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Conserved domains on  [gi|1958683811|ref|XP_038950461|]
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myotubularin-related protein 7 isoform X5 [Rattus norvegicus]

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 ...
 17-205 1.53e-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: 436.70  E-value: 1.53e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  17 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 96
Cdd:cd14583   114 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIA 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  97 KAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIE 176
Cdd:cd14583   194 KAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKFNHRYGHLDGDPKEVSPVIDQFIE 273

                         170       180
                  ....*....|....*....|....*....
gi 1958683811 177 CVWQLMEQFPCAFEFNERFLIHIQHHVYS 205
Cdd:cd14583   274 CVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
 
Name Accession Description Interval E-value
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 17-205 1.53e-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: 436.70  E-value: 1.53e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  17 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 96
Cdd:cd14583   114 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIA 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  97 KAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIE 176
Cdd:cd14583   194 KAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKFNHRYGHLDGDPKEVSPVIDQFIE 273

                         170       180
                  ....*....|....*....|....*....
gi 1958683811 177 CVWQLMEQFPCAFEFNERFLIHIQHHVYS 205
Cdd:cd14583   274 CVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 17-220 2.23e-152

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: 434.98  E-value: 2.23e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  17 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 96
Cdd:pfam06602 127 LNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACNDRSPSMDKWLSRLESSGWLKHIKAILDGACLIA 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  97 KAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDG--DPKEISPVIDQF 174
Cdd:pfam06602 207 QAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGftDSKERSPVFLQF 286

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958683811 175 IECVWQLMEQFPCAFEFNERFLIHIQHHVYSCQFGNFLCNSQKERR 220
Cdd:pfam06602 287 LDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKERV 332
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
100-204 5.42e-07

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 47.74  E-value: 5.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  100 SEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTlkgfmvliekdwisfghkfnhrygnldgdpkeisPVIDQFiECVW 179
Cdd:smart00404  36 SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA----------------------------------GEVDIF-DTVK 80

                           90       100
                   ....*....|....*....|....*
gi 1958683811  180 QLMEQFPCAFEFNERFLIHIQHHVY 204
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
 
Name Accession Description Interval E-value
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 17-205 1.53e-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: 436.70  E-value: 1.53e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  17 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 96
Cdd:cd14583   114 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIA 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  97 KAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIE 176
Cdd:cd14583   194 KAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKFNHRYGHLDGDPKEVSPVIDQFIE 273

                         170       180
                  ....*....|....*....|....*....
gi 1958683811 177 CVWQLMEQFPCAFEFNERFLIHIQHHVYS 205
Cdd:cd14583   274 CVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 17-220 2.23e-152

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: 434.98  E-value: 2.23e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  17 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 96
Cdd:pfam06602 127 LNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACNDRSPSMDKWLSRLESSGWLKHIKAILDGACLIA 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  97 KAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDG--DPKEISPVIDQF 174
Cdd:pfam06602 207 QAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGftDSKERSPVFLQF 286

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958683811 175 IECVWQLMEQFPCAFEFNERFLIHIQHHVYSCQFGNFLCNSQKERR 220
Cdd:pfam06602 287 LDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKERV 332
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 17-205 1.78e-148

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: 423.68  E-value: 1.78e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  17 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 96
Cdd:cd14532   114 INAMANKAAGKGYENEDNYSNIKFQFFGIENIHVMRSSLQKLLEVCELKNPSMSAFLSGLESSGWLKHIKAVMDTSVFIA 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  97 KAVSEeGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIE 176
Cdd:cd14532   194 KAVSE-GASVLVHCSDGWDRTAQTCSLASLLLDPYYRTIKGFQVLIEKEWLSFGHKFTDRCGHLQGDAKEVSPVFTQFLD 272

                         170       180
                  ....*....|....*....|....*....
gi 1958683811 177 CVWQLMEQFPCAFEFNERFLIHIQHHVYS 205
Cdd:cd14532   273 CVWQLMQQFPRAFEFNERFLLTLHDHVYS 301
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 17-205 8.73e-137

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: 394.62  E-value: 8.73e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  17 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 96
Cdd:cd14584   120 LNAMANRAAGKGYENEDNYSNIRFQFIGIENIHVMRSSLQKLLEVCEMKSPSMSDFLTGLENSGWLRHIKAVMDAGVFLA 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  97 KAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIE 176
Cdd:cd14584   200 KAVKEEKASVLVHCSDGWDRTAQVCSLASLLLDPFYRTIKGLMVLIEKEWISMGHKFSQRCGHLDGDPKEVSPVFTQFLE 279

                         170       180
                  ....*....|....*....|....*....
gi 1958683811 177 CVWQLMEQFPCAFEFNERFLIHIQHHVYS 205
Cdd:cd14584   280 CVWQLMEQFPCAFEFNEHFLLEIHDHVFS 308
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 10-205 1.01e-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: 366.18  E-value: 1.01e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  10 VLGVQTILNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIM 89
Cdd:cd14585   107 VMDTRPKLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVCGTKALSVNDFLSGLESSGWLRHIKAVL 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  90 DAGIFIAKAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISP 169
Cdd:cd14585   187 DAAVFLAKAVAVEGASVLVHCSDGWDRTAQVCSLGSLLLDPYYRTIKGFMVLIEKDWISFGHKFSDRCGQLDGDPKEISP 266

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958683811 170 VIDQFIECVWQLMEQFPCAFEFNERFLIHIQHHVYS 205
Cdd:cd14585   267 VFTQFLECVWQLTEQFPRAFEFSEAFLLQIHEHIHS 302
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
 17-180 6.44e-94

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: 282.13  E-value: 6.44e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  17 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIA 96
Cdd:cd14507    61 LNAVANRAKGGGYENTEYYPNCELEFLNIENIHAMRDSLNKLRDACLSPNDEESNWLSALESSGWLEHIRLILKGAVRVA 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  97 KAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLD--GDPKEISPVIDQF 174
Cdd:cd14507   141 DLLEKEGTSVLVHCSDGWDRTSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDknSSDEERSPIFLQF 220


                  ....*.
gi 1958683811 175 IECVWQ 180
Cdd:cd14507   221 LDCVWQ 226
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
 18-204 2.39e-83

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: 255.84  E-value: 2.39e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  18 NAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCelkSPSMSDFLW--GLENSGWLRHIKAIMDAGIFI 95
Cdd:cd14535    62 NAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKDIC---FPNIDDSHWlsNLESTHWLEHIKLILAGAVRI 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  96 AKAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNldGDPK----EISPVI 171
Cdd:cd14535   139 ADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGH--GDKNhsdaDRSPVF 216

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958683811 172 DQFIECVWQLMEQFPCAFEFNERFLIHIQHHVY 204
Cdd:cd14535   217 LQFIDCVWQMTRQFPNAFEFNEHFLITILDHLY 249
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
 17-204 4.72e-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: 232.23  E-value: 4.72e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  17 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCelkSPSMSDFLW--GLENSGWLRHIKAIMDAGIF 94
Cdd:cd14591    61 VNAVANKATGGGYEGDDAYQNAELVFLDIHNIHVMRESLKKLKDIV---YPNVEESHWlsSLESTHWLEHIKLVLTGAIQ 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  95 IAKAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEI--SPVID 172
Cdd:cd14591   138 VADKVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGHGDKNHADAdrSPIFL 217

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958683811 173 QFIECVWQLMEQFPCAFEFNERFLIHIQHHVY 204
Cdd:cd14591   218 QFIDCVWQMSKQFPTAFEFNEQFLITILDHLY 249
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 17-204 1.72e-72

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: 228.76  E-value: 1.72e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  17 LNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCelkSPSMSDFLW--GLENSGWLRHIKAIMDAGIF 94
Cdd:cd14590    74 VNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIV---YPNIEESHWlsNLESTHWLEHIKLILAGALR 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  95 IAKAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEI--SPVID 172
Cdd:cd14590   151 IADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADAdrSPVFL 230

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958683811 173 QFIECVWQLMEQFPCAFEFNERFLIHIQHHVY 204
Cdd:cd14590   231 QFIDCVWQMTRQFPTAFEFNEYFLITILDHLY 262
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
 18-180 3.32e-69

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: 218.85  E-value: 3.32e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  18 NAMANRAAGKGYENEDNYSN--IKFQFIGIENIHVMRNSLQKMLEV------CELKSPSMSDflwGLENSGWLRHIKAIM 89
Cdd:cd17666    67 NAMAQVALGAGTENMDNYKYktAKKIYLGIDNIHVMRDSLNKVTEAlkdgddSNPSYPPLIN---ALKKSNWLKYLAIIL 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  90 DAGIFIAKAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNldgdpKEISP 169
Cdd:cd17666   144 QGADLIAKSIHFNHSHVLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFAERSGH-----KETSP 218

                         170
                  ....*....|.
gi 1958683811 170 VIDQFIECVWQ 180
Cdd:cd17666   219 VFHQFLDCVYQ 229
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 19-204 1.52e-66

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: 212.92  E-value: 1.52e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  19 AMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCelkSPSMSDFLW--GLENSGWLRHIKAIMDAGIFIA 96
Cdd:cd14592    63 ADTNKTKGGGYESESAYPNAELVFLEIHNIHVMRESLRKLKEIV---YPSIDEARWlsNVDGTHWLEYIRMLLAGAVRIA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  97 KAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGD--PKEISPVIDQF 174
Cdd:cd14592   140 DKIESGKTSVVVHCSDGWDRTAQLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGHGDDNhaDADRSPIFLQF 219

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958683811 175 IECVWQLMEQFPCAFEFNERFLIHIQHHVY 204
Cdd:cd14592   220 IDCVWQMTRQFPSAFEFNELFLITILDHLY 249
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 19-180 4.19e-55

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: 182.60  E-value: 4.19e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  19 AMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCElKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKA 98
Cdd:cd14533    67 AVANRAKGGGCECPEYYPNCEVVFMNLANIHAIRKSFHSLRALCS-SAPDQPNWLSNLESTKWLHHLSGLLKAALLVVNA 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  99 VSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDG--DPKEISPVIDQFIE 176
Cdd:cd14533   146 VDEEGRPVLVHCSDGWDRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFGHKFADRCGHGVNseDINERCPVFLQWLD 225


                  ....
gi 1958683811 177 CVWQ 180
Cdd:cd14533   226 CVHQ 229
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 10-180 4.50e-55

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: 184.85  E-value: 4.50e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  10 VLGVQTILNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCElKSPSMSDFLWGLENSGWLRHIKAIM 89
Cdd:cd14587   137 ILDARSYTAAVANRAKGGGCECEEYYPNCEVMFMGMANIHSIRNSFQYLRAVCS-QMPDPGNWLSALESTKWLQHLSVML 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  90 DAGIFIAKAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDG--DPKEI 167
Cdd:cd14587   216 KAAVLVASAVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHQENveDQNEQ 295

                         170
                  ....*....|...
gi 1958683811 168 SPVIDQFIECVWQ 180
Cdd:cd14587   296 CPVFLQWLDCVHQ 308
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 10-180 7.82e-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: 163.65  E-value: 7.82e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  10 VLGVQTILNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCElKSPSMSDFLWGLENSGWLRHIKAIM 89
Cdd:cd14586   146 ILDARSYAAAVANRAKGGGCECPEYYPNCEVVFMGMANIHSIRKSFQSLRLLCT-QMPDPANWLSALESTKWLQHLSMLL 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  90 DAGIFIAKAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHR--YGNLDGDPKEI 167
Cdd:cd14586   225 KSALLVVHAVDRDQRPVLVHCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRcgHGENSDDLNER 304

                         170
                  ....*....|...
gi 1958683811 168 SPVIDQFIECVWQ 180
Cdd:cd14586   305 CPVFLQWLDCVHQ 317
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 19-180 2.65e-44

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: 154.03  E-value: 2.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  19 AMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKA 98
Cdd:cd14536    60 AQQARAKGGGFEPEAHYPQWRRIHKPIERYNVLQESLIKLVEACNDQGHSMDKWLSKLESSNWLSHVKEILTTACLVAQC 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  99 VSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHR-----YGNldGDPKEISPVIDQ 173
Cdd:cd14536   140 IDREGASVLVHGSEGMDSTLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRcaksaYSN--SKQKFESPVFLL 217


                  ....*..
gi 1958683811 174 FIECVWQ 180
Cdd:cd14536   218 FLDCVWQ 224
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 16-184 2.20e-39

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: 142.51  E-value: 2.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  16 ILNAMANRAAGKGYENEdnySNIKFQFIGIE--NIHVMRNSLQKMLEVCELKSPSMSD---FLWGLENSGWLRHIKAIMD 90
Cdd:cd14534   103 VLYVLGEKSQMKGVKAE---SDPKCEFIPVEypEVRQVKASFKKLLRACVPSSAPTEPeqsFLKAVEDSEWLQQLQCLMQ 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  91 agifIAKAVSE----EGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRyGNLDGDPKE 166
Cdd:cd14534   180 ----LSGAVVDlldvQGSSVLLCLEDGWDVTTQVSSLSQLLLDPYYRTLEGFRVLVEKEWLAFGHRFSHR-SNLTAASQS 254

                         170       180
                  ....*....|....*....|
gi 1958683811 167 --ISPVIDQFIECVWQLMEQ 184
Cdd:cd14534   255 sgFAPVFLQFLDAVHQIHRQ 274
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 43-184 4.21e-31

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


Pssm-ID: 350436 [Multi-domain]  Cd Length: 291  Bit Score: 120.84  E-value: 4.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  43 IGIENIHVMRNSLQKMLEVC---ELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKAVsEEGTSVLVHCSDGWDRTAQ 119
Cdd:cd14588   147 IEVFDVRQVKASFKKLMKACvpsCPSTDPSQTYLRTLEESEWLSQLHKLLQVSVLVVELL-DSGSSVLVSLEDGWDITTQ 225

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683811 120 VCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGN-LDGDPKEISPVIDQFIECVWQLMEQ 184
Cdd:cd14588   226 VVSLVQLLSDPYYRTIEGFRLLVEKEWLSFGHRFSHRGAQtLASQSSGFTPVFLQFLDCVHQIHLQ 291
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 41-184 5.87e-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: 5.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  41 QFIGIE--NIHVMRNSLQKMLEVC---ELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKaVSEEGTSVLVHCSDGWD 115
Cdd:cd14589   149 EFVPVEfhDIRQVKASFKKLMRACvpsTIPTDSEVTFLKALGESEWFLQLHRIMQLAVVISE-LLESGSSVMVCLEDGWD 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811 116 RTAQVCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYG-NLDGDPKEISPVIDQFIECVWQLMEQ 184
Cdd:cd14589   228 ITTQVVSLVQLLSDPFYRTLEGFQMLVEKEWLSFGHKFSQRSNlTPNSQGSGFAPIFLQFLDCVHQIHNQ 297
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 45-180 6.15e-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: 6.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  45 IENIHVmrnSLQKMLEVCELKSPS---MSDFLW--GLENSGWLRHIKAIMDAGIFIAKAVSEEGTSVLVHCSDGWDRTAQ 119
Cdd:cd14537    61 LQDVQA---AYLKLRELCTPDSSEqfwVQDSKWysLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQESDGRDLSCV 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683811 120 VCSVASLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNL--DGDPKEISPVIDQFIECVWQ 180
Cdd:cd14537   138 VSSLVQLLLDPHFRTITGFQSLIQKEWVALGHPFCDRLGHVkpNKTESEESPVFLLFLDCVWQ 200
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 68-181 7.30e-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: 7.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  68 SMSDFLWGLENSGWLRHIKAIMDAGIFIAKAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWI 147
Cdd:cd14595    82 SDEKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEWV 161

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958683811 148 SFGHKFNHRYGNLDGDPKEISPVIDQFIECVWQL 181
Cdd:cd14595   162 VAGHPFLQRLNLTRESDKEESPVFLLFLDCVWQL 195
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 70-181 1.35e-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: 86.43  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  70 SDFLW--GLENSGWLRHIKAIMDAGIFIAKAVSEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTLKGFMVLIEKDWI 147
Cdd:cd14594    90 TDVKWfsSLESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQSLIQKEWV 169

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958683811 148 SFGHKFNHRYGNLDGDPKEISPVIDQFIECVWQL 181
Cdd:cd14594   170 MGGHCFLDRCNHLRQNDKEEVPVFLLFLDCVWQL 203
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 47-180 2.49e-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: 2.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  47 NIHVMRNSLQKMLEVCELKSPSMSDFLW--GLENSGWLRHIKAIMDAGIFIAKAVSEEGTSVLVHCSDGWDRTAQVCSVA 124
Cdd:cd14593    60 NIQEIQAAFVKLKQLCVNEPFEETEEKWlsSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLV 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683811 125 SLLLDPYYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIECVWQ 180
Cdd:cd14593   140 QVMLDPYFRTITGFQSLIQKEWVMAGYRFLDRCNHLKKSSKKESPLFLLFLDCVWQ 195
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
100-204 5.42e-07

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 47.74  E-value: 5.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  100 SEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTlkgfmvliekdwisfghkfnhrygnldgdpkeisPVIDQFiECVW 179
Cdd:smart00404  36 SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA----------------------------------GEVDIF-DTVK 80

                           90       100
                   ....*....|....*....|....*
gi 1958683811  180 QLMEQFPCAFEFNERFLIHIQHHVY 204
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 100-204 5.42e-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: 47.74  E-value: 5.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  100 SEEGTSVLVHCSDGWDRTAQVCSVASLLLDPYYRTlkgfmvliekdwisfghkfnhrygnldgdpkeisPVIDQFiECVW 179
Cdd:smart00012  36 SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA----------------------------------GEVDIF-DTVK 80

                           90       100
                   ....*....|....*....|....*
gi 1958683811  180 QLMEQFPCAFEFNERFLIHIQHHVY 204
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 11-128 1.52e-06

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: 47.59  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683811  11 LGVQTILNAMANRAAGKGYENEDNYSNIKFQFIGIEnihvmrnslqkmleVCELKSPSMSDFLWglensgwlrhikaimD 90
Cdd:cd14515    25 LGITHVLNAAEGKKNGEVNTNAKFYKGSGIIYLGIP--------------ASDLPTFDISQYFD---------------E 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958683811  91 AGIFIAKAVSEEGTSVLVHCSDGWDRTAqVCSVASLLL 128
Cdd:cd14515    76 AADFIDKALSDPGGKVLVHCVEGVSRSA-TLVLAYLMI 112
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 65-122 2.08e-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: 2.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683811  65 KSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKAVSEEGTSVLVHCSDGWDRTAQVCS 122
Cdd:cd14494    18 PLEADSRFLKQLGVTTIVDLTLAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVA 75
 
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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