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Conserved domains on  [gi|578800472|ref|XP_006711200|]
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myotubularin-related protein 11 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 182-372 8.98e-109

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


The actual alignment was detected with superfamily member cd14595:

Pssm-ID: 475123  Cd Length: 195  Bit Score: 325.63  E-value: 8.98e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 182 GRGPRLSWHHPGGSDLLRCGGFYTASDPNKEDIRAVELMLQAGHSDVVLVDTMDELPSLADVQLAHLRLRALCLPDSSVA 261
Cdd:cd14595    1 GRIPRWCWHHPGGSDLLRMAGFYTNSDPEKEDIRSVELLLQAGHSQCVIVDTSEELPSPADIQLAYLKLRTLCLPDISVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 262 ED--KWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREW 339
Cdd:cd14595   81 VSdeKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEW 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578800472 340 VAAGHPFLTRLGGTG--ASEEAPVFLLFLDCVWQL 372
Cdd:cd14595  161 VVAGHPFLQRLNLTResDKEESPVFLLFLDCVWQL 195
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 4-88 1.17e-41

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 cd15790:

Pssm-ID: 473070  Cd Length: 123  Bit Score: 146.84  E-value: 1.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472   4 RVTFQPCGWQWN---QDTPLNSEYDFALVNIGRLEAVSGLSRVQLLRPGSLHKFIPEEILIHGRDFRLLRVGFEAGGLEP 80
Cdd:cd15790   36 RVAFVPEHIQKDendHDTVLNSEHDIALPSIDRVVAVQGPTTMKAVTASSGLKFIPEELVIYCRDFRLLRFQFEQSTLEP 115


                 ....*...
gi 578800472  81 QAFQVTMA 88
Cdd:cd15790  116 QAFQITTA 123
3-PAP super family cl13953
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
 479-606 7.29e-20

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: 85.88  E-value: 7.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472  479 SFMVPGPPSSVwlfSRGalTPLNQLCPWRDSPSLLAVSSRWLPRPaiSSESlaDQEWGLPSHWGACPLPPGLL-LPGYLG 557
Cdd:pfam12578   8 SSTLRGPPPSL---KNG--LFRDEEDLLRRNSLLLRLKPDCPLHR--SSDS--NDSEQFFRDWFSKPADLHGLlLPLLSG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578800472  558 PQIRLWRRCYLRGRPEVQMGLSAP-----TISGLQDELSHLQELLRKWTPRISP 606
Cdd:pfam12578  79 PHIKLWKLCYLRWVPEAQINHGGPitafhKLSLLADEVEALQRLLRQYRGGPSE 132
 
Name Accession Description Interval E-value
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 182-372 8.98e-109

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: 325.63  E-value: 8.98e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 182 GRGPRLSWHHPGGSDLLRCGGFYTASDPNKEDIRAVELMLQAGHSDVVLVDTMDELPSLADVQLAHLRLRALCLPDSSVA 261
Cdd:cd14595    1 GRIPRWCWHHPGGSDLLRMAGFYTNSDPEKEDIRSVELLLQAGHSQCVIVDTSEELPSPADIQLAYLKLRTLCLPDISVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 262 ED--KWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREW 339
Cdd:cd14595   81 VSdeKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEW 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578800472 340 VAAGHPFLTRLGGTG--ASEEAPVFLLFLDCVWQL 372
Cdd:cd14595  161 VVAGHPFLQRLNLTResDKEESPVFLLFLDCVWQL 195
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 129-394 1.67e-49

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: 175.36  E-value: 1.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472  129 DWETERKKQ---AARGWRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHPG-GSDLLRCG--- 201
Cdd:pfam06602   9 DPEAEFARQglpSKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKEnGAVITRSSqpl 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472  202 -GFytASDPNKEDiravELMLQA--------GHSDVVLVDTMDELPSLA---------------DVQLAHL--------- 248
Cdd:pfam06602  89 vGL--NGKRSIED----EKLLQAifkssnpySAKKLYIVDARPKLNAMAnrakgggyenednypNCKKIFLgienihvmr 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472  249 ----RLRALCLpDSSVAEDKWLSALEGTRWLDYVRACLRKASDI---------SVLV--------TSRVRS---VILqer 304
Cdd:pfam06602 163 dslnKLVEACN-DRSPSMDKWLSRLESSGWLKHIKAILDGACLIaqavdlegsSVLVhcsdgwdrTAQLTSlaqLLL--- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472  305 gdrDlngllsslvqllsaPEARTLFGFQSLVQREWVAAGHPFLTRLG----GTGASEEAPVFLLFLDCVWQLLQQFPADF 380
Cdd:pfam06602 239 ---D--------------PYYRTIEGFQVLIEKEWLSFGHKFADRCGhlagFTDSKERSPVFLQFLDCVWQLLRQFPCAF 301

                         330
                  ....*....|....
gi 578800472  381 EFSEFFLLALHDSV 394
Cdd:pfam06602 302 EFNERFLIRLLYHL 315
PH-GRAM_MTMR11 cd15790
Myotubularian (MTM) related 11 protein (MTMR11) Pleckstrin Homology-Glucosyltransferases, ...
 4-88 1.17e-41

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: 146.84  E-value: 1.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472   4 RVTFQPCGWQWN---QDTPLNSEYDFALVNIGRLEAVSGLSRVQLLRPGSLHKFIPEEILIHGRDFRLLRVGFEAGGLEP 80
Cdd:cd15790   36 RVAFVPEHIQKDendHDTVLNSEHDIALPSIDRVVAVQGPTTMKAVTASSGLKFIPEELVIYCRDFRLLRFQFEQSTLEP 115


                 ....*...
gi 578800472  81 QAFQVTMA 88
Cdd:cd15790  116 QAFQITTA 123
3-PAP pfam12578
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
 479-606 7.29e-20

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: 85.88  E-value: 7.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472  479 SFMVPGPPSSVwlfSRGalTPLNQLCPWRDSPSLLAVSSRWLPRPaiSSESlaDQEWGLPSHWGACPLPPGLL-LPGYLG 557
Cdd:pfam12578   8 SSTLRGPPPSL---KNG--LFRDEEDLLRRNSLLLRLKPDCPLHR--SSDS--NDSEQFFRDWFSKPADLHGLlLPLLSG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578800472  558 PQIRLWRRCYLRGRPEVQMGLSAP-----TISGLQDELSHLQELLRKWTPRISP 606
Cdd:pfam12578  79 PHIKLWKLCYLRWVPEAQINHGGPitafhKLSLLADEVEALQRLLRQYRGGPSE 132
 
Name Accession Description Interval E-value
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 182-372 8.98e-109

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: 325.63  E-value: 8.98e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 182 GRGPRLSWHHPGGSDLLRCGGFYTASDPNKEDIRAVELMLQAGHSDVVLVDTMDELPSLADVQLAHLRLRALCLPDSSVA 261
Cdd:cd14595    1 GRIPRWCWHHPGGSDLLRMAGFYTNSDPEKEDIRSVELLLQAGHSQCVIVDTSEELPSPADIQLAYLKLRTLCLPDISVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 262 ED--KWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREW 339
Cdd:cd14595   81 VSdeKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEW 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578800472 340 VAAGHPFLTRLGGTG--ASEEAPVFLLFLDCVWQL 372
Cdd:cd14595  161 VVAGHPFLQRLNLTResDKEESPVFLLFLDCVWQL 195
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 182-371 2.73e-75

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: 239.17  E-value: 2.73e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 182 GRGPRLSWHHPGGSDLLRCGGFYtasdpNKEDIRAVELMLQ-------AGHSDVVLVDTMDELPSLADVQLAHLRLRALC 254
Cdd:cd14537    1 GRPPVWCWSHPNGAALVRMAELL-----PTITDRTQENKMLeairkshPNLKKPKVIDLDKLLPSLQDVQAAYLKLRELC 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 255 LPDSSVAED----KWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFG 330
Cdd:cd14537   76 TPDSSEQFWvqdsKWYSLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQESDGRDLSCVVSSLVQLLLDPHFRTITG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 578800472 331 FQSLVQREWVAAGHPFLTRLGGT----GASEEAPVFLLFLDCVWQ 371
Cdd:cd14537  156 FQSLIQKEWVALGHPFCDRLGHVkpnkTESEESPVFLLFLDCVWQ 200
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 129-394 1.67e-49

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: 175.36  E-value: 1.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472  129 DWETERKKQ---AARGWRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHPG-GSDLLRCG--- 201
Cdd:pfam06602   9 DPEAEFARQglpSKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKEnGAVITRSSqpl 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472  202 -GFytASDPNKEDiravELMLQA--------GHSDVVLVDTMDELPSLA---------------DVQLAHL--------- 248
Cdd:pfam06602  89 vGL--NGKRSIED----EKLLQAifkssnpySAKKLYIVDARPKLNAMAnrakgggyenednypNCKKIFLgienihvmr 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472  249 ----RLRALCLpDSSVAEDKWLSALEGTRWLDYVRACLRKASDI---------SVLV--------TSRVRS---VILqer 304
Cdd:pfam06602 163 dslnKLVEACN-DRSPSMDKWLSRLESSGWLKHIKAILDGACLIaqavdlegsSVLVhcsdgwdrTAQLTSlaqLLL--- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472  305 gdrDlngllsslvqllsaPEARTLFGFQSLVQREWVAAGHPFLTRLG----GTGASEEAPVFLLFLDCVWQLLQQFPADF 380
Cdd:pfam06602 239 ---D--------------PYYRTIEGFQVLIEKEWLSFGHKFADRCGhlagFTDSKERSPVFLQFLDCVWQLLRQFPCAF 301

                         330
                  ....*....|....
gi 578800472  381 EFSEFFLLALHDSV 394
Cdd:pfam06602 302 EFNERFLIRLLYHL 315
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 182-371 6.51e-44

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: 155.82  E-value: 6.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 182 GRGPRLSWHHPGGSDLLRCGGFYTASDPNKEDIRAVELMLQAG--HSDVVLVDTMDELPSLADVQLAHLRLRALCLPDS- 258
Cdd:cd14593    1 RRIPLWCWNHPNGSALVRMANIKDLLQQRKIDQRICNAITRSHplRSDVYKSDLDKTLPNIQEIQAAFVKLKQLCVNEPf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 259 SVAEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQRE 338
Cdd:cd14593   81 EETEEKWLSSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLVQVMLDPYFRTITGFQSLIQKE 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578800472 339 WVAAGHPFLTRLGGTGAS--EEAPVFLLFLDCVWQ 371
Cdd:cd14593  161 WVMAGYRFLDRCNHLKKSskKESPLFLLFLDCVWQ 195
PH-GRAM_MTMR11 cd15790
Myotubularian (MTM) related 11 protein (MTMR11) Pleckstrin Homology-Glucosyltransferases, ...
 4-88 1.17e-41

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: 146.84  E-value: 1.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472   4 RVTFQPCGWQWN---QDTPLNSEYDFALVNIGRLEAVSGLSRVQLLRPGSLHKFIPEEILIHGRDFRLLRVGFEAGGLEP 80
Cdd:cd15790   36 RVAFVPEHIQKDendHDTVLNSEHDIALPSIDRVVAVQGPTTMKAVTASSGLKFIPEELVIYCRDFRLLRFQFEQSTLEP 115


                 ....*...
gi 578800472  81 QAFQVTMA 88
Cdd:cd15790  116 QAFQITTA 123
PH-GRAM_MTMR10-like cd13212
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 4-88 5.30e-40

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: 142.37  E-value: 5.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472   4 RVTFQPCGWQWNQ----DTPLNSEYDFALVNIGRLEAVSGLSRVQLLRPGSLHKFIPEEILIHGRDFRLLRVGFEA-GGL 78
Cdd:cd13212   36 KITFQPDDWQWLDntqqKNPLNGEYDFALVCIGQIEAVSDLKRVQLLRPGSLLKFIPEELIIHCKDFRVLRFGFEAtGGE 115

                         90
                 ....*....|
gi 578800472  79 EPQAFQVTMA 88
Cdd:cd13212  116 EPKAFQVTIA 125
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 185-372 1.14e-34

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: 130.35  E-value: 1.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 185 PRLSWHHPGGSDLLRCGGF-----YTASDPNKEDIRAVELMLQAGHSDVVLVDTMDE-LPSLADVQLAHLRLRALCLPDS 258
Cdd:cd14594    4 PIWCWSCHNGCALLKMSALpkeqdDVALQDQKSFLDRIYKTLSRPPYESVKTEDLSAsLPSLQEIQTAYNRFKQLFLIDN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 259 SV----AEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSL 334
Cdd:cd14594   84 STdfwdTDVKWFSSLESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQSL 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 578800472 335 VQREWVAAGHPFLTRLGGTGAS--EEAPVFLLFLDCVWQL 372
Cdd:cd14594  164 IQKEWVMGGHCFLDRCNHLRQNdkEEVPVFLLFLDCVWQL 203
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 142-394 2.51e-34

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: 132.47  E-value: 2.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 142 WRVSTVNERFDVATSLPRYFWVPnRILDSEVRRAFGHFH-QGRGPRLSWHHPGG-SDLLRC----GGFYTASDpnkEDIR 215
Cdd:cd14532   15 WTLSDINKDYELCDTYPRELFVP-TSASTPVLVGSSKFRsKGRLPVLSYLHKDNqAAICRCsqplSGFSARCV---EDEQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 216 AVELMLQAG-HSDVV-LVDTMDELPSLA----------------------DVQLAH-LR------LRALCLPDSSVaeDK 264
Cdd:cd14532   91 LLQAIRKANpNSKFMyVVDTRPKINAMAnkaagkgyenednysnikfqffGIENIHvMRsslqklLEVCELKNPSM--SA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 265 WLSALEGTRWLDYVRACLrkasDISVLVTSRVR---SVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVA 341
Cdd:cd14532  169 FLSGLESSGWLKHIKAVM----DTSVFIAKAVSegaSVLVHCSDGWDRTAQTCSLASLLLDPYYRTIKGFQVLIEKEWLS 244

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578800472 342 AGHPFLTRLG--GTGASEEAPVFLLFLDCVWQLLQQFPADFEFSEFFLLALHDSV 394
Cdd:cd14532  245 FGHKFTDRCGhlQGDAKEVSPVFTQFLDCVWQLMQQFPRAFEFNERFLLTLHDHV 299
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
 182-392 7.12e-29

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: 115.62  E-value: 7.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 182 GRGPRLSWHHP-GGSDLLRCggfytaSDP--------NKEDIRAVELMLQA-GHSDVVLVdtMDELPS------------ 239
Cdd:cd14535    1 NRIPVLSWIHPeSQATITRC------SQPlvgvsgkrSKDDEKYLQLIMDAnAQSHKLFI--MDARPSvnavankakggg 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 240 -------------LADVQLAHL------RLRALCLPdsSVAEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVI 300
Cdd:cd14535   73 yesedayqnaelvFLDIHNIHVmreslrKLKDICFP--NIDDSHWLSNLESTHWLEHIKLILAGAVRIADKVESGKTSVV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 301 LQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGHPFLTRLG----GTGASEEAPVFLLFLDCVWQLLQQF 376
Cdd:cd14535  151 VHCSDGWDRTAQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGhgdkNHSDADRSPVFLQFIDCVWQMTRQF 230

                        250
                 ....*....|....*.
gi 578800472 377 PADFEFSEFFLLALHD 392
Cdd:cd14535  231 PNAFEFNEHFLITILD 246
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 169-392 3.65e-28

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: 113.98  E-value: 3.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 169 DSEVRRAFGHFHQGRGPRLSWHHP-GGSDLLRCggfytaSDP--------NKEDIRAVELMLQA-GHSDVVLVdtMDELP 238
Cdd:cd14590    1 DEELKRVASFRSRGRIPVLSWIHPeSQATITRC------SQPmvgvsgkrSKEDEKYLQAIMDSnAQSHKIFI--FDARP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 239 SL-------------------------ADVQLAHL------RLRALCLPDssVAEDKWLSALEGTRWLDYVRACLRKASD 287
Cdd:cd14590   73 SVnavankakgggyesedayqnaelvfLDIHNIHVmreslrKLKEIVYPN--IEESHWLSNLESTHWLEHIKLILAGALR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 288 ISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGHPFLTRLG----GTGASEEAPVFL 363
Cdd:cd14590  151 IADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGhgdkNHADADRSPVFL 230

                        250       260
                 ....*....|....*....|....*....
gi 578800472 364 LFLDCVWQLLQQFPADFEFSEFFLLALHD 392
Cdd:cd14590  231 QFIDCVWQMTRQFPTAFEFNEYFLITILD 259
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 182-392 1.52e-27

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: 111.61  E-value: 1.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 182 GRGPRLSWHHP-GGSDLLRCGG-FYTASDPN-KEDIRAVELMLQAGHSDVVLVDTMDELPSLAD---------------- 242
Cdd:cd14592    1 GRVPVLSWIHPeSQATITRCSQpLVGPNDKRcKEDEKYLQTIMDANAQSHKLIIFDARQNSVADtnktkgggyesesayp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 243 -VQLAHL-------------RLRALCLPdsSVAEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRD 308
Cdd:cd14592   81 nAELVFLeihnihvmreslrKLKEIVYP--SIDEARWLSNVDGTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGWD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 309 LNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGHPFLTRLGGTGA----SEEAPVFLLFLDCVWQLLQQFPADFEFSE 384
Cdd:cd14592  159 RTAQLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGHGDDnhadADRSPIFLQFIDCVWQMTRQFPSAFEFNE 238


                 ....*...
gi 578800472 385 FFLLALHD 392
Cdd:cd14592  239 LFLITILD 246
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
 182-371 3.05e-27

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: 109.94  E-value: 3.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 182 GRGPRLSWHHP-GGSDLLRCG----GFYTASdpNKEDIRAVELMLQAGHSDVVLVdTMDELPSLA--------------- 241
Cdd:cd14507    1 GRIPVLSWRHPrNGAVICRSSqplvGLTGSR--SKEDEKLLNAIRKASPSSKKLY-IVDARPKLNavanrakgggyente 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 242 ---DVQLAHL-------------RLRALCLPDSSVaEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQ-ER 304
Cdd:cd14507   78 yypNCELEFLnienihamrdslnKLRDACLSPNDE-ESNWLSALESSGWLEHIRLILKGAVRVADLLEKEGTSVLVHcSD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 305 G-DR------------DlngllsslvqllsaPEARTLFGFQSLVQREWVAAGHPFLTRLGGTGA----SEEAPVFLLFLD 367
Cdd:cd14507  157 GwDRtsqltslaqlllD--------------PYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDKnssdEERSPIFLQFLD 222


                 ....
gi 578800472 368 CVWQ 371
Cdd:cd14507  223 CVWQ 226
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
 183-392 4.86e-27

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: 110.12  E-value: 4.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 183 RGPRLSWHHP-GGSDLLRCggfytaSDP--------NKEDIRAVELMLQAGH--SDVVLVDTMDELPSLA---------- 241
Cdd:cd14591    2 RIPVLSWIHPeNQAVIMRC------SQPlvgmsgkrNKDDEKYLDIIREANGqtSKLTIYDARPSVNAVAnkatgggyeg 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 242 ------------DVQLAHL------RLRALCLPDssVAEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQE 303
Cdd:cd14591   76 ddayqnaelvflDIHNIHVmreslkKLKDIVYPN--VEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHC 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 304 RGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGHPFLTRLG----GTGASEEAPVFLLFLDCVWQLLQQFPAD 379
Cdd:cd14591  154 SDGWDRTAQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGhgdkNHADADRSPIFLQFIDCVWQMSKQFPTA 233

                        250
                 ....*....|...
gi 578800472 380 FEFSEFFLLALHD 392
Cdd:cd14591  234 FEFNEQFLITILD 246
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 142-394 1.14e-23

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: 101.87  E-value: 1.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 142 WRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHP-GGSDLLRCG----GFYTASdpnKEDira 216
Cdd:cd14584   21 WEITDANKNYEICSTYPPELVVPKSASKATVVGSSKFRSRGRFPVLSYLYKeNNAAICRCSqplsGFSARC---VED--- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 217 vELMLQA------GHSDVVLVDTMDELPSLAD----------------------VQLAHL------RLRALCLPDSSVAE 262
Cdd:cd14584   95 -EQMLQAiskanpGSPFMYVVDTRPKLNAMANraagkgyenednysnirfqfigIENIHVmrsslqKLLEVCEMKSPSMS 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 263 DkWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAA 342
Cdd:cd14584  174 D-FLTGLENSGWLRHIKAVMDAGVFLAKAVKEEKASVLVHCSDGWDRTAQVCSLASLLLDPFYRTIKGLMVLIEKEWISM 252

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578800472 343 GHPFLTRLG--GTGASEEAPVFLLFLDCVWQLLQQFPADFEFSEFFLLALHDSV 394
Cdd:cd14584  253 GHKFSQRCGhlDGDPKEVSPVFTQFLECVWQLMEQFPCAFEFNEHFLLEIHDHV 306
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 142-375 5.53e-23

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: 98.98  E-value: 5.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 142 WRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHPG-GSDLLRCGGFYTAS------------- 207
Cdd:cd14534    1 FRISTANRDYSICRSYPALVVVPQSVSDESLRKVARCYRQGRFPVVTWRHPRtKALLLRSGGFHGKGvmgmlksantsts 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 208 ---DPNKEDIRAVELM--LQA---------GHSDVVLVDT-------MDELPSLADVQLAHLRLRALCLPDSSVAEDK-- 264
Cdd:cd14534   81 sptVSSSETSSSLEQEkyLSAlvlyvlgekSQMKGVKAESdpkcefiPVEYPEVRQVKASFKKLLRACVPSSAPTEPEqs 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 265 WLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGH 344
Cdd:cd14534  161 FLKAVEDSEWLQQLQCLMQLSGAVVDLLDVQGSSVLLCLEDGWDVTTQVSSLSQLLLDPYYRTLEGFRVLVEKEWLAFGH 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 578800472 345 PFLTRLGGTGASEE---APVFLLFLDCVWQLLQQ 375
Cdd:cd14534  241 RFSHRSNLTAASQSsgfAPVFLQFLDAVHQIHRQ 274
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 142-394 1.27e-22

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: 98.85  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 142 WRVSTVNERFDVATSLPRYFWVPnRILDSEVRRAFGHFH-QGRGPRLSWHHPGG-SDLLRCG----GFytaSDPNKEDIR 215
Cdd:cd14585   15 WQLSDVNRDYKICDTYPRDLYVP-ITASKPIIVGSSKFRsKGRFPVLSYYHQEKkAAICRCSqplsGF---SARCLEDEH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 216 AVELMLQAGHSD--VVLVDTMDELPSLAD---------------------------VQLAHLRLRALCLPDSSVAEDKWL 266
Cdd:cd14585   91 MLQAISKANPNNryMYVMDTRPKLNAMANraagkgyenednysnirfqfvgienihVMRSSLQKLLEVCGTKALSVNDFL 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 267 SALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGHPF 346
Cdd:cd14585  171 SGLESSGWLRHIKAVLDAAVFLAKAVAVEGASVLVHCSDGWDRTAQVCSLGSLLLDPYYRTIKGFMVLIEKDWISFGHKF 250

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 578800472 347 LTRLG--GTGASEEAPVFLLFLDCVWQLLQQFPADFEFSEFFLLALHDSV 394
Cdd:cd14585  251 SDRCGqlDGDPKEISPVFTQFLECVWQLTEQFPRAFEFSEAFLLQIHEHI 300
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 257-371 4.21e-22

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: 95.10  E-value: 4.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 257 DSSVAEDKWLSALEGTRWLDYVR-----ACL----------------RKASDISVLVTSRVRsVILQergdrdlngllss 315
Cdd:cd14536  105 DQGHSMDKWLSKLESSNWLSHVKeilttACLvaqcidregasvlvhgSEGMDSTLQVTSLAQ-IILD------------- 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578800472 316 lvqllsaPEARTLFGFQSLVQREWVAAGHPFLTR-----LGGTGASEEAPVFLLFLDCVWQ 371
Cdd:cd14536  171 -------PDCRTIRGFEALIEREWLQAGHPFQSRcaksaYSNSKQKFESPVFLLFLDCVWQ 224
3-PAP pfam12578
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
 479-606 7.29e-20

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: 85.88  E-value: 7.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472  479 SFMVPGPPSSVwlfSRGalTPLNQLCPWRDSPSLLAVSSRWLPRPaiSSESlaDQEWGLPSHWGACPLPPGLL-LPGYLG 557
Cdd:pfam12578   8 SSTLRGPPPSL---KNG--LFRDEEDLLRRNSLLLRLKPDCPLHR--SSDS--NDSEQFFRDWFSKPADLHGLlLPLLSG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578800472  558 PQIRLWRRCYLRGRPEVQMGLSAP-----TISGLQDELSHLQELLRKWTPRISP 606
Cdd:pfam12578  79 PHIKLWKLCYLRWVPEAQINHGGPitafhKLSLLADEVEALQRLLRQYRGGPSE 132
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 142-394 1.78e-19

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: 89.63  E-value: 1.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 142 WRVSTVNERFDVATSLPRYFWVPNR-----ILDSEVRRAfghfhQGRGPRLSWH-HPGGSDLLRCG----GFytaSDPNK 211
Cdd:cd14583   15 WQVSDVNRDYRVCDTYPTELYVPKSatapiIVGSSKFRS-----RGRFPVLSYYcKDNNASICRSSqplsGF---SARCL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 212 EDiravELMLQA------GHSDVVLVDTMDELPSLAD----------------------VQLAHL------RLRALC-LP 256
Cdd:cd14583   87 ED----EQMLQAirkanpGSDFMYVVDTRPKLNAMANraagkgyenednysnikfqfigIENIHVmrnslqKMLEVCeLR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 257 DSSVAEDKWlsALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQ 336
Cdd:cd14583  163 SPSMGDFLW--GLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIE 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 337 REWVAAGHPFLTRLGGTG--ASEEAPVFLLFLDCVWQLLQQFPADFEFSEFFLLALHDSV 394
Cdd:cd14583  241 KDWVSFGHKFNHRYGHLDgdPKEVSPVIDQFIECVWQLMEQFPCAFEFNERFLIHIHHHI 300
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 250-371 1.36e-16

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: 80.85  E-value: 1.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 250 LRALC--LPDSSvaedKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEART 327
Cdd:cd14587  185 LRAVCsqMPDPG----NWLSALESTKWLQHLSVMLKAAVLVASAVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRT 260

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 578800472 328 LFGFQSLVQREWVAAGHPFLTRLG----GTGASEEAPVFLLFLDCVWQ 371
Cdd:cd14587  261 IEGFQVLVETDWLDFGHKFGDRCGhqenVEDQNEQCPVFLQWLDCVHQ 308
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 250-371 3.01e-16

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: 78.21  E-value: 3.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 250 LRALClpDSSVAEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLF 329
Cdd:cd14533  106 LRALC--SSAPDQPNWLSNLESTKWLHHLSGLLKAALLVVNAVDEEGRPVLVHCSDGWDRTPQIVALAELMLDPYYRTIE 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 578800472 330 GFQSLVQREWVAAGHPFLTRLGGTGASEEA----PVFLLFLDCVWQ 371
Cdd:cd14533  184 GFQVLVEREWLDFGHKFADRCGHGVNSEDInercPVFLQWLDCVHQ 229
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 142-375 2.20e-15

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: 77.27  E-value: 2.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 142 WRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHP-GGSDLLRCGGFY--------------TA 206
Cdd:cd14589    1 FRITAVNRMYSLCRSYPGLLVVPQSVQDSSLQKVARCYRHNRLPVVCWKNSkTKAVLLRSGGFHgkgvvglfksqnphSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 207 SDPNKEDIRAVEL--MLQAGHSDVVLVDTMDELPSLADVQL-------------AHLR---------------------- 249
Cdd:cd14589   81 APASSESSSSIEQekYLQALLNAISVHQKMNGNSTLLQSQLlkrqaalyifgekSQLRgfkldfalncefvpvefhdirq 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 250 --------LRAlCLPDS--SVAEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGdRDLNGLLSSLVQL 319
Cdd:cd14589  161 vkasfkklMRA-CVPSTipTDSEVTFLKALGESEWFLQLHRIMQLAVVISELLESGSSVMVCLEDG-WDITTQVVSLVQL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578800472 320 LSAPEARTLFGFQSLVQREWVAAGHPFLTRLGGTGASEE---APVFLLFLDCVWQLLQQ 375
Cdd:cd14589  239 LSDPFYRTLEGFQMLVEKEWLSFGHKFSQRSNLTPNSQGsgfAPIFLQFLDCVHQIHNQ 297
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 142-371 5.29e-15

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: 76.21  E-value: 5.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 142 WRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHPG-GSDLLRCG-------GFYTASD----- 208
Cdd:cd14586    8 WRISNINEKYKLCGSYPQELIVPAWITDKELESVASFRSWKRIPAVVYRHQSnGAVIARCGqpevswwGWRNADDehlvq 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 209 --------------------------PNKEDIRAVEL---MLQAGHSD--------VVLVDTMDELPSLAD--------- 242
Cdd:cd14586   88 svakacasdssscksvlmtgncsrdfPNGGDLSDVEFdssMSNASGVEslaiqpqkLLILDARSYAAAVANrakgggcec 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 243 -------------------VQLAHLRLRALC--LPDSSvaedKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVIL 301
Cdd:cd14586  168 peyypncevvfmgmanihsIRKSFQSLRLLCtqMPDPA----NWLSALESTKWLQHLSMLLKSALLVVHAVDRDQRPVLV 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578800472 302 QERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGHPFLTRLG-GTGA---SEEAPVFLLFLDCVWQ 371
Cdd:cd14586  244 HCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRCGhGENSddlNERCPVFLQWLDCVHQ 317
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 142-375 1.55e-14

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: 74.62  E-value: 1.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 142 WRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHP-GGSDLLRCGGFY-------------TAS 207
Cdd:cd14588    1 FRISTVNRMYAVCRSYPGLLIVPQSIQDNTIQRISRCYRQNRFPVVCWRNSrTKAVLLRSGGLHgkgvvglfksqnaPAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 208 DPNKEDIRAVEL--MLQA------GHSDVVLVDTMD-------------------------------ELPSLADVQLAHL 248
Cdd:cd14588   81 GQSQTDSTSLEQekYLQAvinsmpRYADASGRNTLSgfraalyiigdksqlkgvkqdplqqwevvpiEVFDVRQVKASFK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578800472 249 RLRALCLPD--SSVAEDKWLSALEGTRWLDYVRACLRkasdISVLVTSRV---RSVILQERGDRDLNGLLSSLVQLLSAP 323
Cdd:cd14588  161 KLMKACVPScpSTDPSQTYLRTLEESEWLSQLHKLLQ----VSVLVVELLdsgSSVLVSLEDGWDITTQVVSLVQLLSDP 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578800472 324 EARTLFGFQSLVQREWVAAGHPFLTRLGGTGASEE---APVFLLFLDCVWQLLQQ 375
Cdd:cd14588  237 YYRTIEGFRLLVEKEWLSFGHRFSHRGAQTLASQSsgfTPVFLQFLDCVHQIHLQ 291
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
 323-371 2.29e-10

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: 60.92  E-value: 2.29e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 578800472 323 PEARTLFGFQSLVQREWVAAGHPFLTRLGgtgASEEAPVFLLFLDCVWQ 371
Cdd:cd17666  184 PYYRTLEGFMVLVEKDWLSFGHRFAERSG---HKETSPVFHQFLDCVYQ 229
PH-GRAM_MTMR10 cd13346
Myotubularian (MTM) related 10 protein (MTMR10) Pleckstrin Homology-Glucosyltransferases, ...
 20-89 9.45e-04

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: 40.68  E-value: 9.45e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578800472  20 LNSEYDFALVNIGRLEAVSGLSRVQ-LLRPGSLHKFIPEEILIHGRDFRLLRVGFEAGGLEpQAFQVTMAI 89
Cdd:cd13346   74 LLGEHDVPLTCIEQIVTVNDTKRKQkVLGPNQKLKFNPTELIIYCKDFRIVRFRFDEAGPE-SAKKVCLAI 143
 
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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