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Conserved domains on  [gi|749750396|ref|XP_011137454|]
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myotubularin-related protein 10-B isoform X1 [Harpegnathos saltator]

Protein Classification

PH domain-containing protein; PH domain-containing RhoGEF family protein( domain architecture ID 13117763)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner; similar to the PH region of pleckstrin homology domain-containing family A member 2 (PLEKHA2/TAAP2) that binds specifically to phosphatidylinositol 3,4-diphosphate (PtdIns3,4P2)| PH domain-containing RhoGEF family protein may function as a guanine nucleotide exchange factor; similar to Homo sapiens pleckstrin homology domain-containing family G member 4B and Danio rerio quattro

Graphical summary

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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 9.66e-113

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: 336.62  E-value: 9.66e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 257 NRPLVWSWTSVYGAALVKMSELLPTITERRHENIMFENIRKSHPQKMQPVVIELNKEI-NVKLIAVGFSKFISLCSAENI 335
Cdd:cd14537    1 GRPPVWCWSHPNGAALVRMAELLPTITDRTQENKMLEAIRKSHPNLKKPKVIDLDKLLpSLQDVQAAYLKLRELCTPDSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 336 RQFWVQDNNFYSLLENTKWLKYISYCLQKAADVCDRL-NLGYSVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLL 414
Cdd:cd14537   81 EQFWVQDSKWYSLLENTKWLHYVSACLKKASEAAEALeSRGRSVVLQESDGRDLSCVVSSLVQLLLDPHFRTITGFQSLI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 749750396 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 7.57e-20

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: 473070  Cd Length: 178  Bit Score: 87.60  E-value: 7.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  33 ENSIKLLPGEVLIAEAQSVLMFSPVSDLKQGISGVLSVTNFKLTFItSDDSNGEDVTHQ-QNHLYGYTDTCLTNIDEIYi 111
Cdd:cd13348   15 EVNPHLLPGEVVLCEANTVLKYTQDDGSQRGVYGRLVCTNFRIAFL-GDDAPQDDNSKQfKNKIYGENDITLQCVDQIY- 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749750396 112 MVGDKKRKLVPGNTVPSKVKGIFII-CKNLRTWSFSFKFSPLGHGKNLLTALLHHAF-PSRHQLLFAYDYKEA 182
Cdd:cd13348   93 GVYDEKKKLITGGLVKNKYPEKLIIhCKDLRVFQFCLRYTKEEEVKRIVSGIIHHTQePKLLKRLFLFSYARA 165
3-PAP super family cl13953
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
 540-571 2.30e-05

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: 463634  Cd Length: 132  Bit Score: 44.28  E-value: 2.30e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 749750396  540 VIKPSCAISNLELWTQCYFRWIPALEIHNGGQ 571
Cdd:pfam12578  71 LLLPLLSGPHIKLWKLCYLRWVPEAQINHGGP 102
 
Name Accession Description Interval E-value
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 257-452 9.66e-113

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: 336.62  E-value: 9.66e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 257 NRPLVWSWTSVYGAALVKMSELLPTITERRHENIMFENIRKSHPQKMQPVVIELNKEI-NVKLIAVGFSKFISLCSAENI 335
Cdd:cd14537    1 GRPPVWCWSHPNGAALVRMAELLPTITDRTQENKMLEAIRKSHPNLKKPKVIDLDKLLpSLQDVQAAYLKLRELCTPDSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 336 RQFWVQDNNFYSLLENTKWLKYISYCLQKAADVCDRL-NLGYSVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLL 414
Cdd:cd14537   81 EQFWVQDSKWYSLLENTKWLHYVSACLKKASEAAEALeSRGRSVVLQESDGRDLSCVVSSLVQLLLDPHFRTITGFQSLI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 749750396 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 5.07e-66

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: 220.04  E-value: 5.07e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  196 DISDWQNELRRTLSNdqIRKAWRLSTVNAKFQLCPSLSQYVIVPASVTDRQLTDAAKHFQGNRPLVWSW-TSVYGAALVK 274
Cdd:pfam06602   6 DLYDPEAEFARQGLP--SKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYrHKENGAVITR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  275 MSELLPTITERRheNI----MFENIRKS-HPQKMQPVVI---------ELNK------EI-----NVKLIAVG------- 322
Cdd:pfam06602  84 SSQPLVGLNGKR--SIedekLLQAIFKSsNPYSAKKLYIvdarpklnaMANRakgggyENednypNCKKIFLGienihvm 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  323 ---FSKFISLCSAENIrqfwvQDNNFYSLLENTKWLKYISYCLQKAADVCDRLNL-GYSVILQEGAGRDLCCVISSLVQL 398
Cdd:pfam06602 162 rdsLNKLVEACNDRSP-----SMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLeGSSVLVHCSDGWDRTAQLTSLAQL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  399 LLDPHFRTITGFQSLLQKEWVAGGHPFCDRLGHIVKTNSEK--SPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWDTAH 476
Cdd:pfam06602 237 LLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGFTDSKerSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLY 316

                         330
                  ....*....|....*
gi 749750396  477 VSIFDTFIFNCERDR 491
Cdd:pfam06602 317 SCQFGTFLCNSEKER 331
PH-GRAM_MTMR12 cd13348
Myotubularian (MTM) related 12 protein (MTMR12) Pleckstrin Homology-Glucosyltransferases, ...
 33-182 7.57e-20

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: 87.60  E-value: 7.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  33 ENSIKLLPGEVLIAEAQSVLMFSPVSDLKQGISGVLSVTNFKLTFItSDDSNGEDVTHQ-QNHLYGYTDTCLTNIDEIYi 111
Cdd:cd13348   15 EVNPHLLPGEVVLCEANTVLKYTQDDGSQRGVYGRLVCTNFRIAFL-GDDAPQDDNSKQfKNKIYGENDITLQCVDQIY- 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749750396 112 MVGDKKRKLVPGNTVPSKVKGIFII-CKNLRTWSFSFKFSPLGHGKNLLTALLHHAF-PSRHQLLFAYDYKEA 182
Cdd:cd13348   93 GVYDEKKKLITGGLVKNKYPEKLIIhCKDLRVFQFCLRYTKEEEVKRIVSGIIHHTQePKLLKRLFLFSYARA 165
3-PAP pfam12578
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
 540-571 2.30e-05

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: 463634  Cd Length: 132  Bit Score: 44.28  E-value: 2.30e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 749750396  540 VIKPSCAISNLELWTQCYFRWIPALEIHNGGQ 571
Cdd:pfam12578  71 LLLPLLSGPHIKLWKLCYLRWVPEAQINHGGP 102
 
Name Accession Description Interval E-value
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 257-452 9.66e-113

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: 336.62  E-value: 9.66e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 257 NRPLVWSWTSVYGAALVKMSELLPTITERRHENIMFENIRKSHPQKMQPVVIELNKEI-NVKLIAVGFSKFISLCSAENI 335
Cdd:cd14537    1 GRPPVWCWSHPNGAALVRMAELLPTITDRTQENKMLEAIRKSHPNLKKPKVIDLDKLLpSLQDVQAAYLKLRELCTPDSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 336 RQFWVQDNNFYSLLENTKWLKYISYCLQKAADVCDRL-NLGYSVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLL 414
Cdd:cd14537   81 EQFWVQDSKWYSLLENTKWLHYVSACLKKASEAAEALeSRGRSVVLQESDGRDLSCVVSSLVQLLLDPHFRTITGFQSLI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 749750396 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 5.07e-66

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: 220.04  E-value: 5.07e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  196 DISDWQNELRRTLSNdqIRKAWRLSTVNAKFQLCPSLSQYVIVPASVTDRQLTDAAKHFQGNRPLVWSW-TSVYGAALVK 274
Cdd:pfam06602   6 DLYDPEAEFARQGLP--SKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYrHKENGAVITR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  275 MSELLPTITERRheNI----MFENIRKS-HPQKMQPVVI---------ELNK------EI-----NVKLIAVG------- 322
Cdd:pfam06602  84 SSQPLVGLNGKR--SIedekLLQAIFKSsNPYSAKKLYIvdarpklnaMANRakgggyENednypNCKKIFLGienihvm 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  323 ---FSKFISLCSAENIrqfwvQDNNFYSLLENTKWLKYISYCLQKAADVCDRLNL-GYSVILQEGAGRDLCCVISSLVQL 398
Cdd:pfam06602 162 rdsLNKLVEACNDRSP-----SMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLeGSSVLVHCSDGWDRTAQLTSLAQL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  399 LLDPHFRTITGFQSLLQKEWVAGGHPFCDRLGHIVKTNSEK--SPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWDTAH 476
Cdd:pfam06602 237 LLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGFTDSKerSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLY 316

                         330
                  ....*....|....*
gi 749750396  477 VSIFDTFIFNCERDR 491
Cdd:pfam06602 317 SCQFGTFLCNSEKER 331
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 261-452 1.39e-54

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: 184.71  E-value: 1.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 261 VWSWTSVYGAALVKMSELLPTITERRHENIMFENIRKSHPQKMQPVVIELNKEI-NVKLIAVGFSKFISLCSAEnirQFW 339
Cdd:cd14593    5 LWCWNHPNGSALVRMANIKDLLQQRKIDQRICNAITRSHPLRSDVYKSDLDKTLpNIQEIQAAFVKLKQLCVNE---PFE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 340 VQDNNFYSLLENTKWLKYISYCLQKAADVCDRLNLGY-SVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLLQKEW 418
Cdd:cd14593   82 ETEEKWLSSLESTRWLEYVRAFLKHSAELVYMLESKHvSVILQEEEGRDLSCVVASLVQVMLDPYFRTITGFQSLIQKEW 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 749750396 419 VAGGHPFCDRLGHIVKTNSEKSPLFLLYLDCVWQ 452
Cdd:cd14593  162 VMAGYRFLDRCNHLKKSSKKESPLFLLFLDCVWQ 195
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 261-453 3.77e-49

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: 170.41  E-value: 3.77e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 261 VWSWTSVYGAALVKMSELLPTITE------RRHENIMFENIRKSHPQKMQPVviELNKEI-NVKLIAVGFSKFISLCSAE 333
Cdd:cd14594    5 IWCWSCHNGCALLKMSALPKEQDDvalqdqKSFLDRIYKTLSRPPYESVKTE--DLSASLpSLQEIQTAYNRFKQLFLID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 334 NIRQFWVQDNNFYSLLENTKWLKYISYCLQKAADVCDRLNL-GYSVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQS 412
Cdd:cd14594   83 NSTDFWDTDVKWFSSLESSNWLEIIRQCLKKAVEVVECLEKqNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQS 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 749750396 413 LLQKEWVAGGHPFCDRLGHIVKTNSEKSPLFLLYLDCVWQL 453
Cdd:cd14594  163 LIQKEWVMGGHCFLDRCNHLRQNDKEEVPVFLLFLDCVWQL 203
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 262-453 8.01e-47

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: 163.85  E-value: 8.01e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 262 WSWTSVYGAALVKMSELLPTITE-----RRHENIMFENirkshpqKMQPVVIELNKEI-NVKLIAVGFSKFISLCSAENI 335
Cdd:cd14595    6 WCWHHPGGSDLLRMAGFYTNSDPekediRSVELLLQAG-------HSQCVIVDTSEELpSPADIQLAYLKLRTLCLPDIS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 336 rqFWVQDNNFYSLLENTKWLKYISYCLQKAADVCDRLNLGY-SVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLL 414
Cdd:cd14595   79 --VSVSDEKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHrSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLV 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 749750396 415 QKEWVAGGHPFCDRLGHIVKTNSEKSPLFLLYLDCVWQL 453
Cdd:cd14595  157 QKEWVVAGHPFLQRLNLTRESDKEESPVFLLFLDCVWQL 195
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 200-476 5.15e-46

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: 165.21  E-value: 5.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 200 WQNELRRT-LSNDQirkaWRLSTVNAKFQLCPSLSQYVIVPASVTDRQLTDAAKHFQGNRPLVWSWTSVYG-AALVKMSE 277
Cdd:cd14532    1 LESEYTRMgVPNDN----WTLSDINKDYELCDTYPRELFVPTSASTPVLVGSSKFRSKGRLPVLSYLHKDNqAAICRCSQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 278 LLPTITERRHEN-IMFENIRKSHPQKMQPVVIELNKEIN-------------------VKLIAVG----------FSKFI 327
Cdd:cd14532   77 PLSGFSARCVEDeQLLQAIRKANPNSKFMYVVDTRPKINamankaagkgyenednysnIKFQFFGienihvmrssLQKLL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 328 SLCSAENIRQfwvqdNNFYSLLENTKWLKYISYCLQKAADVCDRLNLGYSVILQEGAGRDLCCVISSLVQLLLDPHFRTI 407
Cdd:cd14532  157 EVCELKNPSM-----SAFLSGLESSGWLKHIKAVMDTSVFIAKAVSEGASVLVHCSDGWDRTAQTCSLASLLLDPYYRTI 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749750396 408 TGFQSLLQKEWVAGGHPFCDRLGHIVKTNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWDTAH 476
Cdd:cd14532  232 KGFQVLIEKEWLSFGHKFTDRCGHLQGDAKEVSPVFTQFLDCVWQLMQQFPRAFEFNERFLLTLHDHVY 300
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
 326-452 4.22e-38

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: 140.76  E-value: 4.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 326 FISLCSAenIRQFWVQDNNFYSLLENTKWLKYISYCLQKAADVCDRL-NLGYSVILQEGAGRDLCCVISSLVQLLLDPHF 404
Cdd:cd14507   99 LNKLRDA--CLSPNDEESNWLSALESSGWLEHIRLILKGAVRVADLLeKEGTSVLVHCSDGWDRTSQLTSLAQLLLDPYY 176

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 749750396 405 RTITGFQSLLQKEWVAGGHPFCDRLGHIVKTNSEK--SPLFLLYLDCVWQ 452
Cdd:cd14507  177 RTIEGFQVLIEKEWLSFGHKFADRCGHGDKNSSDEerSPIFLQFLDCVWQ 226
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
 340-473 1.93e-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: 131.30  E-value: 1.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 340 VQDNNFYSLLENTKWLKYISYCLQKAADVCDRLNLG-YSVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLLQKEW 418
Cdd:cd14591  110 VEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGkSSVLVHCSDGWDRTAQLTSLAMLMLDSYYRTIEGFEVLVQKEW 189

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749750396 419 VAGGHPFCDRLGHIVK--TNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWD 473
Cdd:cd14591  190 ISFGHKFASRIGHGDKnhADADRSPIFLQFIDCVWQMSKQFPTAFEFNEQFLITILD 246
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 217-456 6.74e-34

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: 130.56  E-value: 6.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 217 WRLSTVNAKFQLCPSLSQYVIVPASVTDRQLTDAAKHFQGNRPLVWSW-----------------TSVYG---------- 269
Cdd:cd14534    1 FRISTANRDYSICRSYPALVVVPQSVSDESLRKVARCYRQGRFPVVTWrhprtkalllrsggfhgKGVMGmlksantsts 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 270 AALVKMSELLPTITERRH----------ENIMFENIRKSHPQKMQPVVIELNKEINVKliaVGFSKFISLCSAENIrqFW 339
Cdd:cd14534   81 SPTVSSSETSSSLEQEKYlsalvlyvlgEKSQMKGVKAESDPKCEFIPVEYPEVRQVK---ASFKKLLRACVPSSA--PT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 340 VQDNNFYSLLENTKWLKYISYCLQKAADVCDRLNL-GYSVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLLQKEW 418
Cdd:cd14534  156 EPEQSFLKAVEDSEWLQQLQCLMQLSGAVVDLLDVqGSSVLLCLEDGWDVTTQVSSLSQLLLDPYYRTLEGFRVLVEKEW 235

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 749750396 419 VAGGHPFCDRLGHIVKT-NSEKSPLFLLYLDCVWQLCQQ 456
Cdd:cd14534  236 LAFGHRFSHRSNLTAASqSSGFAPVFLQFLDAVHQIHRQ 274
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
 340-473 2.48e-33

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: 128.33  E-value: 2.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 340 VQDNNFYSLLENTKWLKYISYCLQKAADVCDRLNLG-YSVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLLQKEW 418
Cdd:cd14535  110 IDDSHWLSNLESTHWLEHIKLILAGAVRIADKVESGkTSVVVHCSDGWDRTAQLTSLAMLMLDPYYRTIRGFEVLIEKEW 189

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749750396 419 VAGGHPFCDRLGHIVK--TNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWD 473
Cdd:cd14535  190 LSFGHKFAQRIGHGDKnhSDADRSPVFLQFIDCVWQMTRQFPNAFEFNEHFLITILD 246
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 340-473 1.73e-32

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: 126.30  E-value: 1.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 340 VQDNNFYSLLENTKWLKYISYCLQKAADVCDRLNLG-YSVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLLQKEW 418
Cdd:cd14590  123 IEESHWLSNLESTHWLEHIKLILAGALRIADKVESGkTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEW 202

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749750396 419 VAGGHPFCDRLGHIVK--TNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWD 473
Cdd:cd14590  203 LSFGHRFQLRVGHGDKnhADADRSPVFLQFIDCVWQMTRQFPTAFEFNEYFLITILD 259
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 340-473 3.29e-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: 122.40  E-value: 3.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 340 VQDNNFYSLLENTKWLKYISYCLQKAADVCDRLNLG-YSVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLLQKEW 418
Cdd:cd14592  110 IDEARWLSNVDGTHWLEYIRMLLAGAVRIADKIESGkTSVVVHCSDGWDRTAQLTSLAMLMLDSYYRTIKGFEVLIEKEW 189

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749750396 419 VAGGHPFCDRLGH--IVKTNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWD 473
Cdd:cd14592  190 ISFGHRFALRVGHgdDNHADADRSPIFLQFIDCVWQMTRQFPSAFEFNELFLITILD 246
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 217-476 4.88e-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 [Multi-domain]  Cd Length: 302  Bit Score: 123.12  E-value: 4.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 217 WRLSTVNAKFQLCPSLSQYVIVPASVTDRQLTDAAK-HFQGNRPLVWSWTSVYGAALVKMSELLPTITERRHENI-MFEN 294
Cdd:cd14585   15 WQLSDVNRDYKICDTYPRDLYVPITASKPIIVGSSKfRSKGRFPVLSYYHQEKKAAICRCSQPLSGFSARCLEDEhMLQA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 295 IRKSHPQKMQPVVIELNKEIN-------------------VKLIAVG----------FSKFISLCSAENIRQfwvqdNNF 345
Cdd:cd14585   95 ISKANPNNRYMYVMDTRPKLNamanraagkgyenednysnIRFQFVGienihvmrssLQKLLEVCGTKALSV-----NDF 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 346 YSLLENTKWLKYISYCLQKAADVCDRLNL-GYSVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLLQKEWVAGGHP 424
Cdd:cd14585  170 LSGLESSGWLRHIKAVLDAAVFLAKAVAVeGASVLVHCSDGWDRTAQVCSLGSLLLDPYYRTIKGFMVLIEKDWISFGHK 249

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 749750396 425 FCDRLGHIVKTNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWDTAH 476
Cdd:cd14585  250 FSDRCGQLDGDPKEISPVFTQFLECVWQLTEQFPRAFEFSEAFLLQIHEHIH 301
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 199-473 2.50e-29

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: 118.44  E-value: 2.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 199 DWQNELRRT-LSNDQirkaWRLSTVNAKFQLCPSLSQYVIVPASVTDRQLTDAAK-HFQGNRPLVWSWTSVYGAALVKMS 276
Cdd:cd14584    6 DLKVDFQRMgIPNDY----WEITDANKNYEICSTYPPELVVPKSASKATVVGSSKfRSRGRFPVLSYLYKENNAAICRCS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 277 ELLPTITERRHEN-IMFENIRKSHPQKMQPVVIELNKEINVKLIAVGFSKFISLCSAENIR-QFWVQDN----------- 343
Cdd:cd14584   82 QPLSGFSARCVEDeQMLQAISKANPGSPFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIRfQFIGIENihvmrsslqkl 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 344 ------------NFYSLLENTKWLKYISYCLQK----AADVCDRlnlGYSVILQEGAGRDLCCVISSLVQLLLDPHFRTI 407
Cdd:cd14584  162 levcemkspsmsDFLTGLENSGWLRHIKAVMDAgvflAKAVKEE---KASVLVHCSDGWDRTAQVCSLASLLLDPFYRTI 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749750396 408 TGFQSLLQKEWVAGGHPFCDRLGHIVKTNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYLTTLWD 473
Cdd:cd14584  239 KGLMVLIEKEWISMGHKFSQRCGHLDGDPKEVSPVFTQFLECVWQLMEQFPCAFEFNEHFLLEIHD 304
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 217-468 1.81e-28

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: 115.83  E-value: 1.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 217 WRLSTVNAKFQLCPSLSQYVIVPASVTDRQLTDAAK-HFQGNRPLVWSWTSVYGAALVKMSELLPTITERRHEN-IMFEN 294
Cdd:cd14583   15 WQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKfRSRGRFPVLSYYCKDNNASICRSSQPLSGFSARCLEDeQMLQA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 295 IRKSHPQKMQPVVIELNKEINV---KLIAVGFS----------KFISLcsaENIRqfwVQDNNFYSL------------- 348
Cdd:cd14583   95 IRKANPGSDFMYVVDTRPKLNAmanRAAGKGYEnednysnikfQFIGI---ENIH---VMRNSLQKMlevcelrspsmgd 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 349 ----LENTKWLKYISYCLQK----AADVCDRlnlGYSVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLLQKEWVA 420
Cdd:cd14583  169 flwgLENSGWLKHIKAIMDAgifiAKAVAEE---GASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVS 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 749750396 421 GGHPFCDRLGHIVKTNSEKSPLFLLYLDCVWQLCQQYPTEFEFTETYL 468
Cdd:cd14583  246 FGHKFNHRYGHLDGDPKEVSPVIDQFIECVWQLMEQFPCAFEFNERFL 293
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 213-452 2.19e-25

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: 107.41  E-value: 2.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 213 IRKAWRLSTVNAKFQLCPSLSQYVIVPASVTDRQLTDAA-------------KHfQGN--------RPLV--WSWTSVYG 269
Cdd:cd14586    4 MQNAWRISNINEKYKLCGSYPQELIVPAWITDKELESVAsfrswkripavvyRH-QSNgaviarcgQPEVswWGWRNADD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 270 AALVK-MSELLPTITERRHENIMFENIRKSHPQKMQPVVIELNKEI---------------------------------- 314
Cdd:cd14586   83 EHLVQsVAKACASDSSSCKSVLMTGNCSRDFPNGGDLSDVEFDSSMsnasgveslaiqpqkllildarsyaaavanrakg 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 315 ----------NVKLIAVGFSKFISL-CSAENIRQFWVQ---DNNFYSLLENTKWLKYISYCLQKAADVCDRLNLGYS-VI 379
Cdd:cd14586  163 ggcecpeyypNCEVVFMGMANIHSIrKSFQSLRLLCTQmpdPANWLSALESTKWLQHLSMLLKSALLVVHAVDRDQRpVL 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749750396 380 LQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLLQKEWVAGGHPFCDRLGHIVKTN--SEKSPLFLLYLDCVWQ 452
Cdd:cd14586  243 VHCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRCGHGENSDdlNERCPVFLQWLDCVHQ 317
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 344-452 2.96e-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: 104.41  E-value: 2.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 344 NFYSLLENTKWLKYISYCLQKAADVCDRLNL-GYSVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLLQKEWVAGG 422
Cdd:cd14533  118 NWLSNLESTKWLHHLSGLLKAALLVVNAVDEeGRPVLVHCSDGWDRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFG 197

                         90       100       110
                 ....*....|....*....|....*....|..
gi 749750396 423 HPFCDRLGHIVKTN--SEKSPLFLLYLDCVWQ 452
Cdd:cd14533  198 HKFADRCGHGVNSEdiNERCPVFLQWLDCVHQ 229
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 216-452 1.08e-24

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: 105.11  E-value: 1.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 216 AWRLSTVNAKFQLCPSLSQYVIVPASVTDRQLTDAAKHFQGNR-PLV---------------------WSW--------- 264
Cdd:cd14587    2 VWRVSEINSNYKLCSSYPQKLLVPVWITDKELENVASFRSWKRiPVVvyrhlrngaviarcsqpeiswWGWrnaddeylv 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 265 TSVYGAAL----VKMSELLPTITERRHENIMFENIRKS-----------HPQKMqpVVIEL------------------- 310
Cdd:cd14587   82 TSIAKACAldpgTRAPGGSPSKGNSDGSDASDTDFDSSltacsavesgaAPQKL--LILDArsytaavanrakgggcece 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 311 ----NKEI------NVKLIAVGFSKFISLCSAenirqfwVQD-NNFYSLLENTKWLKYISYCLQKAADVCDRLNL-GYSV 378
Cdd:cd14587  160 eyypNCEVmfmgmaNIHSIRNSFQYLRAVCSQ-------MPDpGNWLSALESTKWLQHLSVMLKAAVLVASAVDReGRPV 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749750396 379 ILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLLQKEWVAGGHPFCDRLGH--IVKTNSEKSPLFLLYLDCVWQ 452
Cdd:cd14587  233 LVHCSDGWDRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHqeNVEDQNEQCPVFLQWLDCVHQ 308
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 347-452 1.29e-24

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: 102.42  E-value: 1.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 347 SLLENTKWLKYISYCLQKAADV--C-DRLnlGYSVILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLLQKEWVAGGH 423
Cdd:cd14536  115 SKLESSNWLSHVKEILTTACLVaqCiDRE--GASVLVHGSEGMDSTLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGH 192

                         90       100       110
                 ....*....|....*....|....*....|..
gi 749750396 424 PFCDRLGHIVKTNS---EKSPLFLLYLDCVWQ 452
Cdd:cd14536  193 PFQSRCAKSAYSNSkqkFESPVFLLFLDCVWQ 224
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
 348-452 6.02e-23

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: 97.90  E-value: 6.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 348 LLENTKWLKYISYCLQKAADVCDRLNLGYS-VILQEGAGRDLCCVISSLVQLLLDPHFRTITGFQSLLQKEWVAGGHPFC 426
Cdd:cd17666  129 ALKKSNWLKYLAIILQGADLIAKSIHFNHShVLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFA 208

                         90       100
                 ....*....|....*....|....*.
gi 749750396 427 DRLGHivktnSEKSPLFLLYLDCVWQ 452
Cdd:cd17666  209 ERSGH-----KETSPVFHQFLDCVYQ 229
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 217-456 3.26e-22

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: 97.35  E-value: 3.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 217 WRLSTVNAKFQLCPSLSQYVIVPASVTDRQLTDAAKHFQGNRPLVWSW----------------------------TSVY 268
Cdd:cd14588    1 FRISTVNRMYAVCRSYPGLLIVPQSIQDNTIQRISRCYRQNRFPVVCWrnsrtkavllrsgglhgkgvvglfksqnAPAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 269 GAALVKMSEL------------LPTITERRHENIM---------------FENIRKSHPQKMQPVVIELnkeINVKLIAV 321
Cdd:cd14588   81 GQSQTDSTSLeqekylqavinsMPRYADASGRNTLsgfraalyiigdksqLKGVKQDPLQQWEVVPIEV---FDVRQVKA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 322 GFSKFISLCSAENIRQfwVQDNNFYSLLENTKWLKYISYCLQKAADVCDRLNLGYSVILQEGAGRDLCCVISSLVQLLLD 401
Cdd:cd14588  158 SFKKLMKACVPSCPST--DPSQTYLRTLEESEWLSQLHKLLQVSVLVVELLDSGSSVLVSLEDGWDITTQVVSLVQLLSD 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 749750396 402 PHFRTITGFQSLLQKEWVAGGHPFCDRLGHIVKTNSEK-SPLFLLYLDCVWQLCQQ 456
Cdd:cd14588  236 PYYRTIEGFRLLVEKEWLSFGHRFSHRGAQTLASQSSGfTPVFLQFLDCVHQIHLQ 291
PH-GRAM_MTMR12 cd13348
Myotubularian (MTM) related 12 protein (MTMR12) Pleckstrin Homology-Glucosyltransferases, ...
 33-182 7.57e-20

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: 87.60  E-value: 7.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  33 ENSIKLLPGEVLIAEAQSVLMFSPVSDLKQGISGVLSVTNFKLTFItSDDSNGEDVTHQ-QNHLYGYTDTCLTNIDEIYi 111
Cdd:cd13348   15 EVNPHLLPGEVVLCEANTVLKYTQDDGSQRGVYGRLVCTNFRIAFL-GDDAPQDDNSKQfKNKIYGENDITLQCVDQIY- 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749750396 112 MVGDKKRKLVPGNTVPSKVKGIFII-CKNLRTWSFSFKFSPLGHGKNLLTALLHHAF-PSRHQLLFAYDYKEA 182
Cdd:cd13348   93 GVYDEKKKLITGGLVKNKYPEKLIIhCKDLRVFQFCLRYTKEEEVKRIVSGIIHHTQePKLLKRLFLFSYARA 165
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 217-456 9.60e-20

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: 90.37  E-value: 9.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 217 WRLSTVNAKFQLCPSLSQYVIVPASVTDRQLTDAAKHFQGNRPLVWSWTSVYGAALVKMS------------------EL 278
Cdd:cd14589    1 FRITAVNRMYSLCRSYPGLLVVPQSVQDSSLQKVARCYRHNRLPVVCWKNSKTKAVLLRSggfhgkgvvglfksqnphSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 279 LPTITER-----------------------------------RHENIMFENIRKSHPQKMQpVVIELNKEI------NVK 317
Cdd:cd14589   81 APASSESsssieqekylqallnaisvhqkmngnstllqsqllKRQAALYIFGEKSQLRGFK-LDFALNCEFvpvefhDIR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396 318 LIAVGFSKFISLCSAENIRQfwVQDNNFYSLLENTKWLKYISYCLQKAADVCDRLNLGYSVILQEGAGRDLCCVISSLVQ 397
Cdd:cd14589  160 QVKASFKKLMRACVPSTIPT--DSEVTFLKALGESEWFLQLHRIMQLAVVISELLESGSSVMVCLEDGWDITTQVVSLVQ 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749750396 398 LLLDPHFRTITGFQSLLQKEWVAGGHPFCDRLGhiVKTNSEKS---PLFLLYLDCVWQLCQQ 456
Cdd:cd14589  238 LLSDPFYRTLEGFQMLVEKEWLSFGHKFSQRSN--LTPNSQGSgfaPIFLQFLDCVHQIHNQ 297
PH-GRAM_MTMR10-like cd13212
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 39-150 1.16e-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: 73.81  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  39 LPGEVLIAEAQSVLMFSPVSDLKQGISGVLSVTNFKLTFITsDDSNGEDVTHQQNHLYGYTDTCLTNIDEIYIMVGDK-K 117
Cdd:cd13212    1 LPGEQVLAEAPGVRKGLQEDSSQPELSGTLICTNFKITFQP-DDWQWLDNTQQKNPLNGEYDFALVCIGQIEAVSDLKrV 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 749750396 118 RKLVPGNTVPSKVKGIFIICKNLRTWSFSFKFS 150
Cdd:cd13212   80 QLLRPGSLLKFIPEELIIHCKDFRVLRFGFEAT 112
PH-GRAM_MTMR10 cd13346
Myotubularian (MTM) related 10 protein (MTMR10) Pleckstrin Homology-Glucosyltransferases, ...
 37-189 2.68e-15

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: 74.19  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  37 KLLPGEVLIAEAQSVLMFSPVSDLKQGISGVLSVTNFKLTFITsDDSNGEDVTHQQNHLYGYTDTCLTNIDEIyIMVGDK 116
Cdd:cd13346   17 VLLPGEIVVNEVNFVRKCIATDTSQYDLWGKLICTNFKISFIT-DDPMPLQKFHYKNLLLGEHDVPLTCIEQI-VTVNDT 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749750396 117 KRK---LVPGNTVPSKVKGIFIICKNLRTWSFSFKFSPLGHGKNLLTALLHHAFPSRHQLLFAYDY-KEAYYSSLDK 189
Cdd:cd13346   95 KRKqkvLGPNQKLKFNPTELIIYCKDFRIVRFRFDEAGPESAKKVCLAIAHYSQPTDLQLLFAFEYvGKKYHNSAGK 171
PH-GRAM_MTMR11 cd15790
Myotubularian (MTM) related 11 protein (MTMR11) Pleckstrin Homology-Glucosyltransferases, ...
 39-152 3.56e-07

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: 49.39  E-value: 3.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749750396  39 LPGEVLIAEAQSVLMFSPVSDLKQGISGVLSVTNFKLTFITSD---DSNGEDVTHQQNHlygytDTCLTNIDEIYIMVGD 115
Cdd:cd15790    1 LPGEHILEEAVRVRKLVQWRDGEGFLSGTLYCTNFRVAFVPEHiqkDENDHDTVLNSEH-----DIALPSIDRVVAVQGP 75

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 749750396 116 KKRKLV-PGNTVPSKVKGIFIICKNLRTWSFSFKFSPL 152
Cdd:cd15790   76 TTMKAVtASSGLKFIPEELVIYCRDFRLLRFQFEQSTL 113
3-PAP pfam12578
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
 540-571 2.30e-05

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: 463634  Cd Length: 132  Bit Score: 44.28  E-value: 2.30e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 749750396  540 VIKPSCAISNLELWTQCYFRWIPALEIHNGGQ 571
Cdd:pfam12578  71 LLLPLLSGPHIKLWKLCYLRWVPEAQINHGGP 102
 
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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