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Conserved domains on  [gi|2173616156|ref|NP_001013065|]
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myotubularin isoform 1 [Rattus norvegicus]

Protein Classification

myotubularin family protein( domain architecture ID 10352270)

myotubularin family protein similar to myotubularin, a protein tyrosine phosphatase that dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2)

CATH:  3.90.190.10
EC:  3.1.3.-
Gene Ontology:  GO:0004438|GO:0046856|GO:0035091|GO:0006470|GO:0004721
PubMed:  16289848|12925573|9736772|27514797
SCOP:  4001084

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 162-489 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: 461958 [Multi-domain]  Cd Length: 332  Bit Score: 577.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 162 DGWAIYNPVEEYRRQGLP-DRHWRISFVNQRYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENRAAIM 240
Cdd:pfam06602   3 NGWDLYDPEAEFARQGLPsKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVIT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 241 RCSQPLVGVGGKRSRDDERYLDIIRETNKQTS--KLTIYDARPGVNAVANKATGGGYEGEDAYPHAELSFLDIHNIHVMR 318
Cdd:pfam06602  83 RSSQPLVGLNGKRSIEDEKLLQAIFKSSNPYSakKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 319 ESLRRVRDIVYP-HVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRTAQLTTLAMLMLDGFY 397
Cdd:pfam06602 163 DSLNKLVEACNDrSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYY 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 398 RSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQMTKQFPTAFEFNECFLVAILDHLYSCRFGT 477
Cdd:pfam06602 243 RTIEGFQVLIEKEWLSFGHKFADRCGHLAGFTDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGT 322

                         330
                  ....*....|..
gi 2173616156 478 FLLNCEaaRERQ 489
Cdd:pfam06602 323 FLCNSE--KERV 332
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 44-143 4.87e-64

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 cd13355:

Pssm-ID: 473070  Cd Length: 100  Bit Score: 205.47  E-value: 4.87e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  44 ITDKEVIYICPFSGPVKGRLYITNYRLYLRSLETDLAPILDVPLGVISRIEKMGGVTSRGENSYGLDITCKDLRNLRFAL 123
Cdd:cd13355     1 VTDKDVIYICPFNGPVKGRVYITNYRLYFKSTESEPPVTLDVPLGVISRIEKMGGASSRGENSYGLDITCKDMRNLRFAL 80

                          90       100
                  ....*....|....*....|
gi 2173616156 124 KQEGHSRRDIFDVLTRHAFP 143
Cdd:cd13355    81 KQEGHSRRDIFEILTKYAFP 100
 
Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 162-489 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: 461958 [Multi-domain]  Cd Length: 332  Bit Score: 577.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 162 DGWAIYNPVEEYRRQGLP-DRHWRISFVNQRYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENRAAIM 240
Cdd:pfam06602   3 NGWDLYDPEAEFARQGLPsKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVIT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 241 RCSQPLVGVGGKRSRDDERYLDIIRETNKQTS--KLTIYDARPGVNAVANKATGGGYEGEDAYPHAELSFLDIHNIHVMR 318
Cdd:pfam06602  83 RSSQPLVGLNGKRSIEDEKLLQAIFKSSNPYSakKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 319 ESLRRVRDIVYP-HVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRTAQLTTLAMLMLDGFY 397
Cdd:pfam06602 163 DSLNKLVEACNDrSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYY 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 398 RSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQMTKQFPTAFEFNECFLVAILDHLYSCRFGT 477
Cdd:pfam06602 243 RTIEGFQVLIEKEWLSFGHKFADRCGHLAGFTDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGT 322

                         330
                  ....*....|..
gi 2173616156 478 FLLNCEaaRERQ 489
Cdd:pfam06602 323 FLCNSE--KERV 332
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
 223-471 0e+00

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: 528.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 223 NRIPVLSWIHPENRAAIMRCSQPLVGVGGKRSRDDERYLDIIRETNKQTSKLTIYDARPGVNAVANKATGGGYEGEDAYP 302
Cdd:cd14591     1 NRIPVLSWIHPENQAVIMRCSQPLVGMSGKRNKDDEKYLDIIREANGQTSKLTIYDARPSVNAVANKATGGGYEGDDAYQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 303 HAELSFLDIHNIHVMRESLRRVRDIVYPHVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRT 382
Cdd:cd14591    81 NAELVFLDIHNIHVMRESLKKLKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWDRT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 383 AQLTTLAMLMLDGFYRSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQMTKQFPTAFEFNECF 462
Cdd:cd14591   161 AQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGHGDKNHADADRSPIFLQFIDCVWQMSKQFPTAFEFNEQF 240


                  ....*....
gi 2173616156 463 LVAILDHLY 471
Cdd:cd14591   241 LITILDHLY 249
PH-GRAM_MTM1 cd13355
Myotubularian 1 protein (MTM1) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 44-143 4.87e-64

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: 205.47  E-value: 4.87e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  44 ITDKEVIYICPFSGPVKGRLYITNYRLYLRSLETDLAPILDVPLGVISRIEKMGGVTSRGENSYGLDITCKDLRNLRFAL 123
Cdd:cd13355     1 VTDKDVIYICPFNGPVKGRVYITNYRLYFKSTESEPPVTLDVPLGVISRIEKMGGASSRGENSYGLDITCKDMRNLRFAL 80

                          90       100
                  ....*....|....*....|
gi 2173616156 124 KQEGHSRRDIFDVLTRHAFP 143
Cdd:cd13355    81 KQEGHSRRDIFEILTKYAFP 100
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 38-143 4.19e-17

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 77.41  E-value: 4.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  38 LPGESAITDkeviYICPFS---GPVKGRLYITNYRLYLRSLETDLAPILDVPLGVISRIEKMGGVTSRGENSYGLDITCK 114
Cdd:pfam02893  10 PPEERLIAS----YSCYLNrdgGPVQGRLYLTNYRLCFRSLPKGWSTKVVIPLVDIEEIEKLKGGANLFPNGIQVETGSN 85

                          90       100
                  ....*....|....*....|....*....
gi 2173616156 115 DlrNLRFALKQEGHSRRDIFDVLTRHAFP 143
Cdd:pfam02893  86 D--KFSFAGFVTRDEAIEFILALLKNAHP 112
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
38-97 8.75e-12

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 60.30  E-value: 8.75e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2173616156   38 LPGESAITDkeviYICPFS--GPVKGRLYITNYRLYLRSLETDLAPILDVPLGVISRIEKMG 97
Cdd:smart00568   3 PEEEKLIAD----YSCYLSrtGPVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIEKST 60
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
357-471 6.30e-06

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 45.04  E-value: 6.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  357 AIRVADKVASGLSSVLVHCSDGWDRTAQLTTLAMLMLdgfyrsiegfeilvqkewisfghkfssrighgdknhaDADRSP 436
Cdd:smart00404  28 AVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQ-------------------------------------QLEAEA 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2173616156  437 IFLQFIDCVWQMTKQFPTAFEFNECFLVAILDHLY 471
Cdd:smart00404  71 GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
 
Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 162-489 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: 461958 [Multi-domain]  Cd Length: 332  Bit Score: 577.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 162 DGWAIYNPVEEYRRQGLP-DRHWRISFVNQRYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENRAAIM 240
Cdd:pfam06602   3 NGWDLYDPEAEFARQGLPsKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVIT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 241 RCSQPLVGVGGKRSRDDERYLDIIRETNKQTS--KLTIYDARPGVNAVANKATGGGYEGEDAYPHAELSFLDIHNIHVMR 318
Cdd:pfam06602  83 RSSQPLVGLNGKRSIEDEKLLQAIFKSSNPYSakKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 319 ESLRRVRDIVYP-HVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRTAQLTTLAMLMLDGFY 397
Cdd:pfam06602 163 DSLNKLVEACNDrSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYY 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 398 RSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQMTKQFPTAFEFNECFLVAILDHLYSCRFGT 477
Cdd:pfam06602 243 RTIEGFQVLIEKEWLSFGHKFADRCGHLAGFTDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGT 322

                         330
                  ....*....|..
gi 2173616156 478 FLLNCEaaRERQ 489
Cdd:pfam06602 323 FLCNSE--KERV 332
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
 223-471 0e+00

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: 528.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 223 NRIPVLSWIHPENRAAIMRCSQPLVGVGGKRSRDDERYLDIIRETNKQTSKLTIYDARPGVNAVANKATGGGYEGEDAYP 302
Cdd:cd14591     1 NRIPVLSWIHPENQAVIMRCSQPLVGMSGKRNKDDEKYLDIIREANGQTSKLTIYDARPSVNAVANKATGGGYEGDDAYQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 303 HAELSFLDIHNIHVMRESLRRVRDIVYPHVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRT 382
Cdd:cd14591    81 NAELVFLDIHNIHVMRESLKKLKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWDRT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 383 AQLTTLAMLMLDGFYRSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQMTKQFPTAFEFNECF 462
Cdd:cd14591   161 AQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGHGDKNHADADRSPIFLQFIDCVWQMSKQFPTAFEFNEQF 240


                  ....*....
gi 2173616156 463 LVAILDHLY 471
Cdd:cd14591   241 LITILDHLY 249
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
 223-471 5.39e-179

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: 505.83  E-value: 5.39e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 223 NRIPVLSWIHPENRAAIMRCSQPLVGVGGKRSRDDERYLDIIRETNKQTSKLTIYDARPGVNAVANKATGGGYEGEDAYP 302
Cdd:cd14535     1 NRIPVLSWIHPESQATITRCSQPLVGVSGKRSKDDEKYLQLIMDANAQSHKLFIMDARPSVNAVANKAKGGGYESEDAYQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 303 HAELSFLDIHNIHVMRESLRRVRDIVYPHVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRT 382
Cdd:cd14535    81 NAELVFLDIHNIHVMRESLRKLKDICFPNIDDSHWLSNLESTHWLEHIKLILAGAVRIADKVESGKTSVVVHCSDGWDRT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 383 AQLTTLAMLMLDGFYRSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQMTKQFPTAFEFNECF 462
Cdd:cd14535   161 AQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGHGDKNHSDADRSPVFLQFIDCVWQMTRQFPNAFEFNEHF 240


                  ....*....
gi 2173616156 463 LVAILDHLY 471
Cdd:cd14535   241 LITILDHLY 249
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 210-471 2.43e-176

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: 499.56  E-value: 2.43e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 210 DDDLRRVATFRSRNRIPVLSWIHPENRAAIMRCSQPLVGVGGKRSRDDERYLDIIRETNKQTSKLTIYDARPGVNAVANK 289
Cdd:cd14590     1 DEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFDARPSVNAVANK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 290 ATGGGYEGEDAYPHAELSFLDIHNIHVMRESLRRVRDIVYPHVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLS 369
Cdd:cd14590    81 AKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEESHWLSNLESTHWLEHIKLILAGALRIADKVESGKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 370 SVLVHCSDGWDRTAQLTTLAMLMLDGFYRSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQMT 449
Cdd:cd14590   161 SVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVFLQFIDCVWQMT 240

                         250       260
                  ....*....|....*....|..
gi 2173616156 450 KQFPTAFEFNECFLVAILDHLY 471
Cdd:cd14590   241 RQFPTAFEFNEYFLITILDHLY 262
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 224-471 1.94e-151

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: 435.95  E-value: 1.94e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 224 RIPVLSWIHPENRAAIMRCSQPLVGVGGKRSRDDERYLDIIRETNKQTSKLTIYDARPGVNAVANKATGGGYEGEDAYPH 303
Cdd:cd14592     2 RVPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYLQTIMDANAQSHKLIIFDARQNSVADTNKTKGGGYESESAYPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 304 AELSFLDIHNIHVMRESLRRVRDIVYPHVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRTA 383
Cdd:cd14592    82 AELVFLEIHNIHVMRESLRKLKEIVYPSIDEARWLSNVDGTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGWDRTA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 384 QLTTLAMLMLDGFYRSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQMTKQFPTAFEFNECFL 463
Cdd:cd14592   162 QLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGHGDDNHADADRSPIFLQFIDCVWQMTRQFPSAFEFNELFL 241


                  ....*...
gi 2173616156 464 VAILDHLY 471
Cdd:cd14592   242 ITILDHLY 249
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
 223-447 2.05e-137

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: 399.23  E-value: 2.05e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 223 NRIPVLSWIHPENRAAIMRCSQPLVGVGGKRSRDDERYLDIIRETNKQTSKLTIYDARPGVNAVANKATGGGYEGEDAYP 302
Cdd:cd14507     1 GRIPVLSWRHPRNGAVICRSSQPLVGLTGSRSKEDEKLLNAIRKASPSSKKLYIVDARPKLNAVANRAKGGGYENTEYYP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 303 HAELSFLDIHNIHVMRESLRRVRDIVY-PHVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDR 381
Cdd:cd14507    81 NCELEFLNIENIHAMRDSLNKLRDACLsPNDEESNWLSALESSGWLEHIRLILKGAVRVADLLEKEGTSVLVHCSDGWDR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2173616156 382 TAQLTTLAMLMLDGFYRSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQ 447
Cdd:cd14507   161 TSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDKNSSDEERSPIFLQFLDCVWQ 226
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 169-472 5.14e-134

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: 393.25  E-value: 5.14e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 169 PVEEYRRQGLPDRHWRISFVNQRYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENRAAIMRCSQPLVG 248
Cdd:cd14532     1 LESEYTRMGVPNDNWTLSDINKDYELCDTYPRELFVPTSASTPVLVGSSKFRSKGRLPVLSYLHKDNQAAICRCSQPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 249 VGGkRSRDDERYLDIIRETNKQTSKLTIYDARPGVNAVANKATGGGYEGEDAYPHAELSFLDIHNIHVMRESLRRVRDIV 328
Cdd:cd14532    81 FSA-RCVEDEQLLQAIRKANPNSKFMYVVDTRPKINAMANKAAGKGYENEDNYSNIKFQFFGIENIHVMRSSLQKLLEVC 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 329 -YPHVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGlSSVLVHCSDGWDRTAQLTTLAMLMLDGFYRSIEGFEILV 407
Cdd:cd14532   160 eLKNPSMSAFLSGLESSGWLKHIKAVMDTSVFIAKAVSEG-ASVLVHCSDGWDRTAQTCSLASLLLDPYYRTIKGFQVLI 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2173616156 408 QKEWISFGHKFSSRIGHGDKNHADAdrSPIFLQFIDCVWQMTKQFPTAFEFNECFLVAILDHLYS 472
Cdd:cd14532   239 EKEWLSFGHKFTDRCGHLQGDAKEV--SPVFTQFLDCVWQLMQQFPRAFEFNERFLLTLHDHVYS 301
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 163-472 2.87e-115

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: 345.70  E-value: 2.87e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 163 GWAIYNPVEEYRRQGLPDRHWRISFVNQRYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENRAAIMRC 242
Cdd:cd14584     1 GWKLIDLKVDFQRMGIPNDYWEITDANKNYEICSTYPPELVVPKSASKATVVGSSKFRSRGRFPVLSYLYKENNAAICRC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 243 SQPLVGVGGkRSRDDERYLDIIRETNKQTSKLTIYDARPGVNAVANKATGGGYEGEDAYPHAELSFLDIHNIHVMRESLR 322
Cdd:cd14584    81 SQPLSGFSA-RCVEDEQMLQAISKANPGSPFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIRFQFIGIENIHVMRSSLQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 323 RVRDIV---YPHVEEahWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRTAQLTTLAMLMLDGFYRS 399
Cdd:cd14584   160 KLLEVCemkSPSMSD--FLTGLENSGWLRHIKAVMDAGVFLAKAVKEEKASVLVHCSDGWDRTAQVCSLASLLLDPFYRT 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2173616156 400 IEGFEILVQKEWISFGHKFSSRIGHGDKNHADAdrSPIFLQFIDCVWQMTKQFPTAFEFNECFLVAILDHLYS 472
Cdd:cd14584   238 IKGLMVLIEKEWISMGHKFSQRCGHLDGDPKEV--SPVFTQFLECVWQLMEQFPCAFEFNEHFLLEIHDHVFS 308
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 171-472 1.38e-107

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: 325.73  E-value: 1.38e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 171 EEYRRQGLPDRHWRISFVNQRYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENRAAIMRCSQPLVGVG 250
Cdd:cd14585     3 EEYKRMGVPNDYWQLSDVNRDYKICDTYPRDLYVPITASKPIIVGSSKFRSKGRFPVLSYYHQEKKAAICRCSQPLSGFS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 251 GkRSRDDERYLDIIRETNKQTSKLTIYDARPGVNAVANKATGGGYEGEDAYPHAELSFLDIHNIHVMRESLRRVRDIVYP 330
Cdd:cd14585    83 A-RCLEDEHMLQAISKANPNNRYMYVMDTRPKLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVCGT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 331 HVEEAH-WLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRTAQLTTLAMLMLDGFYRSIEGFEILVQK 409
Cdd:cd14585   162 KALSVNdFLSGLESSGWLRHIKAVLDAAVFLAKAVAVEGASVLVHCSDGWDRTAQVCSLGSLLLDPYYRTIKGFMVLIEK 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2173616156 410 EWISFGHKFSSRIGHGDKNHADAdrSPIFLQFIDCVWQMTKQFPTAFEFNECFLVAILDHLYS 472
Cdd:cd14585   242 DWISFGHKFSDRCGQLDGDPKEI--SPVFTQFLECVWQLTEQFPRAFEFSEAFLLQIHEHIHS 302
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 171-472 2.21e-105

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: 319.98  E-value: 2.21e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 171 EEYRRQGLPDRHWRISFVNQRYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENRAAIMRCSQPLVGVG 250
Cdd:cd14583     3 AEYNRMGLPNSLWQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYYCKDNNASICRSSQPLSGFS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 251 GkRSRDDERYLDIIRETNKQTSKLTIYDARPGVNAVANKATGGGYEGEDAYPHAELSFLDIHNIHVMRESLRR---VRDI 327
Cdd:cd14583    83 A-RCLEDEQMLQAIRKANPGSDFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKmleVCEL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 328 VYPHVEEAHWlsSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRTAQLTTLAMLMLDGFYRSIEGFEILV 407
Cdd:cd14583   162 RSPSMGDFLW--GLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLI 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2173616156 408 QKEWISFGHKFSSRIGHGDKNHADAdrSPIFLQFIDCVWQMTKQFPTAFEFNECFLVAILDHLYS 472
Cdd:cd14583   240 EKDWVSFGHKFNHRYGHLDGDPKEV--SPVIDQFIECVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 183-447 1.29e-83

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: 264.20  E-value: 1.29e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 183 WRISFVNQRYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENRAAIMRCSQPLVGVGGKRSRDDERYLD 262
Cdd:cd14587     3 WRVSEINSNYKLCSSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAVIARCSQPEISWWGWRNADDEYLVT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 263 II----------RETNKQTS-------------------------------KLTIYDARPGVNAVANKATGGGYEGEDAY 301
Cdd:cd14587    83 SIakacaldpgtRAPGGSPSkgnsdgsdasdtdfdssltacsavesgaapqKLLILDARSYTAAVANRAKGGGCECEEYY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 302 PHAELSFLDIHNIHVMRESLRRVRDIVYPHVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDR 381
Cdd:cd14587   163 PNCEVMFMGMANIHSIRNSFQYLRAVCSQMPDPGNWLSALESTKWLQHLSVMLKAAVLVASAVDREGRPVLVHCSDGWDR 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2173616156 382 TAQLTTLAMLMLDGFYRSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQ 447
Cdd:cd14587   243 TPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHQENVEDQNEQCPVFLQWLDCVHQ 308
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 180-447 3.15e-83

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: 263.42  E-value: 3.15e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 180 DRHWRISFVNQRYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENRAAIMRCSQPLVGVGGKRSRDDER 259
Cdd:cd14586     5 QNAWRISNINEKYKLCGSYPQELIVPAWITDKELESVASFRSWKRIPAVVYRHQSNGAVIARCGQPEVSWWGWRNADDEH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 260 YL---------------------DIIRE----------------TNK--------QTSKLTIYDARPGVNAVANKATGGG 294
Cdd:cd14586    85 LVqsvakacasdssscksvlmtgNCSRDfpnggdlsdvefdssmSNAsgveslaiQPQKLLILDARSYAAAVANRAKGGG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 295 YEGEDAYPHAELSFLDIHNIHVMRESLRRVRDIVYPHVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVH 374
Cdd:cd14586   165 CECPEYYPNCEVVFMGMANIHSIRKSFQSLRLLCTQMPDPANWLSALESTKWLQHLSMLLKSALLVVHAVDRDQRPVLVH 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2173616156 375 CSDGWDRTAQLTTLAMLMLDGFYRSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQ 447
Cdd:cd14586   245 CSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRCGHGENSDDLNERCPVFLQWLDCVHQ 317
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 223-447 8.13e-79

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: 248.86  E-value: 8.13e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 223 NRIPVLSWIHPENRAAIMRCSQPLVGVGGKRSRDDERYLDIIRET---NKQTSKLTIYDARPGVNAVANKATGGGYEGED 299
Cdd:cd14533     2 KRIPSVVWRHQRNGAVIARCSQPEVGWLGWRNAEDENLLQAIAEAcasNASPKKLLIVDARSYAAAVANRAKGGGCECPE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 300 AYPHAELSFLDIHNIHVMRESLRRVRDIVYPHVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGW 379
Cdd:cd14533    82 YYPNCEVVFMNLANIHAIRKSFHSLRALCSSAPDQPNWLSNLESTKWLHHLSGLLKAALLVVNAVDEEGRPVLVHCSDGW 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2173616156 380 DRTAQLTTLAMLMLDGFYRSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQ 447
Cdd:cd14533   162 DRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFGHKFADRCGHGVNSEDINERCPVFLQWLDCVHQ 229
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
 223-447 8.80e-79

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: 248.51  E-value: 8.80e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 223 NRIPVLSWIHPENRAAIMRCSQPLVGVGGKRSRDDERYLDII-----RETNKQTSKLTIYDARPGVNAVANKATGGGYEG 297
Cdd:cd17666     1 QRIPVLTYLHKANGCSITRSSQPLVGLKQNRSIQDEKLVSEIfntsiNEIYISPQKNLIVDARPTTNAMAQVALGAGTEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 298 ED--AYPHAELSFLDIHNIHVMRESLRRVRDIV----YPHVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSV 371
Cdd:cd17666    81 MDnyKYKTAKKIYLGIDNIHVMRDSLNKVTEALkdgdDSNPSYPPLINALKKSNWLKYLAIILQGADLIAKSIHFNHSHV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2173616156 372 LVHCSDGWDRTAQLTTLAMLMLDGFYRSIEGFEILVQKEWISFGHKFSSRIGHGDKnhadadrSPIFLQFIDCVWQ 447
Cdd:cd17666   161 LIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFAERSGHKET-------SPVFHQFLDCVYQ 229
PH-GRAM_MTM1 cd13355
Myotubularian 1 protein (MTM1) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 44-143 4.87e-64

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: 205.47  E-value: 4.87e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  44 ITDKEVIYICPFSGPVKGRLYITNYRLYLRSLETDLAPILDVPLGVISRIEKMGGVTSRGENSYGLDITCKDLRNLRFAL 123
Cdd:cd13355     1 VTDKDVIYICPFNGPVKGRVYITNYRLYFKSTESEPPVTLDVPLGVISRIEKMGGASSRGENSYGLDITCKDMRNLRFAL 80

                          90       100
                  ....*....|....*....|
gi 2173616156 124 KQEGHSRRDIFDVLTRHAFP 143
Cdd:cd13355    81 KQEGHSRRDIFEILTKYAFP 100
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 224-447 5.23e-58

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: 194.09  E-value: 5.23e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 224 RIPVLSWIHPENRAAIMRCSQPLVGVGGKRSRDDERYLDIIRETNKqtsKLTIYDARPGVNAVANKATGGGYEGEDAYPH 303
Cdd:cd14536     2 RFPVLSYYHKKNGMVLMRSSQPLTGPNGKRCKEDEKLLNAVLGGGK---RGYIIDTRSKNVAQQARAKGGGFEPEAHYPQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 304 AELSFLDIHNIHVMRESL-RRVRDIVYPHVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRT 382
Cdd:cd14536    79 WRRIHKPIERYNVLQESLiKLVEACNDQGHSMDKWLSKLESSNWLSHVKEILTTACLVAQCIDREGASVLVHGSEGMDST 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2173616156 383 AQLTTLAMLMLDGFYRSIEGFEILVQKEWISFGHKFSSRIGHGDKNHA-DADRSPIFLQFIDCVWQ 447
Cdd:cd14536   159 LQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRCAKSAYSNSkQKFESPVFLLFLDCVWQ 224
PH-GRAM_MTM-like cd13223
Myotubularian 1 and related proteins Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase; ...
 44-143 1.64e-55

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: 182.82  E-value: 1.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  44 ITDKEVIYICPFSGPVKGRLYITNYRLYLRSLETDLAPILDVPLGVISRIEKMGGVTSRGENSYGLDITCKDLRNLRFAL 123
Cdd:cd13223     1 LKEKDVTYLCPFRGPVRGTLYITNYRLYFKSRDREPNFVLDVPLGVISRVEKVGGATSRGENSYGLEIHCKDMRNLRFAH 80

                          90       100
                  ....*....|....*....|
gi 2173616156 124 KQEGHSRRDIFDVLTRHAFP 143
Cdd:cd13223    81 KQENHSRRKLYETLQKYAFP 100
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 183-451 1.97e-54

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: 186.42  E-value: 1.97e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 183 WRISFVNQRYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENRAAIMRCSQP-LVGVGGKRsrdderyl 261
Cdd:cd14534     1 FRISTANRDYSICRSYPALVVVPQSVSDESLRKVARCYRQGRFPVVTWRHPRTKALLLRSGGFhGKGVMGML-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 262 diiRETNKQTSKLTIYDARPG--------VNAVA-----NKATGGGYEGEdAYPHAELSFLDIHNIHVMRESLRRVRDIV 328
Cdd:cd14534    73 ---KSANTSTSSPTVSSSETSssleqekyLSALVlyvlgEKSQMKGVKAE-SDPKCEFIPVEYPEVRQVKASFKKLLRAC 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 329 YPHV----EEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRTAQLTTLAMLMLDGFYRSIEGFE 404
Cdd:cd14534   149 VPSSaptePEQSFLKAVEDSEWLQQLQCLMQLSGAVVDLLDVQGSSVLLCLEDGWDVTTQVSSLSQLLLDPYYRTLEGFR 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2173616156 405 ILVQKEWISFGHKFSSRiGHGDKNHADADRSPIFLQFIDCVWQMTKQ 451
Cdd:cd14534   229 VLVEKEWLAFGHRFSHR-SNLTAASQSSGFAPVFLQFLDAVHQIHRQ 274
PH-GRAM_MTMR2_insect-like cd13357
Myotubularian related 2 protein (MTMR2) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 47-143 6.84e-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 Drosophila, sea urchins, mosquitos, bees, ticks, and anemones.


Pssm-ID: 270164  Cd Length: 100  Bit Score: 165.37  E-value: 6.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  47 KEVIYICPFSGPVKGRLYITNYRLYLRSLETDLAPILDVPLGVISRIEKMGGVTSRGENSYGLDITCKDLRNLRFALKQE 126
Cdd:cd13357     4 KDVTYLCPFRGPVRGTLTITNYKLYFKSLDREPPFTVEVPLGVIYRVEKVGGATSRGENSYGLEIFCKDMRNLRFAHKQE 83

                          90
                  ....*....|....*..
gi 2173616156 127 GHSRRDIFDVLTRHAFP 143
Cdd:cd13357    84 NHSRRLVFEKLQAYAFP 100
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 183-451 1.34e-44

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: 160.47  E-value: 1.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 183 WRISFVNQRYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENRAAIMRC----SQPLVGV--------- 249
Cdd:cd14589     1 FRITAVNRMYSLCRSYPGLLVVPQSVQDSSLQKVARCYRHNRLPVVCWKNSKTKAVLLRSggfhGKGVVGLfksqnphsa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 250 -----GGKRSRDDERYLDIIRETNKQTSKLT---------IYDARPGVNAVANKATGGGYEGEDAYpHAELSFLDIHNIH 315
Cdd:cd14589    81 apassESSSSIEQEKYLQALLNAISVHQKMNgnstllqsqLLKRQAALYIFGEKSQLRGFKLDFAL-NCEFVPVEFHDIR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 316 VMRESLRRV-RDIV---YPHVEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGlSSVLVHCSDGWDRTAQLTTLAML 391
Cdd:cd14589   160 QVKASFKKLmRACVpstIPTDSEVTFLKALGESEWFLQLHRIMQLAVVISELLESG-SSVMVCLEDGWDITTQVVSLVQL 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 392 MLDGFYRSIEGFEILVQKEWISFGHKFSSRiGHGDKNHADADRSPIFLQFIDCVWQMTKQ 451
Cdd:cd14589   239 LSDPFYRTLEGFQMLVEKEWLSFGHKFSQR-SNLTPNSQGSGFAPIFLQFLDCVHQIHNQ 297
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 183-451 7.62e-44

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: 158.21  E-value: 7.62e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 183 WRISFVNQRYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENRAAIMRC-------------SQPLVGV 249
Cdd:cd14588     1 FRISTVNRMYAVCRSYPGLLIVPQSIQDNTIQRISRCYRQNRFPVVCWRNSRTKAVLLRSgglhgkgvvglfkSQNAPAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 250 GGKR----SRDDERYLDIIRET----NKQTSKLTIYDARPGVNAVANKATGGGYEgEDAYPHAELSFLDIHNIHVMRESL 321
Cdd:cd14588    81 GQSQtdstSLEQEKYLQAVINSmpryADASGRNTLSGFRAALYIIGDKSQLKGVK-QDPLQQWEVVPIEVFDVRQVKASF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 322 RRVRDIVYPHV----EEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGlSSVLVHCSDGWDRTAQLTTLAMLMLDGFY 397
Cdd:cd14588   160 KKLMKACVPSCpstdPSQTYLRTLEESEWLSQLHKLLQVSVLVVELLDSG-SSVLVSLEDGWDITTQVVSLVQLLSDPYY 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2173616156 398 RSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADAdRSPIFLQFIDCVWQMTKQ 451
Cdd:cd14588   239 RTIEGFRLLVEKEWLSFGHRFSHRGAQTLASQSSG-FTPVFLQFLDCVHQIHLQ 291
PH-GRAM_MTMR2_mammal-like cd13356
Myotubularian related 2 protein (MTMR2) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 36-145 2.05e-42

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: 148.30  E-value: 2.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  36 PRLPGESaITD--KEVIYICPFSGPVKGRLYITNYRLYLRSLETDLAPILDVPLGVISRIEKMGGVTSRGENSYGLDITC 113
Cdd:cd13356     5 PLLPGEN-IKDmaKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVINRVEKIGGASSRGENSYGLETVC 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2173616156 114 KDLRNLRFALKQEGHSRRDIFDVLTRHAFPLA 145
Cdd:cd13356    84 KDIRNLRFAHKPEGRTRRSIFENLMKYAFPVS 115
PH-GRAM_MTMR1 cd13358
Myotubularian related 1 protein (MTMR1) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 47-143 5.83e-38

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: 135.42  E-value: 5.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  47 KEVIYICPFSGPVKGRLYITNYRLYLRSLETDLAPILDVPLGVISRIEKMgGVTSRGENSYGLDITCKDLRNLRFALKQE 126
Cdd:cd13358     5 KDVMYICPFMGAVSGTLTVTDFKMYFKNVERDPPFILDVPLGVISRVEKI-GVQSHGDNSCGIEIVCKDMRNLRLAYKQE 83

                          90
                  ....*....|....*..
gi 2173616156 127 GHSRRDIFDVLTRHAFP 143
Cdd:cd13358    84 EQSKLEIFENLNKHAFP 100
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 223-447 4.05e-33

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: 125.53  E-value: 4.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 223 NRIPVLSWIHPeNRAAIMRCSQpLVGVGGKRsRDDERYLDIIRETNKQTSKLTIYDarPGVNavankatgggyegedayp 302
Cdd:cd14537     1 GRPPVWCWSHP-NGAALVRMAE-LLPTITDR-TQENKMLEAIRKSHPNLKKPKVID--LDKL------------------ 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 303 haelsFLDIHNIHVmreSLRRVRDIVYPHVEEA------HWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCS 376
Cdd:cd14537    58 -----LPSLQDVQA---AYLKLRELCTPDSSEQfwvqdsKWYSLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQES 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2173616156 377 DGWDRTAQLTTLAMLMLDGFYRSIEGFEILVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQ 447
Cdd:cd14537   130 DGRDLSCVVSSLVQLLLDPHFRTITGFQSLIQKEWVALGHPFCDRLGHVKPNKTESEESPVFLLFLDCVWQ 200
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 332-448 2.44e-27

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: 109.15  E-value: 2.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 332 VEEAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRTAQLTTLAMLMLDGFYRSIEGFEILVQKEW 411
Cdd:cd14595    81 VSDEKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEW 160

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2173616156 412 ISFGHKFSSRIG-HGDknhADADRSPIFLQFIDCVWQM 448
Cdd:cd14595   161 VVAGHPFLQRLNlTRE---SDKEESPVFLLFLDCVWQL 195
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 224-447 7.32e-25

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: 102.28  E-value: 7.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 224 RIPVLSWIHPeNRAAIMRCSqpLVGVGGKRSRDDERYLDIIRETNKQTSkltiydarpgvnavankatgggyegeDAYPh 303
Cdd:cd14593     2 RIPLWCWNHP-NGSALVRMA--NIKDLLQQRKIDQRICNAITRSHPLRS--------------------------DVYK- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 304 aelSFLD--IHNIHVMRESLRRVRD--IVYPHVE-EAHWLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDG 378
Cdd:cd14593    52 ---SDLDktLPNIQEIQAAFVKLKQlcVNEPFEEtEEKWLSSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEG 128

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2173616156 379 WDRTAQLTTLAMLMLDGFYRSIEGFEILVQKEWISFGHKFSSRIGHGDKnhADADRSPIFLQFIDCVWQ 447
Cdd:cd14593   129 RDLSCVVASLVQVMLDPYFRTITGFQSLIQKEWVMAGYRFLDRCNHLKK--SSKKESPLFLLFLDCVWQ 195
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 337-448 4.15e-24

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: 100.30  E-value: 4.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 337 WLSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRTAQLTTLAMLMLDGFYRSIEGFEILVQKEWISFGH 416
Cdd:cd14594    94 WFSSLESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQSLIQKEWVMGGH 173

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2173616156 417 KFSSRIGHGDKNhaDADRSPIFLQFIDCVWQM 448
Cdd:cd14594   174 CFLDRCNHLRQN--DKEEVPVFLLFLDCVWQL 203
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 38-143 4.19e-17

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 77.41  E-value: 4.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  38 LPGESAITDkeviYICPFS---GPVKGRLYITNYRLYLRSLETDLAPILDVPLGVISRIEKMGGVTSRGENSYGLDITCK 114
Cdd:pfam02893  10 PPEERLIAS----YSCYLNrdgGPVQGRLYLTNYRLCFRSLPKGWSTKVVIPLVDIEEIEKLKGGANLFPNGIQVETGSN 85

                          90       100
                  ....*....|....*....|....*....
gi 2173616156 115 DlrNLRFALKQEGHSRRDIFDVLTRHAFP 143
Cdd:pfam02893  86 D--KFSFAGFVTRDEAIEFILALLKNAHP 112
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 47-137 2.48e-14

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: 68.95  E-value: 2.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  47 KEVIYICPFSGPVKGRLYITNYRLYLRSLETDLAPILDVPLGVISRIEKMGGVTSrgeNSYGLDITCKDLRNLRFALKQE 126
Cdd:cd10570     7 RFCCALRPRKLPLEGTLYLSTYRLIFSSKADGDETKLVIPLVDITDVEKIAGASF---LPSGLIITCKDFRTIKFSFDSE 83

                          90
                  ....*....|.
gi 2173616156 127 GHSRRDIFDVL 137
Cdd:cd10570    84 DEAVKVIARVL 94
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
38-97 8.75e-12

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 60.30  E-value: 8.75e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2173616156   38 LPGESAITDkeviYICPFS--GPVKGRLYITNYRLYLRSLETDLAPILDVPLGVISRIEKMG 97
Cdd:smart00568   3 PEEEKLIAD----YSCYLSrtGPVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIEKST 60
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
357-471 6.30e-06

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 45.04  E-value: 6.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  357 AIRVADKVASGLSSVLVHCSDGWDRTAQLTTLAMLMLdgfyrsiegfeilvqkewisfghkfssrighgdknhaDADRSP 436
Cdd:smart00404  28 AVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQ-------------------------------------QLEAEA 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2173616156  437 IFLQFIDCVWQMTKQFPTAFEFNECFLVAILDHLY 471
Cdd:smart00404  71 GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 357-471 6.30e-06

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 [Multi-domain]  Cd Length: 105  Bit Score: 45.04  E-value: 6.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  357 AIRVADKVASGLSSVLVHCSDGWDRTAQLTTLAMLMLdgfyrsiegfeilvqkewisfghkfssrighgdknhaDADRSP 436
Cdd:smart00012  28 AVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQ-------------------------------------QLEAEA 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2173616156  437 IFLQFIDCVWQMTKQFPTAFEFNECFLVAILDHLY 471
Cdd:smart00012  71 GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PH-like cd00900
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 49-137 9.47e-05

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.


Pssm-ID: 275390  Cd Length: 89  Bit Score: 41.23  E-value: 9.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156  49 VIYICPFSGPVKGRLYITNYRLYLRSlETDLAPILDVPLGVISRIEkmggVTSRGENSYGLDITCKDLRN-LRFALKQEG 127
Cdd:cd00900     6 VRVYREPTKRVEGTLYITSDRLILRD-KNDGGLELSIPISDIVNVN----VSPQGPSSRYLVLVLKDRGEfVGFSFPKEE 80

                          90
                  ....*....|
gi 2173616156 128 HSRRdIFDVL 137
Cdd:cd00900    81 DAIE-ISDAL 89
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 334-422 1.13e-04

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.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 41.95  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173616156 334 EAHW--LSSLESTHWLEHIKLLLTGAIRVADKVASGLSSVLVHCSDGWDRTAQLTTLAMLMLDGFyrsieGFEILVQKEW 411
Cdd:cd14494    20 EADSrfLKQLGVTTIVDLTLAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVR 94

                          90
                  ....*....|.
gi 2173616156 412 ISFGHKFSSRI 422
Cdd:cd14494    95 LIRPGGIPQTI 105
 
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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