVCELKSPSMSDFLW--GLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVA 131
Cdd:cd14593   60 NIQEIQAAFVKLKQLCVNEPFEETEEKWlsSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLV 139
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568954917 132 SLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIECVWQ 187
Cdd:cd14593  140 QVMLDPYFRTITGFQSLIQKEWVMAGYRFLDRCNHLKKSSKKESPLFLLFLDCVWQ 195
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
107-143 2.04e-06

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: 46.20  E-value: 2.04e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568954917   107 SEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLK 143
Cdd:smart00012  36 SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE 72
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
107-143 2.04e-06

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 46.20  E-value: 2.04e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568954917   107 SEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTLK 143
Cdd:smart00404  36 SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE 72
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
24-135 7.68e-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  Cd Length: 148  Bit Score: 42.58  E-value: 7.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954917  24 LNAMANRAAGKGYENEDNYSNIKFQFIGIEnihvmrnslqkmleVCELKSPSMSDFLWglensgwlrhikaimDAGIFIA 103
Cdd:cd14515   31 LNAAEGKKNGEVNTNAKFYKGSGIIYLGIP--------------ASDLPTFDISQYFD---------------EAADFID 81
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568954917 104 KAVSEEGASVLVHCSDGWDRTAqVCSVASLLL 135
Cdd:cd14515   82 KALSDPGGKVLVHCVEGVSRSA-TLVLAYLMI 112
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
72-129 1.73e-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: 1.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568954917  72 KSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCS 129
Cdd:cd14494   18 PLEADSRFLKQLGVTTIVDLTLAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVA 75
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
98-169 2.81e-03

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  Cd Length: 145  Bit Score: 38.20  E-value: 2.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568954917  98 AGIFIAKAVSEEGASVLVHCSDGWDRTAQVCsVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDG 169
Cdd:cd14580   73 AAEFIHRALNTPGAKVLVHCAVGVSRSATLV-LAYLMIYHQLSLVQAIKTVKERRWIFPNRGFLKQLRKLDQ 143
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
97-135 5.19e-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  Cd Length: 168  Bit Score: 37.44  E-value: 5.19e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 568954917  97 DAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCsVASLLL 135
Cdd:cd14579   95 EAADFIDKALAQKNGRVLVHCREGYSRSPTLV-IAYLML 132
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH