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Conserved domains on  [gi|8393794|ref|NP_058681.1|]
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myotubularin-related protein 1

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List of domain hits

Name Accession Description Interval E-value
PH-GRAM_MTMR1 cd13358
Myotubularian related 1 protein (MTMR1) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
111-210 7.32e-68

Myotubularian related 1 protein (MTMR1) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR1 is a member of the myotubularin protein phosphatase gene family. MTMR1 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. MTMR1 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal PDZ 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: 270165  Cd Length: 100  Bit Score: 218.62  E-value: 7.32e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794  111 KAIVKDVIYICPFMGAVSGTLTVTDFKMYFKNVERDPHFVLDVPLGVISRVEKIGAQSHGDNSCGIEIVCKDMRNLRLAY 190
Cdd:cd13358   1 KAIVKDVMYICPFMGAVSGTLTVTDFKMYFKNVERDPPFILDVPLGVISRVEKIGVQSHGDNSCGIEIVCKDMRNLRLAY 80
                        90       100
                ....*....|....*....|
gi 8393794  191 KQEEQRKLGIFENLNKHAFP 210
Cdd:cd13358  81 KQEEQSKLEIFENLNKHAFP 100
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
217-556 0e+00

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: 253817  Cd Length: 347  Bit Score: 608.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794    217 LFAFNYKEKFPVN----GWKVYDPVSEYKRQGLPNE-SWKISKINSNYEFCDTYPAIIVVPTSVKDDDLSKVAAFRAKGR 291
Cdd:pfam06602   2 LFAFSYNPKFSELerldGWKIFDPEREYKRLGLPNSnAWRISSVNENYEICPSYPAKLIVPKSISDDELKKVAKFRSGGR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794    292 VPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYLQTIMDANAQSHKLTIFDARQNSVADTNKAKGGGYENESAYPNA 371
Cdd:pfam06602  82 FPVLSWRHKENGAVIVRCSQPLVGIMGKRCKEDEKLLAAIRKSNPQSKKLYIVDARPRLNALANKAKGGGYENEDNYPNA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794    372 ELIFLEIHNIHVMRESLRKLKEI-VYPSIDESHWLSNVDGTHWLEYIRVLLAGAVRIADKIESGKTSVVIHCSDGWDRTS 450
Cdd:pfam06602 162 ELIFLGIPNIHVMRESLQKLREAcVTNEPDESSWLSSLESSGWLQHISAILAGAALIADAVDSEGSSVLVHCSDGWDRTA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794    451 QLTSLAMLMLDSYYRTIKGFEALIEKEWISFGHRFALRVGHGDDNHADADRSPIFLQFIDCVWQMTRQFPSAFEFNELFL 530
Cdd:pfam06602 242 QVTSLAQLLLDPYYRTIEGFQVLVEKEWLSFGHKFADRCGHLNNNGDSKERSPVFLQFLDCVWQLMRQFPCAFEFNEFFL 321
                         330       340
                  ....*....|....*....|....*.
gi 8393794    531 ITILDHLYSCLFGTFLCNCEQQRIKE 556
Cdd:pfam06602 322 IFLADHLYSCQFGTFLCNSEKEREEL 347
 
Name Accession Description Interval E-value
PH-GRAM_MTMR1 cd13358
Myotubularian related 1 protein (MTMR1) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
111-210 7.32e-68

Myotubularian related 1 protein (MTMR1) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR1 is a member of the myotubularin protein phosphatase gene family. MTMR1 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. MTMR1 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal PDZ 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: 270165  Cd Length: 100  Bit Score: 218.62  E-value: 7.32e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794  111 KAIVKDVIYICPFMGAVSGTLTVTDFKMYFKNVERDPHFVLDVPLGVISRVEKIGAQSHGDNSCGIEIVCKDMRNLRLAY 190
Cdd:cd13358   1 KAIVKDVMYICPFMGAVSGTLTVTDFKMYFKNVERDPPFILDVPLGVISRVEKIGVQSHGDNSCGIEIVCKDMRNLRLAY 80
                        90       100
                ....*....|....*....|
gi 8393794  191 KQEEQRKLGIFENLNKHAFP 210
Cdd:cd13358  81 KQEEQSKLEIFENLNKHAFP 100
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
217-556 0e+00

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: 253817  Cd Length: 347  Bit Score: 608.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794    217 LFAFNYKEKFPVN----GWKVYDPVSEYKRQGLPNE-SWKISKINSNYEFCDTYPAIIVVPTSVKDDDLSKVAAFRAKGR 291
Cdd:pfam06602   2 LFAFSYNPKFSELerldGWKIFDPEREYKRLGLPNSnAWRISSVNENYEICPSYPAKLIVPKSISDDELKKVAKFRSGGR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794    292 VPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYLQTIMDANAQSHKLTIFDARQNSVADTNKAKGGGYENESAYPNA 371
Cdd:pfam06602  82 FPVLSWRHKENGAVIVRCSQPLVGIMGKRCKEDEKLLAAIRKSNPQSKKLYIVDARPRLNALANKAKGGGYENEDNYPNA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794    372 ELIFLEIHNIHVMRESLRKLKEI-VYPSIDESHWLSNVDGTHWLEYIRVLLAGAVRIADKIESGKTSVVIHCSDGWDRTS 450
Cdd:pfam06602 162 ELIFLGIPNIHVMRESLQKLREAcVTNEPDESSWLSSLESSGWLQHISAILAGAALIADAVDSEGSSVLVHCSDGWDRTA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794    451 QLTSLAMLMLDSYYRTIKGFEALIEKEWISFGHRFALRVGHGDDNHADADRSPIFLQFIDCVWQMTRQFPSAFEFNELFL 530
Cdd:pfam06602 242 QVTSLAQLLLDPYYRTIEGFQVLVEKEWLSFGHKFADRCGHLNNNGDSKERSPVFLQFLDCVWQLMRQFPCAFEFNEFFL 321
                         330       340
                  ....*....|....*....|....*.
gi 8393794    531 ITILDHLYSCLFGTFLCNCEQQRIKE 556
Cdd:pfam06602 322 IFLADHLYSCQFGTFLCNSEKEREEL 347
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
103-165 1.04e-08

domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;


Pssm-ID: 214725  Cd Length: 60  Bit Score: 52.60  E-value: 1.04e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8393794     103 PLFPGESIKAIvkdviYICPFMGA--VSGTLTVTDFKMYFKNVERDPHFVLDVPLGVISRVEKIG 165
Cdd:smart00568   1 KLPEEEKLIAD-----YSCYLSRTgpVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIEKST 60
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
119-165 6.31e-08

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins.


Pssm-ID: 251600  Cd Length: 60  Bit Score: 50.33  E-value: 6.31e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 8393794    119 YICPFMGA---VSGTLTVTDFKMYFKNVERDPHFVLDVPLGVISRVEKIG 165
Cdd:pfam02893  11 YSCYLWTPispVQGRLYLTNYRLCFRSDKFGDSTVVVIPLADIERVEKET 60
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
414-538 1.36e-07

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649  Cd Length: 105  Bit Score: 50.05  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794     414 LEYIRvllagAVRIADKIESGKTSVVIHCSDGWDRTSQLTSLAMLMLDSYYRTikgfealiekewisfghrfalrvghgd 493
Cdd:smart00404  23 LELLR-----AVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--------------------------- 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 8393794     494 dnhadadrspIFLQFIDCVWQMTRQFPSAFEFNELFLITILDHLY 538
Cdd:smart00404  71 ----------GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
 
Name Accession Description Interval E-value
PH-GRAM_MTMR1 cd13358
Myotubularian related 1 protein (MTMR1) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
111-210 7.32e-68

Myotubularian related 1 protein (MTMR1) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR1 is a member of the myotubularin protein phosphatase gene family. MTMR1 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. MTMR1 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal PDZ 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: 270165  Cd Length: 100  Bit Score: 218.62  E-value: 7.32e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794  111 KAIVKDVIYICPFMGAVSGTLTVTDFKMYFKNVERDPHFVLDVPLGVISRVEKIGAQSHGDNSCGIEIVCKDMRNLRLAY 190
Cdd:cd13358   1 KAIVKDVMYICPFMGAVSGTLTVTDFKMYFKNVERDPPFILDVPLGVISRVEKIGVQSHGDNSCGIEIVCKDMRNLRLAY 80
                        90       100
                ....*....|....*....|
gi 8393794  191 KQEEQRKLGIFENLNKHAFP 210
Cdd:cd13358  81 KQEEQSKLEIFENLNKHAFP 100
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
217-556 0e+00

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: 253817  Cd Length: 347  Bit Score: 608.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794    217 LFAFNYKEKFPVN----GWKVYDPVSEYKRQGLPNE-SWKISKINSNYEFCDTYPAIIVVPTSVKDDDLSKVAAFRAKGR 291
Cdd:pfam06602   2 LFAFSYNPKFSELerldGWKIFDPEREYKRLGLPNSnAWRISSVNENYEICPSYPAKLIVPKSISDDELKKVAKFRSGGR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794    292 VPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYLQTIMDANAQSHKLTIFDARQNSVADTNKAKGGGYENESAYPNA 371
Cdd:pfam06602  82 FPVLSWRHKENGAVIVRCSQPLVGIMGKRCKEDEKLLAAIRKSNPQSKKLYIVDARPRLNALANKAKGGGYENEDNYPNA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794    372 ELIFLEIHNIHVMRESLRKLKEI-VYPSIDESHWLSNVDGTHWLEYIRVLLAGAVRIADKIESGKTSVVIHCSDGWDRTS 450
Cdd:pfam06602 162 ELIFLGIPNIHVMRESLQKLREAcVTNEPDESSWLSSLESSGWLQHISAILAGAALIADAVDSEGSSVLVHCSDGWDRTA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794    451 QLTSLAMLMLDSYYRTIKGFEALIEKEWISFGHRFALRVGHGDDNHADADRSPIFLQFIDCVWQMTRQFPSAFEFNELFL 530
Cdd:pfam06602 242 QVTSLAQLLLDPYYRTIEGFQVLVEKEWLSFGHKFADRCGHLNNNGDSKERSPVFLQFLDCVWQLMRQFPCAFEFNEFFL 321
                         330       340
                  ....*....|....*....|....*.
gi 8393794    531 ITILDHLYSCLFGTFLCNCEQQRIKE 556
Cdd:pfam06602 322 IFLADHLYSCQFGTFLCNSEKEREEL 347
PH-GRAM_MTM-like cd13223
Myotubularian 1 and related proteins Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase; ...
112-210 3.67e-51

Myotubularian 1 and related proteins Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase; MTM1, MTMR1, and MTMR2 are members of the myotubularin protein phosphatase gene family. They contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. In addition MTMR1 (Myotubularian related 1 protein) and MTMR2 (Myotubularian related 2 protein) contain a C-terminal PDZ domain. Mutations in MTMR2 are a cause of Charcot-Marie-Tooth disease type 4B, an autosomal recessive demyelinating neuropathy. The protein can self-associate and form heteromers with MTMR5 and MTMR12. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. 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 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: 275407  Cd Length: 100  Bit Score: 172.81  E-value: 3.67e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794  112 AIVKDVIYICPFMGAVSGTLTVTDFKMYFKNVERDPHFVLDVPLGVISRVEKIGAQSH-GDNSCGIEIVCKDMRNLRLAY 190
Cdd:cd13223   1 LKEKDVTYLCPFRGPVRGTLYITNYRLYFKSRDREPNFVLDVPLGVISRVEKVGGATSrGENSYGLEIHCKDMRNLRFAH 80
                        90       100
                ....*....|....*....|
gi 8393794  191 KQEEQRKLGIFENLNKHAFP 210
Cdd:cd13223  81 KQENHSRRKLYETLQKYAFP 100
PH-GRAM_MTMR2_mammal-like cd13356
Myotubularian related 2 protein (MTMR2) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
99-212 5.33e-49

Myotubularian related 2 protein (MTMR2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR2 is a member of the myotubularin protein phosphatase gene family. MTMR2 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. Mutations in MTMR2 are a cause of Charcot-Marie-Tooth disease type 4B, an autosomal recessive demyelinating neuropathy. The protein can self-associate and form heteromers with MTMR5 and MTMR12. MTMR2 contains a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal PDZ 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.Members in this cd include mammals, chickens, anoles, human body lice, and aphids.


Pssm-ID: 270163  Cd Length: 115  Bit Score: 167.56  E-value: 5.33e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794   99 MEEAPLFPGESIKAIVKDVIYICPFMGAVSGTLTVTDFKMYFKNVERDPHFVLDVPLGVISRVEKI-GAQSHGDNSCGIE 177
Cdd:cd13356   1 MEEPPLLPGENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVINRVEKIgGASSRGENSYGLE 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 8393794  178 IVCKDMRNLRLAYKQEEQRKLGIFENLNKHAFPLS 212
Cdd:cd13356  81 TVCKDIRNLRFAHKPEGRTRRSIFENLMKYAFPVS 115
PH-GRAM_MTMR2_insect-like cd13357
Myotubularian related 2 protein (MTMR2) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
112-210 1.59e-41

Myotubularian related 2 protein (MTMR2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR2 is a member of the myotubularin protein phosphatase gene family. MTMR2 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. Mutations in MTMR2 are a cause of Charcot-Marie-Tooth disease type 4B, an autosomal recessive demyelinating neuropathy. The protein can self-associate and form heteromers with MTMR5 and MTMR12. MTMR2 contains a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal PDZ 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. Members in this cd include Drosophila, sea urchins, mosquitos, bees, ticks, and anemones.


Pssm-ID: 270164  Cd Length: 100  Bit Score: 146.11  E-value: 1.59e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794  112 AIVKDVIYICPFMGAVSGTLTVTDFKMYFKNVERDPHFVLDVPLGVISRVEKIG-AQSHGDNSCGIEIVCKDMRNLRLAY 190
Cdd:cd13357   1 AIAKDVTYLCPFRGPVRGTLTITNYKLYFKSLDREPPFTVEVPLGVIYRVEKVGgATSRGENSYGLEIFCKDMRNLRFAH 80
                        90       100
                ....*....|....*....|
gi 8393794  191 KQEEQRKLGIFENLNKHAFP 210
Cdd:cd13357  81 KQENHSRRLVFEKLQAYAFP 100
PH-GRAM_MTM1 cd13355
Myotubularian 1 protein (MTM1) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
115-210 2.88e-39

Myotubularian 1 protein (MTM1) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTM1 is a member of the myotubularin protein phosphatase gene family. It is required for muscle cell differentiation and mutations in this gene have been identified as being responsible for X-linked myotubular myopathy, a severe congenital muscle disorder characterized by defective muscle cell development. Since its initial discovery, there have been an additional 14 myotubularin-related proteins identified. MTM1 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The protein can self-associate and form heteromers with MTMR12. MTM1 contains a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. 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. 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. All 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 and PH domains C-terminal to the coiled-coil region.


Pssm-ID: 270162  Cd Length: 100  Bit Score: 139.99  E-value: 2.88e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794  115 KDVIYICPFMGAVSGTLTVTDFKMYFKNVERDPHFVLDVPLGVISRVEKI-GAQSHGDNSCGIEIVCKDMRNLRLAYKQE 193
Cdd:cd13355   4 KDVIYICPFNGPVKGRVYITNYRLYFKSTESEPPVTLDVPLGVISRIEKMgGASSRGENSYGLDITCKDMRNLRFALKQE 83
                        90
                ....*....|....*..
gi 8393794  194 EQRKLGIFENLNKHAFP 210
Cdd:cd13355  84 GHSRRDIFEILTKYAFP 100
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
103-165 1.04e-08

domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;


Pssm-ID: 214725  Cd Length: 60  Bit Score: 52.60  E-value: 1.04e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8393794     103 PLFPGESIKAIvkdviYICPFMGA--VSGTLTVTDFKMYFKNVERDPHFVLDVPLGVISRVEKIG 165
Cdd:smart00568   1 KLPEEEKLIAD-----YSCYLSRTgpVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIEKST 60
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
119-165 6.31e-08

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins.


Pssm-ID: 251600  Cd Length: 60  Bit Score: 50.33  E-value: 6.31e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 8393794    119 YICPFMGA---VSGTLTVTDFKMYFKNVERDPHFVLDVPLGVISRVEKIG 165
Cdd:pfam02893  11 YSCYLWTPispVQGRLYLTNYRLCFRSDKFGDSTVVVIPLADIERVEKET 60
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
114-195 1.06e-07

Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) 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: 275393  Cd Length: 94  Bit Score: 50.07  E-value: 1.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794  114 VKDVIYICPFMGAVSGTLTVTDFKMYFKNVERDPHFVLDVPLGVISRVEKIGAQShgDNSCGIEIVCKDMRNLRLAYKQE 193
Cdd:cd10570   6 VRFCCALRPRKLPLEGTLYLSTYRLIFSSKADGDETKLVIPLVDITDVEKIAGAS--FLPSGLIITCKDFRTIKFSFDSE 83

                ..
gi 8393794  194 EQ 195
Cdd:cd10570  84 DE 85
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
414-538 1.36e-07

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649  Cd Length: 105  Bit Score: 50.05  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794     414 LEYIRvllagAVRIADKIESGKTSVVIHCSDGWDRTSQLTSLAMLMLDSYYRTikgfealiekewisfghrfalrvghgd 493
Cdd:smart00404  23 LELLR-----AVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--------------------------- 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 8393794     494 dnhadadrspIFLQFIDCVWQMTRQFPSAFEFNELFLITILDHLY 538
Cdd:smart00404  71 ----------GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
414-538 1.36e-07

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469  Cd Length: 105  Bit Score: 50.05  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393794     414 LEYIRvllagAVRIADKIESGKTSVVIHCSDGWDRTSQLTSLAMLMLDSYYRTikgfealiekewisfghrfalrvghgd 493
Cdd:smart00012  23 LELLR-----AVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--------------------------- 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 8393794     494 dnhadadrspIFLQFIDCVWQMTRQFPSAFEFNELFLITILDHLY 538
Cdd:smart00012  71 ----------GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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