NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|801400033|ref|XP_012060555|]
View 

Protein Classification

PH-like and PTP-MTMR10-like domain-containing protein (domain architecture ID 13117763)

protein containing domains PH-like, PTP-MTMR10-like, and 3-PAP

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-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
257-452 3.95e-110

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: 330.07  E-value: 3.95e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 257 NRPPVWSWTSSHGAALVKMSELLPTITERMQENIMFENVRKSHPQKIPPVVIELNKEI-NVKLIAASFTKFINLCTPENI 335
Cdd:cd14537    1 GRPPVWCWSHPNGAALVRMAELLPTITDRTQENKMLEAIRKSHPNLKKPKVIDLDKLLpSLQDVQAAYLKLRELCTPDSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 336 RQFWIQDNNFYSLLENTKWLKYISYCLQKTVEVCDHL-NLGISVILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQSLL 414
Cdd:cd14537   81 EQFWVQDSKWYSLLENTKWLHYVSACLKKASEAAEALeSRGRSVVLQESDGRDLSCVVSSLVQLLLDPHFRTITGFQSLI 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 801400033 415 QKEWVAGGHPFCDRLGHIV--KTNSEKSPLFLLYLDCVWQ 452
Cdd:cd14537  161 QKEWVALGHPFCDRLGHVKpnKTESEESPVFLLFLDCVWQ 200
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
33-182 2.13e-18

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13348:

Pssm-ID: 418428  Cd Length: 178  Bit Score: 83.36  E-value: 2.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  33 ENSIKLLPGEVLIAEAQSVLMFLPVSDLKQGISGVLSVTNFKLTFVTSGDSNGENVTRQQNHLYGYTDTCLTNIDEIYiM 112
Cdd:cd13348   15 EVNPHLLPGEVVLCEANTVLKYTQDDGSQRGVYGRLVCTNFRIAFLGDDAPQDDNSKQFKNKIYGENDITLQCVDQIY-G 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 801400033 113 IGDKKRKLVPGNTVPSKVKGIFII-CKNLRTWSFSFKFSPVGHGKNLLTALLHHAF-PSRHQLLFAYDYKEA 182
Cdd:cd13348   94 VYDEKKKLITGGLVKNKYPEKLIIhCKDLRVFQFCLRYTKEEEVKRIVSGIIHHTQePKLLKRLFLFSYARA 165
3-PAP super family cl13953
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
538-591 5.59e-08

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


The actual alignment was detected with superfamily member pfam12578:

Pssm-ID: 403693  Cd Length: 128  Bit Score: 51.63  E-value: 5.59e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 801400033  538 TENETIIKPLYAVSSLELWTQCYFRWIPTLEIRNGGQ----RHIELY---IRLLQNDINQH 591
Cdd:pfam12578  62 ADLHGLLLPQLSGPHIKLWKQCYLRWVPEAQINHGGPitafHKLSLLadeVDALQRLLRQY 122
 
Name Accession Description Interval E-value
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
257-452 3.95e-110

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: 330.07  E-value: 3.95e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 257 NRPPVWSWTSSHGAALVKMSELLPTITERMQENIMFENVRKSHPQKIPPVVIELNKEI-NVKLIAASFTKFINLCTPENI 335
Cdd:cd14537    1 GRPPVWCWSHPNGAALVRMAELLPTITDRTQENKMLEAIRKSHPNLKKPKVIDLDKLLpSLQDVQAAYLKLRELCTPDSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 336 RQFWIQDNNFYSLLENTKWLKYISYCLQKTVEVCDHL-NLGISVILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQSLL 414
Cdd:cd14537   81 EQFWVQDSKWYSLLENTKWLHYVSACLKKASEAAEALeSRGRSVVLQESDGRDLSCVVSSLVQLLLDPHFRTITGFQSLI 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 801400033 415 QKEWVAGGHPFCDRLGHIV--KTNSEKSPLFLLYLDCVWQ 452
Cdd:cd14537  161 QKEWVALGHPFCDRLGHVKpnKTESEESPVFLLFLDCVWQ 200
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
196-491 8.70e-73

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: 237.76  E-value: 8.70e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  196 DISDWQNELKRtLCSDeTKKGWRLSMVNAKFQLCPSLSQYVVVPASVTDSQLTDAARHFQGNRPPVWSW-TSSHGAALVK 274
Cdd:pfam06602   6 DLYDPEAEFAR-QGLP-SKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYrHKENGAVITR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  275 MSELLPTITERM--QENIMFENVRKSHPQKIPPVVIELNKEINVKLIAA-----------------------------SF 323
Cdd:pfam06602  84 SSQPLVGLNGKRciEDEKLLNAIFKSNPYSKKLYIVDARPKLNAMANRAkgggyenednypnckkiflgienihvmrdSL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  324 TKFINLCTPENIrqfwiQDNNFYSLLENTKWLKYISYCLQKTVEVCDHLNL-GISVILQ--EGAarDLCCVISSLAQLLL 400
Cdd:pfam06602 164 NKLVEACNDRSS-----SMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLeGSSVLVHcsDGW--DRTAQLTSLAQLLL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  401 DHHFRTIVGFQSLLQKEWVAGGHPFCDRLGHIVKTNSEK--SPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWDAAHVS 478
Cdd:pfam06602 237 DPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAYFSDSKerSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLDHLYSC 316
                         330
                  ....*....|...
gi 801400033  479 IFDTFIFNCERDR 491
Cdd:pfam06602 317 QFGTFLCNSEKER 329
PH-GRAM_MTMR12 cd13348
Myotubularian (MTM) related 12 protein (MTMR12) Pleckstrin Homology-Glucosyltransferases, ...
33-182 2.13e-18

Myotubularian (MTM) related 12 protein (MTMR12) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR12 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Glu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR12 contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, a SET interaction domain, and a C-terminal a coiled-coil domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date.


Pssm-ID: 275418  Cd Length: 178  Bit Score: 83.36  E-value: 2.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  33 ENSIKLLPGEVLIAEAQSVLMFLPVSDLKQGISGVLSVTNFKLTFVTSGDSNGENVTRQQNHLYGYTDTCLTNIDEIYiM 112
Cdd:cd13348   15 EVNPHLLPGEVVLCEANTVLKYTQDDGSQRGVYGRLVCTNFRIAFLGDDAPQDDNSKQFKNKIYGENDITLQCVDQIY-G 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 801400033 113 IGDKKRKLVPGNTVPSKVKGIFII-CKNLRTWSFSFKFSPVGHGKNLLTALLHHAF-PSRHQLLFAYDYKEA 182
Cdd:cd13348   94 VYDEKKKLITGGLVKNKYPEKLIIhCKDLRVFQFCLRYTKEEEVKRIVSGIIHHTQePKLLKRLFLFSYARA 165
3-PAP pfam12578
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
538-591 5.59e-08

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


Pssm-ID: 403693  Cd Length: 128  Bit Score: 51.63  E-value: 5.59e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 801400033  538 TENETIIKPLYAVSSLELWTQCYFRWIPTLEIRNGGQ----RHIELY---IRLLQNDINQH 591
Cdd:pfam12578  62 ADLHGLLLPQLSGPHIKLWKQCYLRWVPEAQINHGGPitafHKLSLLadeVDALQRLLRQY 122
 
Name Accession Description Interval E-value
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
257-452 3.95e-110

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: 330.07  E-value: 3.95e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 257 NRPPVWSWTSSHGAALVKMSELLPTITERMQENIMFENVRKSHPQKIPPVVIELNKEI-NVKLIAASFTKFINLCTPENI 335
Cdd:cd14537    1 GRPPVWCWSHPNGAALVRMAELLPTITDRTQENKMLEAIRKSHPNLKKPKVIDLDKLLpSLQDVQAAYLKLRELCTPDSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 336 RQFWIQDNNFYSLLENTKWLKYISYCLQKTVEVCDHL-NLGISVILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQSLL 414
Cdd:cd14537   81 EQFWVQDSKWYSLLENTKWLHYVSACLKKASEAAEALeSRGRSVVLQESDGRDLSCVVSSLVQLLLDPHFRTITGFQSLI 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 801400033 415 QKEWVAGGHPFCDRLGHIV--KTNSEKSPLFLLYLDCVWQ 452
Cdd:cd14537  161 QKEWVALGHPFCDRLGHVKpnKTESEESPVFLLFLDCVWQ 200
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
196-491 8.70e-73

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: 237.76  E-value: 8.70e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  196 DISDWQNELKRtLCSDeTKKGWRLSMVNAKFQLCPSLSQYVVVPASVTDSQLTDAARHFQGNRPPVWSW-TSSHGAALVK 274
Cdd:pfam06602   6 DLYDPEAEFAR-QGLP-SKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYrHKENGAVITR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  275 MSELLPTITERM--QENIMFENVRKSHPQKIPPVVIELNKEINVKLIAA-----------------------------SF 323
Cdd:pfam06602  84 SSQPLVGLNGKRciEDEKLLNAIFKSNPYSKKLYIVDARPKLNAMANRAkgggyenednypnckkiflgienihvmrdSL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  324 TKFINLCTPENIrqfwiQDNNFYSLLENTKWLKYISYCLQKTVEVCDHLNL-GISVILQ--EGAarDLCCVISSLAQLLL 400
Cdd:pfam06602 164 NKLVEACNDRSS-----SMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLeGSSVLVHcsDGW--DRTAQLTSLAQLLL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  401 DHHFRTIVGFQSLLQKEWVAGGHPFCDRLGHIVKTNSEK--SPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWDAAHVS 478
Cdd:pfam06602 237 DPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAYFSDSKerSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLDHLYSC 316
                         330
                  ....*....|...
gi 801400033  479 IFDTFIFNCERDR 491
Cdd:pfam06602 317 QFGTFLCNSEKER 329
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
258-452 1.98e-52

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: 178.93  E-value: 1.98e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 258 RPPVWSWTSSHGAALVKMSELLPTITERMQENIMFENVRKSHPQKIPPVVIELNKEI-NVKLIAASFTKFINLCTPENIR 336
Cdd:cd14593    2 RIPLWCWNHPNGSALVRMANIKDLLQQRKIDQRICNAITRSHPLRSDVYKSDLDKTLpNIQEIQAAFVKLKQLCVNEPFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 337 QfwiQDNNFYSLLENTKWLKYISYCLQKTVEV-----CDHlnlgISVILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQ 411
Cdd:cd14593   82 E---TEEKWLSSLESTRWLEYVRAFLKHSAELvymleSKH----VSVILQEEEGRDLSCVVASLVQVMLDPYFRTITGFQ 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 801400033 412 SLLQKEWVAGGHPFCDRLGHIVKTNSEKSPLFLLYLDCVWQ 452
Cdd:cd14593  155 SLIQKEWVMAGYRFLDRCNHLKKSSKKESPLFLLFLDCVWQ 195
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
260-453 3.36e-50

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: 173.10  E-value: 3.36e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 260 PVWSWTSSHGAALVKMSELLPT---ITERMQENI---MFENVRKSHPQKIPPVviELNKEI-NVKLIAASFTKFINLCTP 332
Cdd:cd14594    4 PIWCWSCHNGCALLKMSALPKEqddVALQDQKSFldrIYKTLSRPPYESVKTE--DLSASLpSLQEIQTAYNRFKQLFLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 333 ENIRQFWIQDNNFYSLLENTKWLKYISYCLQKTVEVCDHLNL-GISVILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQ 411
Cdd:cd14594   82 DNSTDFWDTDVKWFSSLESSNWLEIIRQCLKKAVEVVECLEKqNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQ 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 801400033 412 SLLQKEWVAGGHPFCDRLGHIVKTNSEKSPLFLLYLDCVWQL 453
Cdd:cd14594  162 SLIQKEWVMGGHCFLDRCNHLRQNDKEEVPVFLLFLDCVWQL 203
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
217-476 2.57e-47

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: 168.67  E-value: 2.57e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 217 WRLSMVNAKFQLCPSLSQYVVVPASVTDSQLTDAARHFQGNRPPVWSW--TSSHgAALVKMSELLPTITERMQEN-IMFE 293
Cdd:cd14532   15 WTLSDINKDYELCDTYPRELFVPTSASTPVLVGSSKFRSKGRLPVLSYlhKDNQ-AAICRCSQPLSGFSARCVEDeQLLQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 294 NVRKSHPQKIPPVVIELNKEINVKLIAASFTKFINLCTPENIR-QFW-IQD----------------------NNFYSLL 349
Cdd:cd14532   94 AIRKANPNSKFMYVVDTRPKINAMANKAAGKGYENEDNYSNIKfQFFgIENihvmrsslqkllevcelknpsmSAFLSGL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 350 ENTKWLKYISYCLQKTVEVCDHLNLGISVILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFCDRL 429
Cdd:cd14532  174 ESSGWLKHIKAVMDTSVFIAKAVSEGASVLVHCSDGWDRTAQTCSLASLLLDPYYRTIKGFQVLIEKEWLSFGHKFTDRC 253
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 801400033 430 GHIVKTNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWDAAH 476
Cdd:cd14532  254 GHLQGDAKEVSPVFTQFLDCVWQLMQQFPRAFEFNERFLLTLHDHVY 300
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
258-453 1.35e-45

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: 160.38  E-value: 1.35e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 258 RPPVWSWTSSHGAALVKMSELLPTITE-----RMQENIMFENvrksHPQkipPVVIELNKEI-NVKLIAASFTKFINLCT 331
Cdd:cd14595    2 RIPRWCWHHPGGSDLLRMAGFYTNSDPekediRSVELLLQAG----HSQ---CVIVDTSEELpSPADIQLAYLKLRTLCL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 332 PENIrqFWIQDNNFYSLLENTKWLKYISYCLQKTVEVCDHLNLG-ISVILQEGAARDLCCVISSLAQLLLDHHFRTIVGF 410
Cdd:cd14595   75 PDIS--VSVSDEKWLSNLEGTRWLDHVRACLRKASEVSCLLAERhRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGF 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 801400033 411 QSLLQKEWVAGGHPFCDRLGHIVKTNSEKSPLFLLYLDCVWQL 453
Cdd:cd14595  153 QSLVQKEWVVAGHPFLQRLNLTRESDKEESPVFLLFLDCVWQL 195
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
217-456 8.66e-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: 141.35  E-value: 8.66e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 217 WRLSMVNAKFQLCPSLSQYVVVPASVTDSQLTDAARHFQGNRPPVWSWTSS------------HGAALVKMSELLPTITE 284
Cdd:cd14534    1 FRISTANRDYSICRSYPALVVVPQSVSDESLRKVARCYRQGRFPVVTWRHPrtkalllrsggfHGKGVMGMLKSANTSTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 285 RM------------QENIMFENV-----RKSHPQKI--------PPVVIELNKEINVKliaASFTKFINLCTPENIrqFW 339
Cdd:cd14534   81 SPtvsssetsssleQEKYLSALVlyvlgEKSQMKGVkaesdpkcEFIPVEYPEVRQVK---ASFKKLLRACVPSSA--PT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 340 IQDNNFYSLLENTKWLKYISYCLQKTVEVCDHLNL-GISVILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQSLLQKEW 418
Cdd:cd14534  156 EPEQSFLKAVEDSEWLQQLQCLMQLSGAVVDLLDVqGSSVLLCLEDGWDVTTQVSSLSQLLLDPYYRTLEGFRVLVEKEW 235
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 801400033 419 VAGGHPFCDRLGHIVKT-NSEKSPLFLLYLDCVWQLCQQ 456
Cdd:cd14534  236 LAFGHRFSHRSNLTAASqSSGFAPVFLQFLDAVHQIHRQ 274
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
257-452 2.96e-37

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: 138.45  E-value: 2.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 257 NRPPVWSWTSS-HGAALVKMSELLPTITER---MQENImFENVRKSHPQKIPPVVIEL---------------------- 310
Cdd:cd14507    1 GRIPVLSWRHPrNGAVICRSSQPLVGLTGSrskEDEKL-LNAIRKASPSSKKLYIVDArpklnavanrakgggyenteyy 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 311 -NKEI------NVKLIAASFTKFINLCTPENIrqfwiQDNNFYSLLENTKWLKYISYCLQKTVEVCDHL-NLGISVILQE 382
Cdd:cd14507   80 pNCELeflnieNIHAMRDSLNKLRDACLSPND-----EESNWLSALESSGWLEHIRLILKGAVRVADLLeKEGTSVLVHC 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 801400033 383 GAARDLCCVISSLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFCDRLGHIVKTNSEK--SPLFLLYLDCVWQ 452
Cdd:cd14507  155 SDGWDRTSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDKNSSDEerSPIFLQFLDCVWQ 226
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
315-473 2.52e-34

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: 130.92  E-value: 2.52e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 315 NVKLIAASFTKFINLCTPEnirqfwIQDNNFYSLLENTKWLKYISYCLQKTVEVCDHLNLG-ISVILQEGAARDLCCVIS 393
Cdd:cd14591   91 NIHVMRESLKKLKDIVYPN------VEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGkSSVLVHCSDGWDRTAQLT 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 394 SLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFCDRLGHIVK--TNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYLTTL 471
Cdd:cd14591  165 SLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGHGDKnhADADRSPIFLQFIDCVWQMSKQFPTAFEFNEQFLITI 244

                 ..
gi 801400033 472 WD 473
Cdd:cd14591  245 LD 246
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
244-473 3.30e-33

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: 128.23  E-value: 3.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 244 DSQLTDAARHFQGNRPPVWSWTSSHG-AALVKMSELLPTIT-------ERMQENIMFENVrKSHPQKI----PPVVIELN 311
Cdd:cd14590    1 DEELKRVASFRSRGRIPVLSWIHPESqATITRCSQPMVGVSgkrskedEKYLQAIMDSNA-QSHKIFIfdarPSVNAVAN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 312 K---------------EI------NVKLIAASFTKFINLCTPEnirqfwIQDNNFYSLLENTKWLKYISYCLQKTVEVCD 370
Cdd:cd14590   80 KakgggyesedayqnaELvfldihNIHVMRESLRKLKEIVYPN------IEESHWLSNLESTHWLEHIKLILAGALRIAD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 371 HLNLG-ISVILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFCDRLGHIVK--TNSEKSPLFLLYL 447
Cdd:cd14590  154 KVESGkTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKnhADADRSPVFLQFI 233
                        250       260
                 ....*....|....*....|....*.
gi 801400033 448 DCVWQLCQQYPTEFEFTETYLTTLWD 473
Cdd:cd14590  234 DCVWQMTRQFPTAFEFNEYFLITILD 259
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
315-473 1.51e-32

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: 126.02  E-value: 1.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 315 NVKLIAASFTKFINLCTPEnirqfwIQDNNFYSLLENTKWLKYISYCLQKTVEVCDHLNLG-ISVILQEGAARDLCCVIS 393
Cdd:cd14535   91 NIHVMRESLRKLKDICFPN------IDDSHWLSNLESTHWLEHIKLILAGAVRIADKVESGkTSVVVHCSDGWDRTAQLT 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 394 SLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFCDRLGHIVK--TNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYLTTL 471
Cdd:cd14535  165 SLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGHGDKnhSDADRSPVFLQFIDCVWQMTRQFPNAFEFNEHFLITI 244

                 ..
gi 801400033 472 WD 473
Cdd:cd14535  245 LD 246
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
217-476 3.58e-31

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


Pssm-ID: 350433  Cd Length: 302  Bit Score: 123.50  E-value: 3.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 217 WRLSMVNAKFQLCPSLSQYVVVPASVTDSQLTDAARHFQGNRPPVWSW-TSSHGAALVKMSELLPTITER-MQENIMFEN 294
Cdd:cd14585   15 WQLSDVNRDYKICDTYPRDLYVPITASKPIIVGSSKFRSKGRFPVLSYyHQEKKAAICRCSQPLSGFSARcLEDEHMLQA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 295 VRKSHPQKIPPVVIELNKEINVKLIAASFTKFINLCTPENIR-QF-----------------------WIQDNNFYSLLE 350
Cdd:cd14585   95 ISKANPNNRYMYVMDTRPKLNAMANRAAGKGYENEDNYSNIRfQFvgienihvmrsslqkllevcgtkALSVNDFLSGLE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 351 NTKWLKYISYCLQKTVEVCDHLNL-GISVILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFCDRL 429
Cdd:cd14585  175 SSGWLRHIKAVLDAAVFLAKAVAVeGASVLVHCSDGWDRTAQVCSLGSLLLDPYYRTIKGFMVLIEKDWISFGHKFSDRC 254
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 801400033 430 GHIVKTNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWDAAH 476
Cdd:cd14585  255 GQLDGDPKEISPVFTQFLECVWQLTEQFPRAFEFSEAFLLQIHEHIH 301
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
315-473 5.13e-31

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: 121.62  E-value: 5.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 315 NVKLIAASFTKFINLCTPEnirqfwIQDNNFYSLLENTKWLKYISYCLQKTVEVCDHLNLG-ISVILQEGAARDLCCVIS 393
Cdd:cd14592   91 NIHVMRESLRKLKEIVYPS------IDEARWLSNVDGTHWLEYIRMLLAGAVRIADKIESGkTSVVVHCSDGWDRTAQLT 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 394 SLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFCDRLGH--IVKTNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYLTTL 471
Cdd:cd14592  165 SLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGHgdDNHADADRSPIFLQFIDCVWQMTRQFPSAFEFNELFLITI 244

                 ..
gi 801400033 472 WD 473
Cdd:cd14592  245 LD 246
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
217-473 5.39e-31

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


Pssm-ID: 350432  Cd Length: 308  Bit Score: 123.06  E-value: 5.39e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 217 WRLSMVNAKFQLCPSLSQYVVVPASVTDSQLTDAARHFQGNRPPVWSWT-SSHGAALVKMSELLPTITERMQEN-IMFEN 294
Cdd:cd14584   21 WEITDANKNYEICSTYPPELVVPKSASKATVVGSSKFRSRGRFPVLSYLyKENNAAICRCSQPLSGFSARCVEDeQMLQA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 295 VRKSHPQKIPPVVIELNKEINVKLIAASFTKFINLCTPENIR-QFWIQDN-----------------------NFYSLLE 350
Cdd:cd14584  101 ISKANPGSPFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIRfQFIGIENihvmrsslqkllevcemkspsmsDFLTGLE 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 351 NTKWLKYISYCLQKTV----EVCDHlnlGISVILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFC 426
Cdd:cd14584  181 NSGWLRHIKAVMDAGVflakAVKEE---KASVLVHCSDGWDRTAQVCSLASLLLDPFYRTIKGLMVLIEKEWISMGHKFS 257
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 801400033 427 DRLGHIVKTNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWD 473
Cdd:cd14584  258 QRCGHLDGDPKEVSPVFTQFLECVWQLMEQFPCAFEFNEHFLLEIHD 304
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
217-468 2.11e-29

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: 118.52  E-value: 2.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 217 WRLSMVNAKFQLCPSLSQYVVVPASVTDSQLTDAARHFQGNRPPVWSW-TSSHGAALVKMSELLPTITER-MQENIMFEN 294
Cdd:cd14583   15 WQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYyCKDNNASICRSSQPLSGFSARcLEDEQMLQA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 295 VRKSHPQKIPPVVIELNKEINVKLIAASFTKFINLCTPENIRQFWIQDNNFYSL------------------------LE 350
Cdd:cd14583   95 IRKANPGSDFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMrnslqkmlevcelrspsmgdflwgLE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 351 NTKWLKYISYCLQKTVEVCDHL-NLGISVILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFCDRL 429
Cdd:cd14583  175 NSGWLKHIKAIMDAGIFIAKAVaEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKFNHRY 254
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 801400033 430 GHIVKTNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYL 468
Cdd:cd14583  255 GHLDGDPKEVSPVIDQFIECVWQLMEQFPCAFEFNERFL 293
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
300-452 6.74e-25

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: 103.25  E-value: 6.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 300 PQKIPPVVIELNKEINVKLIAASFTKFINLCTPENirqfwiQDNNFYSLLENTKWLKYISYCLQKTVEVCDHLNL-GISV 378
Cdd:cd14533   80 PEYYPNCEVVFMNLANIHAIRKSFHSLRALCSSAP------DQPNWLSNLESTKWLHHLSGLLKAALLVVNAVDEeGRPV 153
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 801400033 379 ILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFCDRLGHIVKTN--SEKSPLFLLYLDCVWQ 452
Cdd:cd14533  154 LVHCSDGWDRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFGHKFADRCGHGVNSEdiNERCPVFLQWLDCVHQ 229
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
217-456 7.87e-25

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: 105.05  E-value: 7.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 217 WRLSMVNAKFQLCPSLSQYVVVPASVTDSQLTDAARHFQGNRPPVWSWTSS------------HGAALVKM--------- 275
Cdd:cd14588    1 FRISTVNRMYAVCRSYPGLLIVPQSIQDNTIQRISRCYRQNRFPVVCWRNSrtkavllrsgglHGKGVVGLfksqnapaa 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 276 -------SEL------------LPTITERMQENIM---------------FENVRKSHPQKIPPVVIELnkeINVKLIAA 321
Cdd:cd14588   81 gqsqtdsTSLeqekylqavinsMPRYADASGRNTLsgfraalyiigdksqLKGVKQDPLQQWEVVPIEV---FDVRQVKA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 322 SFTKFINLCTPENIRQfwIQDNNFYSLLENTKWLKYISYCLQKTVEVCDHLNLGISVILQEGAARDLCCVISSLAQLLLD 401
Cdd:cd14588  158 SFKKLMKACVPSCPST--DPSQTYLRTLEESEWLSQLHKLLQVSVLVVELLDSGSSVLVSLEDGWDITTQVVSLVQLLSD 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 801400033 402 HHFRTIVGFQSLLQKEWVAGGHPFCDRLGHIVKTNSEK-SPLFLLYLDCVWQLCQQ 456
Cdd:cd14588  236 PYYRTIEGFRLLVEKEWLSFGHRFSHRGAQTLASQSSGfTPVFLQFLDCVHQIHLQ 291
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
212-452 3.16e-24

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: 103.95  E-value: 3.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 212 ETKKGWRLSMVNAKFQLCPSLSQYVVVPASVTDSQLTDAA-------------RHfQGN--------RPPV--WSWTSSH 268
Cdd:cd14586    3 DMQNAWRISNINEKYKLCGSYPQELIVPAWITDKELESVAsfrswkripavvyRH-QSNgaviarcgQPEVswWGWRNAD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 269 GAALVK-MSELLPTITERMQENIMFENVRKSHPQ----------------------KIPPVVIEL--------------- 310
Cdd:cd14586   82 DEHLVQsVAKACASDSSSCKSVLMTGNCSRDFPNggdlsdvefdssmsnasgveslAIQPQKLLIldarsyaaavanrak 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 311 -----------NKEI------NVKLIAASFTKFINLCT--PEnirqfwiqDNNFYSLLENTKWLKYISYCLQKTVEVCDH 371
Cdd:cd14586  162 gggcecpeyypNCEVvfmgmaNIHSIRKSFQSLRLLCTqmPD--------PANWLSALESTKWLQHLSMLLKSALLVVHA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 372 LNLGIS-VILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFCDRLGHIVKTN--SEKSPLFLLYLD 448
Cdd:cd14586  234 VDRDQRpVLVHCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRCGHGENSDdlNERCPVFLQWLD 313

                 ....
gi 801400033 449 CVWQ 452
Cdd:cd14586  314 CVHQ 317
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
310-452 1.84e-23

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: 98.95  E-value: 1.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 310 LNKEI-NVKLIAASFTKFINLCTPENIR-QFWIqdnnfySLLENTKWLKYISYCLQK--TVEVCDHlNLGISVILQEGAA 385
Cdd:cd14536   82 IHKPIeRYNVLQESLIKLVEACNDQGHSmDKWL------SKLESSNWLSHVKEILTTacLVAQCID-REGASVLVHGSEG 154
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 386 RDLCCVISSLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFCDRLGHIVKTNS---EKSPLFLLYLDCVWQ 452
Cdd:cd14536  155 MDSTLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRCAKSAYSNSkqkFESPVFLLFLDCVWQ 224
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
217-456 2.86e-23

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


Pssm-ID: 350437  Cd Length: 297  Bit Score: 100.38  E-value: 2.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 217 WRLSMVNAKFQLCPSLSQYVVVPASVTDSQLTDAARHFQGNRPPVWSWTSS------------HGAALVKM------SEL 278
Cdd:cd14589    1 FRITAVNRMYSLCRSYPGLLVVPQSVQDSSLQKVARCYRHNRLPVVCWKNSktkavllrsggfHGKGVVGLfksqnpHSA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 279 LPTITERM----QE-------------------NIMFENV------------RKSHPQ--KIPPVvieLNKEI------N 315
Cdd:cd14589   81 APASSESSssieQEkylqallnaisvhqkmngnSTLLQSQllkrqaalyifgEKSQLRgfKLDFA---LNCEFvpvefhD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 316 VKLIAASFTKFINLCTPENIRQfwIQDNNFYSLLENTKWLKYISYCLQKTVEVCDHLNLGISVI--LQEGAarDLCCVIS 393
Cdd:cd14589  158 IRQVKASFKKLMRACVPSTIPT--DSEVTFLKALGESEWFLQLHRIMQLAVVISELLESGSSVMvcLEDGW--DITTQVV 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 801400033 394 SLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFCDRLGhiVKTNSEKS---PLFLLYLDCVWQLCQQ 456
Cdd:cd14589  234 SLVQLLSDPFYRTLEGFQMLVEKEWLSFGHKFSQRSN--LTPNSQGSgfaPIFLQFLDCVHQIHNQ 297
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
217-452 3.00e-22

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: 97.80  E-value: 3.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 217 WRLSMVNAKFQLCPSLSQYVVVPASVTDSQLTDAARHFQGNRPPV----------------------WSWTSSHGAALV- 273
Cdd:cd14587    3 WRVSEINSNYKLCSSYPQKLLVPVWITDKELENVASFRSWKRIPVvvyrhlrngaviarcsqpeiswWGWRNADDEYLVt 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 274 ---KMSELLPTIteRMQENIMFENVRKSH----------------------PQKI------------------------- 303
Cdd:cd14587   83 siaKACALDPGT--RAPGGSPSKGNSDGSdasdtdfdssltacsavesgaaPQKLlildarsytaavanrakgggcecee 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 304 --PPVVIELNKEINVKLIAASFTKFINLCTPenirqfwIQD-NNFYSLLENTKWLKYISYCLQKTVEVCDHLNL-GISVI 379
Cdd:cd14587  161 yyPNCEVMFMGMANIHSIRNSFQYLRAVCSQ-------MPDpGNWLSALESTKWLQHLSVMLKAAVLVASAVDReGRPVL 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 801400033 380 LQEGAARDLCCVISSLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFCDRLGH--IVKTNSEKSPLFLLYLDCVWQ 452
Cdd:cd14587  234 VHCSDGWDRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHqeNVEDQNEQCPVFLQWLDCVHQ 308
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
348-452 5.20e-20

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: 89.43  E-value: 5.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033 348 LLENTKWLKYISYCLQKTVEVCDHLNLGIS-VILQEGAARDLCCVISSLAQLLLDHHFRTIVGFQSLLQKEWVAGGHPFC 426
Cdd:cd17666  129 ALKKSNWLKYLAIILQGADLIAKSIHFNHShVLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFA 208
                         90       100
                 ....*....|....*....|....*.
gi 801400033 427 DRLGHivktnSEKSPLFLLYLDCVWQ 452
Cdd:cd17666  209 ERSGH-----KETSPVFHQFLDCVYQ 229
PH-GRAM_MTMR12 cd13348
Myotubularian (MTM) related 12 protein (MTMR12) Pleckstrin Homology-Glucosyltransferases, ...
33-182 2.13e-18

Myotubularian (MTM) related 12 protein (MTMR12) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR12 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Glu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR12 contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, a SET interaction domain, and a C-terminal a coiled-coil domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date.


Pssm-ID: 275418  Cd Length: 178  Bit Score: 83.36  E-value: 2.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  33 ENSIKLLPGEVLIAEAQSVLMFLPVSDLKQGISGVLSVTNFKLTFVTSGDSNGENVTRQQNHLYGYTDTCLTNIDEIYiM 112
Cdd:cd13348   15 EVNPHLLPGEVVLCEANTVLKYTQDDGSQRGVYGRLVCTNFRIAFLGDDAPQDDNSKQFKNKIYGENDITLQCVDQIY-G 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 801400033 113 IGDKKRKLVPGNTVPSKVKGIFII-CKNLRTWSFSFKFSPVGHGKNLLTALLHHAF-PSRHQLLFAYDYKEA 182
Cdd:cd13348   94 VYDEKKKLITGGLVKNKYPEKLIIhCKDLRVFQFCLRYTKEEEVKRIVSGIIHHTQePKLLKRLFLFSYARA 165
PH-GRAM_MTMR10-like cd13212
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
39-150 7.50e-15

Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR10, MTMR11, and MTMR12 are catalytically inactive phosphatases that play a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. They contains a Glu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. They contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, a SET interaction domain, and a C-terminal coiled-coil domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275399  Cd Length: 125  Bit Score: 71.49  E-value: 7.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  39 LPGEVLIAEAQSVLMFLPVSDLKQGISGVLSVTNFKLTFVTSGDSNGENvTRQQNHLYGYTDTCLTNIDEIYIMIGDK-K 117
Cdd:cd13212    1 LPGEQVLAEAPGVRKGLQEDSSQPELSGTLICTNFKITFQPDDWQWLDN-TQQKNPLNGEYDFALVCIGQIEAVSDLKrV 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 801400033 118 RKLVPGNTVPSKVKGIFIICKNLRTWSFSFKFS 150
Cdd:cd13212   80 QLLRPGSLLKFIPEELIIHCKDFRVLRFGFEAT 112
PH-GRAM_MTMR10 cd13346
Myotubularian (MTM) related 10 protein (MTMR10) Pleckstrin Homology-Glucosyltransferases, ...
37-189 2.03e-13

Myotubularian (MTM) related 10 protein (MTMR10) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR10 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Glu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR10 contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, and a SET interaction domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date.


Pssm-ID: 270154  Cd Length: 177  Bit Score: 68.80  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  37 KLLPGEVLIAEAQSVLMFLPVSDLKQGISGVLSVTNFKLTFVTSgDSNGENVTRQQNHLYGYTDTCLTNIDEIyIMIGDK 116
Cdd:cd13346   17 VLLPGEIVVNEVNFVRKCIATDTSQYDLWGKLICTNFKISFITD-DPMPLQKFHYKNLLLGEHDVPLTCIEQI-VTVNDT 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 801400033 117 KRK---LVPGNTVPSKVKGIFIICKNLRTWSFSFKFSPVGHGKNLLTALLHHAFPSRHQLLFAYDY-KEAYYSSLDK 189
Cdd:cd13346   95 KRKqkvLGPNQKLKFNPTELIIYCKDFRIVRFRFDEAGPESAKKVCLAIAHYSQPTDLQLLFAFEYvGKKYHNSAGK 171
PH-GRAM_MTMR11 cd15790
Myotubularian (MTM) related 11 protein (MTMR11) Pleckstrin Homology-Glucosyltransferases, ...
39-147 1.13e-08

Myotubularian (MTM) related 11 protein (MTMR11) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR10, MTMR11, and MTMR12 are catalytically inactive phosphatases that play a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. They contains a Glu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. They contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, a SET interaction domain, and a C-terminal coiled-coil domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275433  Cd Length: 123  Bit Score: 53.63  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801400033  39 LPGEVLIAEAQSVLMFLPVSDLKQGISGVLSVTNFKLTFVTSGDSNGENvtRQQNHLYGYTDTCLTNIDEIYIMIGDKKR 118
Cdd:cd15790    1 LPGEHILEEAVRVRKLVQWRDGEGFLSGTLYCTNFRVAFVPEHIQKDEN--DHDTVLNSEHDIALPSIDRVVAVQGPTTM 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 801400033 119 KLV-PGNTVPSKVKGIFIICKNLRTWSFSF 147
Cdd:cd15790   79 KAVtASSGLKFIPEELVIYCRDFRLLRFQF 108
3-PAP pfam12578
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
538-591 5.59e-08

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


Pssm-ID: 403693  Cd Length: 128  Bit Score: 51.63  E-value: 5.59e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 801400033  538 TENETIIKPLYAVSSLELWTQCYFRWIPTLEIRNGGQ----RHIELY---IRLLQNDINQH 591
Cdd:pfam12578  62 ADLHGLLLPQLSGPHIKLWKQCYLRWVPEAQINHGGPitafHKLSLLadeVDALQRLLRQY 122
 
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