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Conserved domains on  [gi|1370451681|ref|XP_024308346|]
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myotubularin-related protein 11 isoform X1 [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 ...
 218-408 2.14e-108

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: 326.02  E-value: 2.14e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 218 GRGPRLSWHHPGGSDLLRCGGFYTASDPNKEDIRAVELMLQAGHSDVVLVDTMDELPSLADVQLAHLRLRALCLPDSSVA 297
Cdd:cd14595     1 GRIPRWCWHHPGGSDLLRMAGFYTNSDPEKEDIRSVELLLQAGHSQCVIVDTSEELPSPADIQLAYLKLRTLCLPDISVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 298 ED--KWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREW 375
Cdd:cd14595    81 VSdeKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEW 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1370451681 376 VAAGHPFLTRLGGTG--ASEEAPVFLLFLDCVWQL 408
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 ...
 48-124 2.18e-35

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: 129.90  E-value: 2.18e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451681  48 PDASQDTPLNSEYDFALVNIGRLEAVSGLSRVQLLRPGSLHKFIPEEILIHGRDFRLLRVGFEAGGLEPQAFQVTMA 124
Cdd:cd15790    47 DENDHDTVLNSEHDIALPSIDRVVAVQGPTTMKAVTASSGLKFIPEELVIYCRDFRLLRFQFEQSTLEPQAFQITTA 123
3-PAP super family cl13953
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
 515-642 6.98e-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: 6.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 515 SFMVPGPPSSVwlfSRGalTPLNQLCPWRDSPSLLAVSSRWLPRPaiSSESlaDQEWGLPSHWGACPLPPGLL-LPGYLG 593
Cdd:pfam12578   8 SSTLRGPPPSL---KNG--LFRDEEDLLRRNSLLLRLKPDCPLHR--SSDS--NDSEQFFRDWFSKPADLHGLlLPLLSG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370451681 594 PQIRLWRRCYLRGRPEVQMGLSAP-----TISGLQDELSHLQELLRKWTPRISP 642
Cdd:pfam12578  79 PHIKLWKLCYLRWVPEAQINHGGPitafhKLSLLADEVEALQRLLRQYRGGPSE 132
 
Name Accession Description Interval E-value
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 218-408 2.14e-108

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: 326.02  E-value: 2.14e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 218 GRGPRLSWHHPGGSDLLRCGGFYTASDPNKEDIRAVELMLQAGHSDVVLVDTMDELPSLADVQLAHLRLRALCLPDSSVA 297
Cdd:cd14595     1 GRIPRWCWHHPGGSDLLRMAGFYTNSDPEKEDIRSVELLLQAGHSQCVIVDTSEELPSPADIQLAYLKLRTLCLPDISVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 298 ED--KWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREW 375
Cdd:cd14595    81 VSdeKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEW 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1370451681 376 VAAGHPFLTRLGGTG--ASEEAPVFLLFLDCVWQL 408
Cdd:cd14595   161 VVAGHPFLQRLNLTResDKEESPVFLLFLDCVWQL 195
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 165-430 1.32e-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: 176.13  E-value: 1.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 165 DWETERKKQ---AARGWRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHPG-GSDLLRCG--- 237
Cdd:pfam06602   9 DPEAEFARQglpSKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKEnGAVITRSSqpl 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 238 -GFytASDPNKEDiravELMLQA--------GHSDVVLVDTMDELPSLA---------------DVQLAHL--------- 284
Cdd:pfam06602  89 vGL--NGKRSIED----EKLLQAifkssnpySAKKLYIVDARPKLNAMAnrakgggyenednypNCKKIFLgienihvmr 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 285 ----RLRALCLpDSSVAEDKWLSALEGTRWLDYVRACLRKASDI---------SVLV--------TSRVRS---VILqer 340
Cdd:pfam06602 163 dslnKLVEACN-DRSPSMDKWLSRLESSGWLKHIKAILDGACLIaqavdlegsSVLVhcsdgwdrTAQLTSlaqLLL--- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 341 gdrDlngllsslvqllsaPEARTLFGFQSLVQREWVAAGHPFLTRLG----GTGASEEAPVFLLFLDCVWQLLQQFPADF 416
Cdd:pfam06602 239 ---D--------------PYYRTIEGFQVLIEKEWLSFGHKFADRCGhlagFTDSKERSPVFLQFLDCVWQLLRQFPCAF 301

                         330
                  ....*....|....
gi 1370451681 417 EFSEFFLLALHDSV 430
Cdd:pfam06602 302 EFNERFLIRLLYHL 315
PH-GRAM_MTMR11 cd15790
Myotubularian (MTM) related 11 protein (MTMR11) Pleckstrin Homology-Glucosyltransferases, ...
 48-124 2.18e-35

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: 129.90  E-value: 2.18e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451681  48 PDASQDTPLNSEYDFALVNIGRLEAVSGLSRVQLLRPGSLHKFIPEEILIHGRDFRLLRVGFEAGGLEPQAFQVTMA 124
Cdd:cd15790    47 DENDHDTVLNSEHDIALPSIDRVVAVQGPTTMKAVTASSGLKFIPEELVIYCRDFRLLRFQFEQSTLEPQAFQITTA 123
3-PAP pfam12578
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
 515-642 6.98e-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: 6.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 515 SFMVPGPPSSVwlfSRGalTPLNQLCPWRDSPSLLAVSSRWLPRPaiSSESlaDQEWGLPSHWGACPLPPGLL-LPGYLG 593
Cdd:pfam12578   8 SSTLRGPPPSL---KNG--LFRDEEDLLRRNSLLLRLKPDCPLHR--SSDS--NDSEQFFRDWFSKPADLHGLlLPLLSG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370451681 594 PQIRLWRRCYLRGRPEVQMGLSAP-----TISGLQDELSHLQELLRKWTPRISP 642
Cdd:pfam12578  79 PHIKLWKLCYLRWVPEAQINHGGPitafhKLSLLADEVEALQRLLRQYRGGPSE 132
 
Name Accession Description Interval E-value
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 218-408 2.14e-108

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: 326.02  E-value: 2.14e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 218 GRGPRLSWHHPGGSDLLRCGGFYTASDPNKEDIRAVELMLQAGHSDVVLVDTMDELPSLADVQLAHLRLRALCLPDSSVA 297
Cdd:cd14595     1 GRIPRWCWHHPGGSDLLRMAGFYTNSDPEKEDIRSVELLLQAGHSQCVIVDTSEELPSPADIQLAYLKLRTLCLPDISVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 298 ED--KWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREW 375
Cdd:cd14595    81 VSdeKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEW 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1370451681 376 VAAGHPFLTRLGGTG--ASEEAPVFLLFLDCVWQL 408
Cdd:cd14595   161 VVAGHPFLQRLNLTResDKEESPVFLLFLDCVWQL 195
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 218-407 2.49e-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: 240.32  E-value: 2.49e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 218 GRGPRLSWHHPGGSDLLRCGGFYtasdpNKEDIRAVELMLQ-------AGHSDVVLVDTMDELPSLADVQLAHLRLRALC 290
Cdd:cd14537     1 GRPPVWCWSHPNGAALVRMAELL-----PTITDRTQENKMLeairkshPNLKKPKVIDLDKLLPSLQDVQAAYLKLRELC 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 291 LPDSSVAED----KWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFG 366
Cdd:cd14537    76 TPDSSEQFWvqdsKWYSLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQESDGRDLSCVVSSLVQLLLDPHFRTITG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1370451681 367 FQSLVQREWVAAGHPFLTRLGGT----GASEEAPVFLLFLDCVWQ 407
Cdd:cd14537   156 FQSLIQKEWVALGHPFCDRLGHVkpnkTESEESPVFLLFLDCVWQ 200
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 165-430 1.32e-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: 176.13  E-value: 1.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 165 DWETERKKQ---AARGWRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHPG-GSDLLRCG--- 237
Cdd:pfam06602   9 DPEAEFARQglpSKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKEnGAVITRSSqpl 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 238 -GFytASDPNKEDiravELMLQA--------GHSDVVLVDTMDELPSLA---------------DVQLAHL--------- 284
Cdd:pfam06602  89 vGL--NGKRSIED----EKLLQAifkssnpySAKKLYIVDARPKLNAMAnrakgggyenednypNCKKIFLgienihvmr 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 285 ----RLRALCLpDSSVAEDKWLSALEGTRWLDYVRACLRKASDI---------SVLV--------TSRVRS---VILqer 340
Cdd:pfam06602 163 dslnKLVEACN-DRSPSMDKWLSRLESSGWLKHIKAILDGACLIaqavdlegsSVLVhcsdgwdrTAQLTSlaqLLL--- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 341 gdrDlngllsslvqllsaPEARTLFGFQSLVQREWVAAGHPFLTRLG----GTGASEEAPVFLLFLDCVWQLLQQFPADF 416
Cdd:pfam06602 239 ---D--------------PYYRTIEGFQVLIEKEWLSFGHKFADRCGhlagFTDSKERSPVFLQFLDCVWQLLRQFPCAF 301

                         330
                  ....*....|....
gi 1370451681 417 EFSEFFLLALHDSV 430
Cdd:pfam06602 302 EFNERFLIRLLYHL 315
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 218-407 5.18e-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: 156.59  E-value: 5.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 218 GRGPRLSWHHPGGSDLLRCGGFYTASDPNKEDIRAVELMLQAG--HSDVVLVDTMDELPSLADVQLAHLRLRALCLPDS- 294
Cdd:cd14593     1 RRIPLWCWNHPNGSALVRMANIKDLLQQRKIDQRICNAITRSHplRSDVYKSDLDKTLPNIQEIQAAFVKLKQLCVNEPf 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 295 SVAEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQRE 374
Cdd:cd14593    81 EETEEKWLSSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLVQVMLDPYFRTITGFQSLIQKE 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1370451681 375 WVAAGHPFLTRLGGTGAS--EEAPVFLLFLDCVWQ 407
Cdd:cd14593   161 WVMAGYRFLDRCNHLKKSskKESPLFLLFLDCVWQ 195
PH-GRAM_MTMR11 cd15790
Myotubularian (MTM) related 11 protein (MTMR11) Pleckstrin Homology-Glucosyltransferases, ...
 48-124 2.18e-35

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: 129.90  E-value: 2.18e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451681  48 PDASQDTPLNSEYDFALVNIGRLEAVSGLSRVQLLRPGSLHKFIPEEILIHGRDFRLLRVGFEAGGLEPQAFQVTMA 124
Cdd:cd15790    47 DENDHDTVLNSEHDIALPSIDRVVAVQGPTTMKAVTASSGLKFIPEELVIYCRDFRLLRFQFEQSTLEPQAFQITTA 123
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 221-408 5.73e-35

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: 131.50  E-value: 5.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 221 PRLSWHHPGGSDLLRCGGF-----YTASDPNKEDIRAVELMLQAGHSDVVLVDTMDE-LPSLADVQLAHLRLRALCLPDS 294
Cdd:cd14594     4 PIWCWSCHNGCALLKMSALpkeqdDVALQDQKSFLDRIYKTLSRPPYESVKTEDLSAsLPSLQEIQTAYNRFKQLFLIDN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 295 SV----AEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSL 370
Cdd:cd14594    84 STdfwdTDVKWFSSLESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQSL 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370451681 371 VQREWVAAGHPFLTRLGGTGAS--EEAPVFLLFLDCVWQL 408
Cdd:cd14594   164 IQKEWVMGGHCFLDRCNHLRQNdkEEVPVFLLFLDCVWQL 203
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 178-430 3.06e-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: 3.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 178 WRVSTVNERFDVATSLPRYFWVPnRILDSEVRRAFGHFH-QGRGPRLSWHHPGG-SDLLRC----GGFYTASDpnkEDIR 251
Cdd:cd14532    15 WTLSDINKDYELCDTYPRELFVP-TSASTPVLVGSSKFRsKGRLPVLSYLHKDNqAAICRCsqplSGFSARCV---EDEQ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 252 AVELMLQAG-HSDVV-LVDTMDELPSLA----------------------DVQLAH-LR------LRALCLPDSSVaeDK 300
Cdd:cd14532    91 LLQAIRKANpNSKFMyVVDTRPKINAMAnkaagkgyenednysnikfqffGIENIHvMRsslqklLEVCELKNPSM--SA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 301 WLSALEGTRWLDYVRACLrkasDISVLVTSRVR---SVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVA 377
Cdd:cd14532   169 FLSGLESSGWLKHIKAVM----DTSVFIAKAVSegaSVLVHCSDGWDRTAQTCSLASLLLDPYYRTIKGFQVLIEKEWLS 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370451681 378 AGHPFLTRLG--GTGASEEAPVFLLFLDCVWQLLQQFPADFEFSEFFLLALHDSV 430
Cdd:cd14532   245 FGHKFTDRCGhlQGDAKEVSPVFTQFLDCVWQLMQQFPRAFEFNERFLLTLHDHV 299
PH-GRAM_MTMR10-like cd13212
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 23-124 1.50e-33

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: 124.65  E-value: 1.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681  23 SQRWGLSRKIGCRSPGVVSLAVAWPP--DASQDTPLNSEYDFALVNIGRLEAVSGLSRVQLLRPGSLHKFIPEEILIHGR 100
Cdd:cd13212    21 SSQPELSGTLICTNFKITFQPDDWQWldNTQQKNPLNGEYDFALVCIGQIEAVSDLKRVQLLRPGSLLKFIPEELIIHCK 100

                          90       100
                  ....*....|....*....|....*
gi 1370451681 101 DFRLLRVGFEA-GGLEPQAFQVTMA 124
Cdd:cd13212   101 DFRVLRFGFEAtGGEEPKAFQVTIA 125
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
 218-428 4.64e-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: 116.01  E-value: 4.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 218 GRGPRLSWHHP-GGSDLLRCggfytaSDP--------NKEDIRAVELMLQA-GHSDVVLVdtMDELPS------------ 275
Cdd:cd14535     1 NRIPVLSWIHPeSQATITRC------SQPlvgvsgkrSKDDEKYLQLIMDAnAQSHKLFI--MDARPSvnavankakggg 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 276 -------------LADVQLAHL------RLRALCLPdsSVAEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVI 336
Cdd:cd14535    73 yesedayqnaelvFLDIHNIHVmreslrKLKDICFP--NIDDSHWLSNLESTHWLEHIKLILAGAVRIADKVESGKTSVV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 337 LQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGHPFLTRLG----GTGASEEAPVFLLFLDCVWQLLQQF 412
Cdd:cd14535   151 VHCSDGWDRTAQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGhgdkNHSDADRSPVFLQFIDCVWQMTRQF 230

                         250
                  ....*....|....*.
gi 1370451681 413 PADFEFSEFFLLALHD 428
Cdd:cd14535   231 PNAFEFNEHFLITILD 246
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 205-428 4.26e-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: 4.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 205 DSEVRRAFGHFHQGRGPRLSWHHP-GGSDLLRCggfytaSDP--------NKEDIRAVELMLQA-GHSDVVLVdtMDELP 274
Cdd:cd14590     1 DEELKRVASFRSRGRIPVLSWIHPeSQATITRC------SQPmvgvsgkrSKEDEKYLQAIMDSnAQSHKIFI--FDARP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 275 SL-------------------------ADVQLAHL------RLRALCLPDssVAEDKWLSALEGTRWLDYVRACLRKASD 323
Cdd:cd14590    73 SVnavankakgggyesedayqnaelvfLDIHNIHVmreslrKLKEIVYPN--IEESHWLSNLESTHWLEHIKLILAGALR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 324 ISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGHPFLTRLG----GTGASEEAPVFL 399
Cdd:cd14590   151 IADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGhgdkNHADADRSPVFL 230

                         250       260
                  ....*....|....*....|....*....
gi 1370451681 400 LFLDCVWQLLQQFPADFEFSEFFLLALHD 428
Cdd:cd14590   231 QFIDCVWQMTRQFPTAFEFNEYFLITILD 259
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 218-428 1.41e-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: 111.99  E-value: 1.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 218 GRGPRLSWHHP-GGSDLLRCGG-FYTASDPN-KEDIRAVELMLQAGHSDVVLVDTMDELPSLAD---------------- 278
Cdd:cd14592     1 GRVPVLSWIHPeSQATITRCSQpLVGPNDKRcKEDEKYLQTIMDANAQSHKLIIFDARQNSVADtnktkgggyesesayp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 279 -VQLAHL-------------RLRALCLPdsSVAEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRD 344
Cdd:cd14592    81 nAELVFLeihnihvmreslrKLKEIVYP--SIDEARWLSNVDGTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGWD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 345 LNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGHPFLTRLGGTGA----SEEAPVFLLFLDCVWQLLQQFPADFEFSE 420
Cdd:cd14592   159 RTAQLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGHGDDnhadADRSPIFLQFIDCVWQMTRQFPSAFEFNE 238


                  ....*...
gi 1370451681 421 FFLLALHD 428
Cdd:cd14592   239 LFLITILD 246
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
 218-407 2.48e-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: 110.33  E-value: 2.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 218 GRGPRLSWHHP-GGSDLLRCG----GFYTASdpNKEDIRAVELMLQAGHSDVVLVdTMDELPSLA--------------- 277
Cdd:cd14507     1 GRIPVLSWRHPrNGAVICRSSqplvGLTGSR--SKEDEKLLNAIRKASPSSKKLY-IVDARPKLNavanrakgggyente 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 278 ---DVQLAHL-------------RLRALCLPDSSVaEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQ-ER 340
Cdd:cd14507    78 yypNCELEFLnienihamrdslnKLRDACLSPNDE-ESNWLSALESSGWLEHIRLILKGAVRVADLLEKEGTSVLVHcSD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 341 G-DR------------DlngllsslvqllsaPEARTLFGFQSLVQREWVAAGHPFLTRLGGTGA----SEEAPVFLLFLD 403
Cdd:cd14507   157 GwDRtsqltslaqlllD--------------PYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDKnssdEERSPIFLQFLD 222


                  ....
gi 1370451681 404 CVWQ 407
Cdd:cd14507   223 CVWQ 226
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
 219-428 5.50e-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: 5.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 219 RGPRLSWHHP-GGSDLLRCggfytaSDP--------NKEDIRAVELMLQAGH--SDVVLVDTMDELPSLA---------- 277
Cdd:cd14591     2 RIPVLSWIHPeNQAVIMRC------SQPlvgmsgkrNKDDEKYLDIIREANGqtSKLTIYDARPSVNAVAnkatgggyeg 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 278 ------------DVQLAHL------RLRALCLPDssVAEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQE 339
Cdd:cd14591    76 ddayqnaelvflDIHNIHVmreslkKLKDIVYPN--VEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHC 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 340 RGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGHPFLTRLG----GTGASEEAPVFLLFLDCVWQLLQQFPAD 415
Cdd:cd14591   154 SDGWDRTAQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGhgdkNHADADRSPIFLQFIDCVWQMSKQFPTA 233

                         250
                  ....*....|...
gi 1370451681 416 FEFSEFFLLALHD 428
Cdd:cd14591   234 FEFNEQFLITILD 246
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 178-430 8.90e-24

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: 102.26  E-value: 8.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 178 WRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHP-GGSDLLRCG----GFYTASdpnKEDira 252
Cdd:cd14584    21 WEITDANKNYEICSTYPPELVVPKSASKATVVGSSKFRSRGRFPVLSYLYKeNNAAICRCSqplsGFSARC---VED--- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 253 vELMLQA------GHSDVVLVDTMDELPSLAD----------------------VQLAHL------RLRALCLPDSSVAE 298
Cdd:cd14584    95 -EQMLQAiskanpGSPFMYVVDTRPKLNAMANraagkgyenednysnirfqfigIENIHVmrsslqKLLEVCEMKSPSMS 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 299 DkWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAA 378
Cdd:cd14584   174 D-FLTGLENSGWLRHIKAVMDAGVFLAKAVKEEKASVLVHCSDGWDRTAQVCSLASLLLDPFYRTIKGLMVLIEKEWISM 252

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370451681 379 GHPFLTRLG--GTGASEEAPVFLLFLDCVWQLLQQFPADFEFSEFFLLALHDSV 430
Cdd:cd14584   253 GHKFSQRCGhlDGDPKEVSPVFTQFLECVWQLMEQFPCAFEFNEHFLLEIHDHV 306
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 178-411 5.91e-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: 5.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 178 WRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHPG-GSDLLRCGGFYTAS------------- 243
Cdd:cd14534     1 FRISTANRDYSICRSYPALVVVPQSVSDESLRKVARCYRQGRFPVVTWRHPRtKALLLRSGGFHGKGvmgmlksantsts 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 244 ---DPNKEDIRAVELM--LQA---------GHSDVVLVDT-------MDELPSLADVQLAHLRLRALCLPDSSVAEDK-- 300
Cdd:cd14534    81 sptVSSSETSSSLEQEkyLSAlvlyvlgekSQMKGVKAESdpkcefiPVEYPEVRQVKASFKKLLRACVPSSAPTEPEqs 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 301 WLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGH 380
Cdd:cd14534   161 FLKAVEDSEWLQQLQCLMQLSGAVVDLLDVQGSSVLLCLEDGWDVTTQVSSLSQLLLDPYYRTLEGFRVLVEKEWLAFGH 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370451681 381 PFLTRLGGTGASEE---APVFLLFLDCVWQLLQQ 411
Cdd:cd14534   241 RFSHRSNLTAASQSsgfAPVFLQFLDAVHQIHRQ 274
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 178-430 1.29e-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: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 178 WRVSTVNERFDVATSLPRYFWVPnRILDSEVRRAFGHFH-QGRGPRLSWHHPGG-SDLLRCG----GFytaSDPNKEDIR 251
Cdd:cd14585    15 WQLSDVNRDYKICDTYPRDLYVP-ITASKPIIVGSSKFRsKGRFPVLSYYHQEKkAAICRCSqplsGF---SARCLEDEH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 252 AVELMLQAGHSD--VVLVDTMDELPSLAD---------------------------VQLAHLRLRALCLPDSSVAEDKWL 302
Cdd:cd14585    91 MLQAISKANPNNryMYVMDTRPKLNAMANraagkgyenednysnirfqfvgienihVMRSSLQKLLEVCGTKALSVNDFL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 303 SALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGHPF 382
Cdd:cd14585   171 SGLESSGWLRHIKAVLDAAVFLAKAVAVEGASVLVHCSDGWDRTAQVCSLGSLLLDPYYRTIKGFMVLIEKDWISFGHKF 250

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370451681 383 LTRLG--GTGASEEAPVFLLFLDCVWQLLQQFPADFEFSEFFLLALHDSV 430
Cdd:cd14585   251 SDRCGqlDGDPKEISPVFTQFLECVWQLTEQFPRAFEFSEAFLLQIHEHI 300
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 293-407 5.05e-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: 5.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 293 DSSVAEDKWLSALEGTRWLDYVR-----ACL----------------RKASDISVLVTSRVRsVILQergdrdlngllss 351
Cdd:cd14536   105 DQGHSMDKWLSKLESSNWLSHVKeilttACLvaqcidregasvlvhgSEGMDSTLQVTSLAQ-IILD------------- 170

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370451681 352 lvqllsaPEARTLFGFQSLVQREWVAAGHPFLTR-----LGGTGASEEAPVFLLFLDCVWQ 407
Cdd:cd14536   171 -------PDCRTIRGFEALIEREWLQAGHPFQSRcaksaYSNSKQKFESPVFLLFLDCVWQ 224
3-PAP pfam12578
Myotubularin-associated protein; This domain family is found in eukaryotes, and is typically ...
 515-642 6.98e-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: 6.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 515 SFMVPGPPSSVwlfSRGalTPLNQLCPWRDSPSLLAVSSRWLPRPaiSSESlaDQEWGLPSHWGACPLPPGLL-LPGYLG 593
Cdd:pfam12578   8 SSTLRGPPPSL---KNG--LFRDEEDLLRRNSLLLRLKPDCPLHR--SSDS--NDSEQFFRDWFSKPADLHGLlLPLLSG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370451681 594 PQIRLWRRCYLRGRPEVQMGLSAP-----TISGLQDELSHLQELLRKWTPRISP 642
Cdd:pfam12578  79 PHIKLWKLCYLRWVPEAQINHGGPitafhKLSLLADEVEALQRLLRQYRGGPSE 132
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 178-430 1.91e-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: 1.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 178 WRVSTVNERFDVATSLPRYFWVPNR-----ILDSEVRRAfghfhQGRGPRLSWH-HPGGSDLLRCG----GFytaSDPNK 247
Cdd:cd14583    15 WQVSDVNRDYRVCDTYPTELYVPKSatapiIVGSSKFRS-----RGRFPVLSYYcKDNNASICRSSqplsGF---SARCL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 248 EDiravELMLQA------GHSDVVLVDTMDELPSLAD----------------------VQLAHL------RLRALC-LP 292
Cdd:cd14583    87 ED----EQMLQAirkanpGSDFMYVVDTRPKLNAMANraagkgyenednysnikfqfigIENIHVmrnslqKMLEVCeLR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 293 DSSVAEDKWlsALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQ 372
Cdd:cd14583   163 SPSMGDFLW--GLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 373 REWVAAGHPFLTRLGGTG--ASEEAPVFLLFLDCVWQLLQQFPADFEFSEFFLLALHDSV 430
Cdd:cd14583   241 KDWVSFGHKFNHRYGHLDgdPKEVSPVIDQFIECVWQLMEQFPCAFEFNERFLIHIHHHI 300
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 286-407 1.45e-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: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 286 LRALC--LPDSSvaedKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEART 363
Cdd:cd14587   185 LRAVCsqMPDPG----NWLSALESTKWLQHLSVMLKAAVLVASAVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRT 260

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370451681 364 LFGFQSLVQREWVAAGHPFLTRLG----GTGASEEAPVFLLFLDCVWQ 407
Cdd:cd14587   261 IEGFQVLVETDWLDFGHKFGDRCGhqenVEDQNEQCPVFLQWLDCVHQ 308
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 286-407 2.70e-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: 78.60  E-value: 2.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 286 LRALClpDSSVAEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLF 365
Cdd:cd14533   106 LRALC--SSAPDQPNWLSNLESTKWLHHLSGLLKAALLVVNAVDEEGRPVLVHCSDGWDRTPQIVALAELMLDPYYRTIE 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1370451681 366 GFQSLVQREWVAAGHPFLTRLGGTGASEEA----PVFLLFLDCVWQ 407
Cdd:cd14533   184 GFQVLVEREWLDFGHKFADRCGHGVNSEDInercPVFLQWLDCVHQ 229
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 178-411 1.94e-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: 77.65  E-value: 1.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 178 WRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHP-GGSDLLRCGGFY--------------TA 242
Cdd:cd14589     1 FRITAVNRMYSLCRSYPGLLVVPQSVQDSSLQKVARCYRHNRLPVVCWKNSkTKAVLLRSGGFHgkgvvglfksqnphSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 243 SDPNKEDIRAVEL--MLQAGHSDVVLVDTMDELPSLADVQL-------------AHLR---------------------- 285
Cdd:cd14589    81 APASSESSSSIEQekYLQALLNAISVHQKMNGNSTLLQSQLlkrqaalyifgekSQLRgfkldfalncefvpvefhdirq 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 286 --------LRAlCLPDS--SVAEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGdRDLNGLLSSLVQL 355
Cdd:cd14589   161 vkasfkklMRA-CVPSTipTDSEVTFLKALGESEWFLQLHRIMQLAVVISELLESGSSVMVCLEDG-WDITTQVVSLVQL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451681 356 LSAPEARTLFGFQSLVQREWVAAGHPFLTRLGGTGASEE---APVFLLFLDCVWQLLQQ 411
Cdd:cd14589   239 LSDPFYRTLEGFQMLVEKEWLSFGHKFSQRSNLTPNSQGsgfAPIFLQFLDCVHQIHNQ 297
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 178-407 5.48e-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: 76.60  E-value: 5.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 178 WRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHPG-GSDLLRCG-------GFYTASD----- 244
Cdd:cd14586     8 WRISNINEKYKLCGSYPQELIVPAWITDKELESVASFRSWKRIPAVVYRHQSnGAVIARCGqpevswwGWRNADDehlvq 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 245 --------------------------PNKEDIRAVEL---MLQAGHSD--------VVLVDTMDELPSLAD--------- 278
Cdd:cd14586    88 svakacasdssscksvlmtgncsrdfPNGGDLSDVEFdssMSNASGVEslaiqpqkLLILDARSYAAAVANrakgggcec 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 279 -------------------VQLAHLRLRALC--LPDSSvaedKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVIL 337
Cdd:cd14586   168 peyypncevvfmgmanihsIRKSFQSLRLLCtqMPDPA----NWLSALESTKWLQHLSMLLKSALLVVHAVDRDQRPVLV 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370451681 338 QERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGHPFLTRLG-GTGA---SEEAPVFLLFLDCVWQ 407
Cdd:cd14586   244 HCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRCGhGENSddlNERCPVFLQWLDCVHQ 317
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 178-411 1.66e-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: 1.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 178 WRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHP-GGSDLLRCGGFY-------------TAS 243
Cdd:cd14588     1 FRISTVNRMYAVCRSYPGLLIVPQSIQDNTIQRISRCYRQNRFPVVCWRNSrTKAVLLRSGGLHgkgvvglfksqnaPAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 244 DPNKEDIRAVEL--MLQA------GHSDVVLVDTMD-------------------------------ELPSLADVQLAHL 284
Cdd:cd14588    81 GQSQTDSTSLEQekYLQAvinsmpRYADASGRNTLSgfraalyiigdksqlkgvkqdplqqwevvpiEVFDVRQVKASFK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451681 285 RLRALCLPD--SSVAEDKWLSALEGTRWLDYVRACLRkasdISVLVTSRV---RSVILQERGDRDLNGLLSSLVQLLSAP 359
Cdd:cd14588   161 KLMKACVPScpSTDPSQTYLRTLEESEWLSQLHKLLQ----VSVLVVELLdsgSSVLVSLEDGWDITTQVVSLVQLLSDP 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370451681 360 EARTLFGFQSLVQREWVAAGHPFLTRLGGTGASEE---APVFLLFLDCVWQLLQQ 411
Cdd:cd14588   237 YYRTIEGFRLLVEKEWLSFGHRFSHRGAQTLASQSsgfTPVFLQFLDCVHQIHLQ 291
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
 359-407 2.46e-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: 2.46e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370451681 359 PEARTLFGFQSLVQREWVAAGHPFLTRLGgtgASEEAPVFLLFLDCVWQ 407
Cdd:cd17666   184 PYYRTLEGFMVLVEKDWLSFGHRFAERSG---HKETSPVFHQFLDCVYQ 229
PH-GRAM_MTMR10 cd13346
Myotubularian (MTM) related 10 protein (MTMR10) Pleckstrin Homology-Glucosyltransferases, ...
 56-125 1.01e-03

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: 1.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370451681  56 LNSEYDFALVNIGRLEAVSGLSRVQ-LLRPGSLHKFIPEEILIHGRDFRLLRVGFEAGGLEpQAFQVTMAI 125
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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