NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17737395|ref|NP_523489|]
View 

myotubularin, isoform A [Drosophila melanogaster]

Protein Classification

myotubularin family protein( domain architecture ID 10193449)

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)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 184-509 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: 570.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395   184 DGWAVYEPLAELRRLGVPN-DMWRATKLNESYAICDSYPAVWAVPKAASDDFLRRVAQFRSRCRLPVLSWMNPRTQATIT 262
Cdd:pfam06602   3 NGWDLYDPEAEFARQGLPSkDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVIT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395   263 RCSQPLVGVSGKRNSDDEAYLSFIMEANA--QSDKLTIMDARPSANAIANKAKGGGYESEDAYKNVEINFLDIHNIHVMR 340
Cdd:pfam06602  83 RSSQPLVGLNGKRSIEDEKLLQAIFKSSNpySAKKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395   341 ESLRKVKEACFPTT-DDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRTAQLTALSMLLLDPHY 419
Cdd:pfam06602 163 DSLNKLVEACNDRSpSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYY 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395   420 RTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDADRSPVFLQFIDSVWQVSQQFNNAFEFNEHFLITIVDHLYSCRFGT 499
Cdd:pfam06602 243 RTIEGFQVLIEKEWLSFGHKFADRCGHLAGFTDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGT 322

                         330
                  ....*....|
gi 17737395   500 FLCNTEAERV 509
Cdd:pfam06602 323 FLCNSEKERV 332
PH-GRAM_MTMR2_insect-like cd13357
Myotubularian related 2 protein (MTMR2) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 57-159 4.17e-67

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: 213.90  E-value: 4.17e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395  57 DQKNDVTYVCPYRGPVFGALTITNYRLYFRSLplrDQEPPVVVDVPLGVIARVEKIGGATSRGENSYGIEIFCKDMRNLR 136
Cdd:cd13357   1 AIAKDVTYLCPFRGPVRGTLTITNYKLYFKSL---DREPPFTVEVPLGVIYRVEKVGGATSRGENSYGLEIFCKDMRNLR 77

                        90       100
                ....*....|....*....|...
gi 17737395 137 FAHKQQNHSRRTVFEKLQANAFP 159
Cdd:cd13357  78 FAHKQENHSRRLVFEKLQAYAFP 100
 
Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 184-509 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: 570.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395   184 DGWAVYEPLAELRRLGVPN-DMWRATKLNESYAICDSYPAVWAVPKAASDDFLRRVAQFRSRCRLPVLSWMNPRTQATIT 262
Cdd:pfam06602   3 NGWDLYDPEAEFARQGLPSkDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVIT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395   263 RCSQPLVGVSGKRNSDDEAYLSFIMEANA--QSDKLTIMDARPSANAIANKAKGGGYESEDAYKNVEINFLDIHNIHVMR 340
Cdd:pfam06602  83 RSSQPLVGLNGKRSIEDEKLLQAIFKSSNpySAKKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395   341 ESLRKVKEACFPTT-DDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRTAQLTALSMLLLDPHY 419
Cdd:pfam06602 163 DSLNKLVEACNDRSpSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYY 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395   420 RTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDADRSPVFLQFIDSVWQVSQQFNNAFEFNEHFLITIVDHLYSCRFGT 499
Cdd:pfam06602 243 RTIEGFQVLIEKEWLSFGHKFADRCGHLAGFTDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGT 322

                         330
                  ....*....|
gi 17737395   500 FLCNTEAERV 509
Cdd:pfam06602 323 FLCNSEKERV 332
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
 245-493 0e+00

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: 532.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 245 CRLPVLSWMNPRTQATITRCSQPLVGVSGKRNSDDEAYLSFIMEANAQSDKLTIMDARPSANAIANKAKGGGYESEDAYK 324
Cdd:cd14535   1 NRIPVLSWIHPESQATITRCSQPLVGVSGKRSKDDEKYLQLIMDANAQSHKLFIMDARPSVNAVANKAKGGGYESEDAYQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 325 NVEINFLDIHNIHVMRESLRKVKEACFPTTDDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRT 404
Cdd:cd14535  81 NAELVFLDIHNIHVMRESLRKLKDICFPNIDDSHWLSNLESTHWLEHIKLILAGAVRIADKVESGKTSVVVHCSDGWDRT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 405 AQLTALSMLLLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDADRSPVFLQFIDSVWQVSQQFNNAFEFNEHF 484
Cdd:cd14535 161 AQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGHGDKNHSDADRSPVFLQFIDCVWQMTRQFPNAFEFNEHF 240


                ....*....
gi 17737395 485 LITIVDHLY 493
Cdd:cd14535 241 LITILDHLY 249
PH-GRAM_MTMR2_insect-like cd13357
Myotubularian related 2 protein (MTMR2) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 57-159 4.17e-67

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: 213.90  E-value: 4.17e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395  57 DQKNDVTYVCPYRGPVFGALTITNYRLYFRSLplrDQEPPVVVDVPLGVIARVEKIGGATSRGENSYGIEIFCKDMRNLR 136
Cdd:cd13357   1 AIAKDVTYLCPFRGPVRGTLTITNYKLYFKSL---DREPPFTVEVPLGVIYRVEKVGGATSRGENSYGLEIFCKDMRNLR 77

                        90       100
                ....*....|....*....|...
gi 17737395 137 FAHKQQNHSRRTVFEKLQANAFP 159
Cdd:cd13357  78 FAHKQENHSRRLVFEKLQAYAFP 100
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 41-159 1.34e-21

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: 90.12  E-value: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395    41 ILRDTPFGYLEGEEDQDqkndvTYVCPY---RGPVFGALTITNYRLYFRSLPLrdqEPPVVVDVPLGVIARVEKIGGATS 117
Cdd:pfam02893   1 ELFRKKFKLPPEERLIA-----SYSCYLnrdGGPVQGRLYLTNYRLCFRSLPK---GWSTKVVIPLVDIEEIEKLKGGAN 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 17737395   118 RGENSYGIEIFCKDmrNLRFAHKQQNHSRRTVFEKLQANAFP 159
Cdd:pfam02893  73 LFPNGIQVETGSND--KFSFAGFVTRDEAIEFILALLKNAHP 112
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
48-113 3.69e-13

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 64.15  E-value: 3.69e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17737395     48 GYLEGEEDQDqkndvTYVCPY--RGPVFGALTITNYRLYFRSLPLRDqepPVVVDVPLGVIARVEKIG 113
Cdd:smart00568   1 KLPEEEKLIA-----DYSCYLsrTGPVQGRLYISNYRLCFRSNLPGK---LTKVVIPLADITRIEKST 60
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
379-493 5.00e-08

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 51.21  E-value: 5.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395    379 AVRIVDKVETM---STSVVVHCSDGWDRTAQLTALSMLLLDPHYRTvrgfevliekewlsfghkfqqrighgdnkhsdad 455
Cdd:smart00404  25 LLRAVKKNLNQsesSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA---------------------------------- 70

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 17737395    456 rspVFLQFIDSVWQVSQQFNNAFEFNEHFLITIVDHLY 493
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 ...
 184-509 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: 570.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395   184 DGWAVYEPLAELRRLGVPN-DMWRATKLNESYAICDSYPAVWAVPKAASDDFLRRVAQFRSRCRLPVLSWMNPRTQATIT 262
Cdd:pfam06602   3 NGWDLYDPEAEFARQGLPSkDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVIT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395   263 RCSQPLVGVSGKRNSDDEAYLSFIMEANA--QSDKLTIMDARPSANAIANKAKGGGYESEDAYKNVEINFLDIHNIHVMR 340
Cdd:pfam06602  83 RSSQPLVGLNGKRSIEDEKLLQAIFKSSNpySAKKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395   341 ESLRKVKEACFPTT-DDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRTAQLTALSMLLLDPHY 419
Cdd:pfam06602 163 DSLNKLVEACNDRSpSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYY 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395   420 RTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDADRSPVFLQFIDSVWQVSQQFNNAFEFNEHFLITIVDHLYSCRFGT 499
Cdd:pfam06602 243 RTIEGFQVLIEKEWLSFGHKFADRCGHLAGFTDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGT 322

                         330
                  ....*....|
gi 17737395   500 FLCNTEAERV 509
Cdd:pfam06602 323 FLCNSEKERV 332
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
 245-493 0e+00

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: 532.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 245 CRLPVLSWMNPRTQATITRCSQPLVGVSGKRNSDDEAYLSFIMEANAQSDKLTIMDARPSANAIANKAKGGGYESEDAYK 324
Cdd:cd14535   1 NRIPVLSWIHPESQATITRCSQPLVGVSGKRSKDDEKYLQLIMDANAQSHKLFIMDARPSVNAVANKAKGGGYESEDAYQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 325 NVEINFLDIHNIHVMRESLRKVKEACFPTTDDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRT 404
Cdd:cd14535  81 NAELVFLDIHNIHVMRESLRKLKDICFPNIDDSHWLSNLESTHWLEHIKLILAGAVRIADKVESGKTSVVVHCSDGWDRT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 405 AQLTALSMLLLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDADRSPVFLQFIDSVWQVSQQFNNAFEFNEHF 484
Cdd:cd14535 161 AQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGHGDKNHSDADRSPVFLQFIDCVWQMTRQFPNAFEFNEHF 240


                ....*....
gi 17737395 485 LITIVDHLY 493
Cdd:cd14535 241 LITILDHLY 249
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 232-493 3.45e-163

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: 466.82  E-value: 3.45e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 232 DDFLRRVAQFRSRCRLPVLSWMNPRTQATITRCSQPLVGVSGKRNSDDEAYLSFIMEANAQSDKLTIMDARPSANAIANK 311
Cdd:cd14590   1 DEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFDARPSVNAVANK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 312 AKGGGYESEDAYKNVEINFLDIHNIHVMRESLRKVKEACFPTTDDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMST 391
Cdd:cd14590  81 AKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEESHWLSNLESTHWLEHIKLILAGALRIADKVESGKT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 392 SVVVHCSDGWDRTAQLTALSMLLLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDADRSPVFLQFIDSVWQVS 471
Cdd:cd14590 161 SVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVFLQFIDCVWQMT 240

                       250       260
                ....*....|....*....|..
gi 17737395 472 QQFNNAFEFNEHFLITIVDHLY 493
Cdd:cd14590 241 RQFPTAFEFNEYFLITILDHLY 262
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
 245-493 3.46e-149

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: 430.60  E-value: 3.46e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 245 CRLPVLSWMNPRTQATITRCSQPLVGVSGKRNSDDEAYLSFIMEANAQSDKLTIMDARPSANAIANKAKGGGYESEDAYK 324
Cdd:cd14591   1 NRIPVLSWIHPENQAVIMRCSQPLVGMSGKRNKDDEKYLDIIREANGQTSKLTIYDARPSVNAVANKATGGGYEGDDAYQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 325 NVEINFLDIHNIHVMRESLRKVKEACFPTTDDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRT 404
Cdd:cd14591  81 NAELVFLDIHNIHVMRESLKKLKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWDRT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 405 AQLTALSMLLLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDADRSPVFLQFIDSVWQVSQQFNNAFEFNEHF 484
Cdd:cd14591 161 AQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGHGDKNHADADRSPIFLQFIDCVWQMSKQFPTAFEFNEQF 240


                ....*....
gi 17737395 485 LITIVDHLY 493
Cdd:cd14591 241 LITILDHLY 249
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 246-493 4.91e-144

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: 417.46  E-value: 4.91e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 246 RLPVLSWMNPRTQATITRCSQPLVGVSGKRNSDDEAYLSFIMEANAQSDKLTIMDARPSANAIANKAKGGGYESEDAYKN 325
Cdd:cd14592   2 RVPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYLQTIMDANAQSHKLIIFDARQNSVADTNKTKGGGYESESAYPN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 326 VEINFLDIHNIHVMRESLRKVKEACFPTTDDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRTA 405
Cdd:cd14592  82 AELVFLEIHNIHVMRESLRKLKEIVYPSIDEARWLSNVDGTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGWDRTA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 406 QLTALSMLLLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDADRSPVFLQFIDSVWQVSQQFNNAFEFNEHFL 485
Cdd:cd14592 162 QLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGHGDDNHADADRSPIFLQFIDCVWQMTRQFPSAFEFNELFL 241


                ....*...
gi 17737395 486 ITIVDHLY 493
Cdd:cd14592 242 ITILDHLY 249
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 193-494 2.81e-140

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: 409.81  E-value: 2.81e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 193 AELRRLGVPNDMWRATKLNESYAICDSYPAVWAVPKAASDDFLRRVAQFRSRCRLPVLSWMNPRTQATITRCSQPLVGVS 272
Cdd:cd14532   3 SEYTRMGVPNDNWTLSDINKDYELCDTYPRELFVPTSASTPVLVGSSKFRSKGRLPVLSYLHKDNQAAICRCSQPLSGFS 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 273 GkRNSDDEAYLSFIMEANAQSDKLTIMDARPSANAIANKAKGGGYESEDAYKNVEINFLDIHNIHVMRESLRKVKEAC-F 351
Cdd:cd14532  83 A-RCVEDEQLLQAIRKANPNSKFMYVVDTRPKINAMANKAAGKGYENEDNYSNIKFQFFGIENIHVMRSSLQKLLEVCeL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 352 PTTDDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETmSTSVVVHCSDGWDRTAQLTALSMLLLDPHYRTVRGFEVLIEK 431
Cdd:cd14532 162 KNPSMSAFLSGLESSGWLKHIKAVMDTSVFIAKAVSE-GASVLVHCSDGWDRTAQTCSLASLLLDPYYRTIKGFQVLIEK 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17737395 432 EWLSFGHKFQQRIGH--GDNKhsdaDRSPVFLQFIDSVWQVSQQFNNAFEFNEHFLITIVDHLYS 494
Cdd:cd14532 241 EWLSFGHKFTDRCGHlqGDAK----EVSPVFTQFLDCVWQLMQQFPRAFEFNERFLLTLHDHVYS 301
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
 245-469 2.29e-138

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: 401.93  E-value: 2.29e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 245 CRLPVLSWMNPRTQATITRCSQPLVGVSGKRNSDDEAYLSFIMEANAQSDKLTIMDARPSANAIANKAKGGGYESEDAYK 324
Cdd:cd14507   1 GRIPVLSWRHPRNGAVICRSSQPLVGLTGSRSKEDEKLLNAIRKASPSSKKLYIVDARPKLNAVANRAKGGGYENTEYYP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 325 NVEINFLDIHNIHVMRESLRKVKEACFPTTD-DSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDR 403
Cdd:cd14507  81 NCELEFLNIENIHAMRDSLNKLRDACLSPNDeESNWLSALESSGWLEHIRLILKGAVRVADLLEKEGTSVLVHCSDGWDR 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17737395 404 TAQLTALSMLLLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDADRSPVFLQFIDSVWQ 469
Cdd:cd14507 161 TSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDKNSSDEERSPIFLQFLDCVWQ 226
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 185-494 1.81e-114

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: 344.16  E-value: 1.81e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 185 GWAVYEPLAELRRLGVPNDMWRATKLNESYAICDSYPAVWAVPKAASDDFLRRVAQFRSRCRLPVLSWMNPRTQATITRC 264
Cdd:cd14584   1 GWKLIDLKVDFQRMGIPNDYWEITDANKNYEICSTYPPELVVPKSASKATVVGSSKFRSRGRFPVLSYLYKENNAAICRC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 265 SQPLVGVSGkRNSDDEAYLSFIMEANAQSDKLTIMDARPSANAIANKAKGGGYESEDAYKNVEINFLDIHNIHVMRESLR 344
Cdd:cd14584  81 SQPLSGFSA-RCVEDEQMLQAISKANPGSPFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIRFQFIGIENIHVMRSSLQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 345 KVKEAC-FPTTDDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRTAQLTALSMLLLDPHYRTVR 423
Cdd:cd14584 160 KLLEVCeMKSPSMSDFLTGLENSGWLRHIKAVMDAGVFLAKAVKEEKASVLVHCSDGWDRTAQVCSLASLLLDPFYRTIK 239

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17737395 424 GFEVLIEKEWLSFGHKFQQRIGH--GDNKhsdaDRSPVFLQFIDSVWQVSQQFNNAFEFNEHFLITIVDHLYS 494
Cdd:cd14584 240 GLMVLIEKEWISMGHKFSQRCGHldGDPK----EVSPVFTQFLECVWQLMEQFPCAFEFNEHFLLEIHDHVFS 308
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 193-494 2.21e-108

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: 328.46  E-value: 2.21e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 193 AELRRLGVPNDMWRATKLNESYAICDSYPAVWAVPKAASDDFLRRVAQFRSRCRLPVLSWMNPRTQATITRCSQPLVGVS 272
Cdd:cd14583   3 AEYNRMGLPNSLWQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYYCKDNNASICRSSQPLSGFS 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 273 GkRNSDDEAYLSFIMEANAQSDKLTIMDARPSANAIANKAKGGGYESEDAYKNVEINFLDIHNIHVMRESLRKVKEAC-- 350
Cdd:cd14583  83 A-RCLEDEQMLQAIRKANPGSDFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCel 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 351 -FPTTDDSKWqtAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRTAQLTALSMLLLDPHYRTVRGFEVLI 429
Cdd:cd14583 162 rSPSMGDFLW--GLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLI 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17737395 430 EKEWLSFGHKFQQRIGHGDNKHSDAdrSPVFLQFIDSVWQVSQQFNNAFEFNEHFLITIVDHLYS 494
Cdd:cd14583 240 EKDWVSFGHKFNHRYGHLDGDPKEV--SPVIDQFIECVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 193-494 5.55e-106

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: 322.26  E-value: 5.55e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 193 AELRRLGVPNDMWRATKLNESYAICDSYPAVWAVPKAASDDFLRRVAQFRSRCRLPVLSWMNPRTQATITRCSQPLVGVS 272
Cdd:cd14585   3 EEYKRMGVPNDYWQLSDVNRDYKICDTYPRDLYVPITASKPIIVGSSKFRSKGRFPVLSYYHQEKKAAICRCSQPLSGFS 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 273 GkRNSDDEAYLSFIMEANAQSDKLTIMDARPSANAIANKAKGGGYESEDAYKNVEINFLDIHNIHVMRESLRKVKEAC-- 350
Cdd:cd14585  83 A-RCLEDEHMLQAISKANPNNRYMYVMDTRPKLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVCgt 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 351 --FPTTDdskWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRTAQLTALSMLLLDPHYRTVRGFEVL 428
Cdd:cd14585 162 kaLSVND---FLSGLESSGWLRHIKAVLDAAVFLAKAVAVEGASVLVHCSDGWDRTAQVCSLGSLLLDPYYRTIKGFMVL 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17737395 429 IEKEWLSFGHKFQQRIGH--GDNKhsdaDRSPVFLQFIDSVWQVSQQFNNAFEFNEHFLITIVDHLYS 494
Cdd:cd14585 239 IEKDWISFGHKFSDRCGQldGDPK----EISPVFTQFLECVWQLTEQFPRAFEFSEAFLLQIHEHIHS 302
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 203-469 2.90e-82

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: 261.12  E-value: 2.90e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 203 DMWRATKLNESYAICDSYPAVWAVPKAASDDFLRRVAQFRSRCRLPVLSWMNPRTQATITRCSQPLVGVSGKRNSDDEAY 282
Cdd:cd14587   1 NVWRVSEINSNYKLCSSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAVIARCSQPEISWWGWRNADDEYL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 283 LSFIMEA-----------------------NAQSD------------------KLTIMDARPSANAIANKAKGGGYESED 321
Cdd:cd14587  81 VTSIAKAcaldpgtrapggspskgnsdgsdASDTDfdssltacsavesgaapqKLLILDARSYTAAVANRAKGGGCECEE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 322 AYKNVEINFLDIHNIHVMRESLRKVKEACFPTTDDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGW 401
Cdd:cd14587 161 YYPNCEVMFMGMANIHSIRNSFQYLRAVCSQMPDPGNWLSALESTKWLQHLSVMLKAAVLVASAVDREGRPVLVHCSDGW 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17737395 402 DRTAQLTALSMLLLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDADRSPVFLQFIDSVWQ 469
Cdd:cd14587 241 DRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHQENVEDQNEQCPVFLQWLDCVHQ 308
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 202-469 6.88e-81

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: 257.64  E-value: 6.88e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 202 NDMWRATKLNESYAICDSYPAVWAVPKAASDDFLRRVAQFRSRCRLPVLSWMNPRTQATITRCSQPLVGVSGKRNSDDEA 281
Cdd:cd14586   5 QNAWRISNINEKYKLCGSYPQELIVPAWITDKELESVASFRSWKRIPAVVYRHQSNGAVIARCGQPEVSWWGWRNADDEH 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 282 YLSFIMEANA---------------------------------------------QSDKLTIMDARPSANAIANKAKGGG 316
Cdd:cd14586  85 LVQSVAKACAsdssscksvlmtgncsrdfpnggdlsdvefdssmsnasgveslaiQPQKLLILDARSYAAAVANRAKGGG 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 317 YESEDAYKNVEINFLDIHNIHVMRESLRKVKEACFPTTDDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVH 396
Cdd:cd14586 165 CECPEYYPNCEVVFMGMANIHSIRKSFQSLRLLCTQMPDPANWLSALESTKWLQHLSMLLKSALLVVHAVDRDQRPVLVH 244

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17737395 397 CSDGWDRTAQLTALSMLLLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDADRSPVFLQFIDSVWQ 469
Cdd:cd14586 245 CSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRCGHGENSDDLNERCPVFLQWLDCVHQ 317
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 246-469 4.12e-80

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: 252.32  E-value: 4.12e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 246 RLPVLSWMNPRTQATITRCSQPLVGVSGKRNSDDEAYLSFIMEA---NAQSDKLTIMDARPSANAIANKAKGGGYESEDA 322
Cdd:cd14533   3 RIPSVVWRHQRNGAVIARCSQPEVGWLGWRNAEDENLLQAIAEAcasNASPKKLLIVDARSYAAAVANRAKGGGCECPEY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 323 YKNVEINFLDIHNIHVMRESLRKVKEACFPTTDDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWD 402
Cdd:cd14533  83 YPNCEVVFMNLANIHAIRKSFHSLRALCSSAPDQPNWLSNLESTKWLHHLSGLLKAALLVVNAVDEEGRPVLVHCSDGWD 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17737395 403 RTAQLTALSMLLLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDADRSPVFLQFIDSVWQ 469
Cdd:cd14533 163 RTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFGHKFADRCGHGVNSEDINERCPVFLQWLDCVHQ 229
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
 246-469 5.19e-77

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: 244.28  E-value: 5.19e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 246 RLPVLSWMNPRTQATITRCSQPLVGVSGKRNSDDEAYLSFIMEANAQSDKLT-----IMDARPSANAIANKAKGGGYESE 320
Cdd:cd17666   2 RIPVLTYLHKANGCSITRSSQPLVGLKQNRSIQDEKLVSEIFNTSINEIYISpqknlIVDARPTTNAMAQVALGAGTENM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 321 D--AYKNVEINFLDIHNIHVMRESLRKVKEAcFPTTDDSKW-----QTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSV 393
Cdd:cd17666  82 DnyKYKTAKKIYLGIDNIHVMRDSLNKVTEA-LKDGDDSNPsypplINALKKSNWLKYLAIILQGADLIAKSIHFNHSHV 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17737395 394 VVHCSDGWDRTAQLTALSMLLLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHgdnkhsdADRSPVFLQFIDSVWQ 469
Cdd:cd17666 161 LIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFAERSGH-------KETSPVFHQFLDCVYQ 229
PH-GRAM_MTMR2_insect-like cd13357
Myotubularian related 2 protein (MTMR2) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 57-159 4.17e-67

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: 213.90  E-value: 4.17e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395  57 DQKNDVTYVCPYRGPVFGALTITNYRLYFRSLplrDQEPPVVVDVPLGVIARVEKIGGATSRGENSYGIEIFCKDMRNLR 136
Cdd:cd13357   1 AIAKDVTYLCPFRGPVRGTLTITNYKLYFKSL---DREPPFTVEVPLGVIYRVEKVGGATSRGENSYGLEIFCKDMRNLR 77

                        90       100
                ....*....|....*....|...
gi 17737395 137 FAHKQQNHSRRTVFEKLQANAFP 159
Cdd:cd13357  78 FAHKQENHSRRLVFEKLQAYAFP 100
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 205-473 2.14e-62

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: 207.60  E-value: 2.14e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 205 WRATKLNESYAICDSYPAVWAVPKAASDDFLRRVAQFRSRCRLPVLSWMNPRTQATITRCSQP-LVGVSGKRNSddeayl 283
Cdd:cd14534   1 FRISTANRDYSICRSYPALVVVPQSVSDESLRKVARCYRQGRFPVVTWRHPRTKALLLRSGGFhGKGVMGMLKS------ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 284 sfimeANAQSDKLTIMDARPSA--------NAIA-----NKAKGGGYESEdAYKNVEINFLDIHNIHVMRESLRKVKEAC 350
Cdd:cd14534  75 -----ANTSTSSPTVSSSETSSsleqekylSALVlyvlgEKSQMKGVKAE-SDPKCEFIPVEYPEVRQVKASFKKLLRAC 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 351 ----FPTTDDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRTAQLTALSMLLLDPHYRTVRGFE 426
Cdd:cd14534 149 vpssAPTEPEQSFLKAVEDSEWLQQLQCLMQLSGAVVDLLDVQGSSVLLCLEDGWDVTTQVSSLSQLLLDPYYRTLEGFR 228

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 17737395 427 VLIEKEWLSFGHKFQQRIGHGDNKHSDAdRSPVFLQFIDSVWQVSQQ 473
Cdd:cd14534 229 VLVEKEWLAFGHRFSHRSNLTAASQSSG-FAPVFLQFLDAVHQIHRQ 274
PH-GRAM_MTM-like cd13223
Myotubularian 1 and related proteins Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase; ...
 57-159 2.56e-59

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: 193.22  E-value: 2.56e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395  57 DQKNDVTYVCPYRGPVFGALTITNYRLYFRSlplRDQEPPVVVDVPLGVIARVEKIGGATSRGENSYGIEIFCKDMRNLR 136
Cdd:cd13223   1 LKEKDVTYLCPFRGPVRGTLYITNYRLYFKS---RDREPNFVLDVPLGVISRVEKVGGATSRGENSYGLEIHCKDMRNLR 77

                        90       100
                ....*....|....*....|...
gi 17737395 137 FAHKQQNHSRRTVFEKLQANAFP 159
Cdd:cd13223  78 FAHKQENHSRRKLYETLQKYAFP 100
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 246-469 2.95e-55

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: 187.16  E-value: 2.95e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 246 RLPVLSWMNPRTQATITRCSQPLVGVSGKRNSDDEAYLSFIMEANAQSdklTIMDARPSANAIANKAKGGGYESEDAYKN 325
Cdd:cd14536   2 RFPVLSYYHKKNGMVLMRSSQPLTGPNGKRCKEDEKLLNAVLGGGKRG---YIIDTRSKNVAQQARAKGGGFEPEAHYPQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 326 VEINFLDIHNIHVMRESLRKVKEACfptTDDS----KWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGW 401
Cdd:cd14536  79 WRRIHKPIERYNVLQESLIKLVEAC---NDQGhsmdKWLSKLESSNWLSHVKEILTTACLVAQCIDREGASVLVHGSEGM 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17737395 402 DRTAQLTALSMLLLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHS-DADRSPVFLQFIDSVWQ 469
Cdd:cd14536 156 DSTLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRCAKSAYSNSkQKFESPVFLLFLDCVWQ 224
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 205-473 2.04e-47

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: 168.56  E-value: 2.04e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 205 WRATKLNESYAICDSYPAVWAVPKAASDDFLRRVAQFRSRCRLPVLSWMNPRTQATITRC----SQPLVGVSGKRNS--- 277
Cdd:cd14589   1 FRITAVNRMYSLCRSYPGLLVVPQSVQDSSLQKVARCYRHNRLPVVCWKNSKTKAVLLRSggfhGKGVVGLFKSQNPhsa 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 278 -----------DDEAYLSFIMEANAQSDKL----TIMDA----RPSANAI-ANKAKGGGYESEDAYkNVEINFLDIHNIH 337
Cdd:cd14589  81 apassessssiEQEKYLQALLNAISVHQKMngnsTLLQSqllkRQAALYIfGEKSQLRGFKLDFAL-NCEFVPVEFHDIR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 338 VMRESLRKVKEAC----FPTTDDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMStSVVVHCSDGWDRTAQLTALSML 413
Cdd:cd14589 160 QVKASFKKLMRACvpstIPTDSEVTFLKALGESEWFLQLHRIMQLAVVISELLESGS-SVMVCLEDGWDITTQVVSLVQL 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 414 LLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDAdRSPVFLQFIDSVWQVSQQ 473
Cdd:cd14589 239 LSDPFYRTLEGFQMLVEKEWLSFGHKFSQRSNLTPNSQGSG-FAPIFLQFLDCVHQIHNQ 297
PH-GRAM_MTM1 cd13355
Myotubularian 1 protein (MTM1) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 61-159 6.85e-47

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: 160.02  E-value: 6.85e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395  61 DVTYVCPYRGPVFGALTITNYRLYFRSLplrDQEPPVVVDVPLGVIARVEKIGGATSRGENSYGIEIFCKDMRNLRFAHK 140
Cdd:cd13355   5 DVIYICPFNGPVKGRVYITNYRLYFKST---ESEPPVTLDVPLGVISRIEKMGGASSRGENSYGLDITCKDMRNLRFALK 81

                        90
                ....*....|....*....
gi 17737395 141 QQNHSRRTVFEKLQANAFP 159
Cdd:cd13355  82 QEGHSRRDIFEILTKYAFP 100
PH-GRAM_MTMR2_mammal-like cd13356
Myotubularian related 2 protein (MTMR2) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 50-161 2.52e-45

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: 156.39  E-value: 2.52e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395  50 LEGEEDQDQKNDVTYVCPYRGPVFGALTITNYRLYFRSLplrDQEPPVVVDVPLGVIARVEKIGGATSRGENSYGIEIFC 129
Cdd:cd13356   7 LPGENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSM---ERDPPFVLDASLGVINRVEKIGGASSRGENSYGLETVC 83

                        90       100       110
                ....*....|....*....|....*....|..
gi 17737395 130 KDMRNLRFAHKQQNHSRRTVFEKLQANAFPLS 161
Cdd:cd13356  84 KDIRNLRFAHKPEGRTRRSIFENLMKYAFPVS 115
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 205-473 4.42e-45

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: 162.06  E-value: 4.42e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 205 WRATKLNESYAICDSYPAVWAVPKAASDDFLRRVAQFRSRCRLPVLSWMNPRTQATITRC----SQPLVGVSGKRNS--- 277
Cdd:cd14588   1 FRISTVNRMYAVCRSYPGLLIVPQSIQDNTIQRISRCYRQNRFPVVCWRNSRTKAVLLRSgglhGKGVVGLFKSQNApaa 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 278 ----------DDEAYLSFIMEANAQ----SDKLTIMDARPSANAIANKAKGGGYESeDAYKNVEINFLDIHNIHVMRESL 343
Cdd:cd14588  81 gqsqtdstslEQEKYLQAVINSMPRyadaSGRNTLSGFRAALYIIGDKSQLKGVKQ-DPLQQWEVVPIEVFDVRQVKASF 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 344 RKVKEACFP---TTDDS-KWQTAIDNTLWLKHIRCILAGAVRIVDKVETMStSVVVHCSDGWDRTAQLTALSMLLLDPHY 419
Cdd:cd14588 160 KKLMKACVPscpSTDPSqTYLRTLEESEWLSQLHKLLQVSVLVVELLDSGS-SVLVSLEDGWDITTQVVSLVQLLSDPYY 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 17737395 420 RTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDAdRSPVFLQFIDSVWQVSQQ 473
Cdd:cd14588 239 RTIEGFRLLVEKEWLSFGHRFSHRGAQTLASQSSG-FTPVFLQFLDCVHQIHLQ 291
PH-GRAM_MTMR1 cd13358
Myotubularian related 1 protein (MTMR1) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 61-159 1.26e-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: 137.73  E-value: 1.26e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395  61 DVTYVCPYRGPVFGALTITNYRLYFRSLplrDQEPPVVVDVPLGVIARVEKIGgATSRGENSYGIEIFCKDMRNLRFAHK 140
Cdd:cd13358   6 DVMYICPFMGAVSGTLTVTDFKMYFKNV---ERDPPFILDVPLGVISRVEKIG-VQSHGDNSCGIEIVCKDMRNLRLAYK 81

                        90
                ....*....|....*....
gi 17737395 141 QQNHSRRTVFEKLQANAFP 159
Cdd:cd13358  82 QEEQSKLEIFENLNKHAFP 100
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 329-469 3.47e-34

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: 129.00  E-value: 3.47e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 329 NFLDIHNIHVmreSLRKVKEACFPTT------DDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWD 402
Cdd:cd14537  57 LLPSLQDVQA---AYLKLRELCTPDSseqfwvQDSKWYSLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQESDGRD 133

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17737395 403 RTAQLTALSMLLLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHGDNKHSDADRSPVFLQFIDSVWQ 469
Cdd:cd14537 134 LSCVVSSLVQLLLDPHFRTITGFQSLIQKEWVALGHPFCDRLGHVKPNKTESEESPVFLLFLDCVWQ 200
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 345-470 2.64e-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: 2.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 345 KVKEACFP----TTDDSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRTAQLTALSMLLLDPHYR 420
Cdd:cd14595  68 KLRTLCLPdisvSVSDEKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHAR 147

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17737395 421 TVRGFEVLIEKEWLSFGHKFQQRIGHgdNKHSDADRSPVFLQFIDSVWQV 470
Cdd:cd14595 148 TISGFQSLVQKEWVVAGHPFLQRLNL--TRESDKEESPVFLLFLDCVWQL 195
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 335-469 9.13e-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: 101.89  E-value: 9.13e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 335 NIHVMRESLRKVKEAC----FPTTDDsKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRTAQLTAL 410
Cdd:cd14593  60 NIQEIQAAFVKLKQLCvnepFEETEE-KWLSSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASL 138

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17737395 411 SMLLLDPHYRTVRGFEVLIEKEWLSFGHKFQQRIGHgdNKHSDADRSPVFLQFIDSVWQ 469
Cdd:cd14593 139 VQVMLDPYFRTITGFQSLIQKEWVMAGYRFLDRCNH--LKKSSKKESPLFLLFLDCVWQ 195
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 356-470 1.39e-23

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: 98.76  E-value: 1.39e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 356 DSKWQTAIDNTLWLKHIRCILAGAVRIVDKVETMSTSVVVHCSDGWDRTAQLTALSMLLLDPHYRTVRGFEVLIEKEWLS 435
Cdd:cd14594  91 DVKWFSSLESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQSLIQKEWVM 170

                        90       100       110
                ....*....|....*....|....*....|....*
gi 17737395 436 FGHKFQQRIGHgdNKHSDADRSPVFLQFIDSVWQV 470
Cdd:cd14594 171 GGHCFLDRCNH--LRQNDKEEVPVFLLFLDCVWQL 203
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 41-159 1.34e-21

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: 90.12  E-value: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395    41 ILRDTPFGYLEGEEDQDqkndvTYVCPY---RGPVFGALTITNYRLYFRSLPLrdqEPPVVVDVPLGVIARVEKIGGATS 117
Cdd:pfam02893   1 ELFRKKFKLPPEERLIA-----SYSCYLnrdGGPVQGRLYLTNYRLCFRSLPK---GWSTKVVIPLVDIEEIEKLKGGAN 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 17737395   118 RGENSYGIEIFCKDmrNLRFAHKQQNHSRRTVFEKLQANAFP 159
Cdd:pfam02893  73 LFPNGIQVETGSND--KFSFAGFVTRDEAIEFILALLKNAHP 112
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 57-153 6.41e-15

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: 70.49  E-value: 6.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395  57 DQKNDVTYVCPYR---GPVFGALTITNYRLYFRSlplRDQEPPVVVDVPLGVIARVEKIGGATSrgeNSYGIEIFCKDMR 133
Cdd:cd10570   1 IEKLGVRFCCALRprkLPLEGTLYLSTYRLIFSS---KADGDETKLVIPLVDITDVEKIAGASF---LPSGLIITCKDFR 74

                        90       100
                ....*....|....*....|
gi 17737395 134 NLRFAHKQQNHSRRTVFEKL 153
Cdd:cd10570  75 TIKFSFDSEDEAVKVIARVL 94
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
48-113 3.69e-13

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 64.15  E-value: 3.69e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17737395     48 GYLEGEEDQDqkndvTYVCPY--RGPVFGALTITNYRLYFRSLPLRDqepPVVVDVPLGVIARVEKIG 113
Cdd:smart00568   1 KLPEEEKLIA-----DYSCYLsrTGPVQGRLYISNYRLCFRSNLPGK---LTKVVIPLADITRIEKST 60
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
379-493 5.00e-08

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 51.21  E-value: 5.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395    379 AVRIVDKVETM---STSVVVHCSDGWDRTAQLTALSMLLLDPHYRTvrgfevliekewlsfghkfqqrighgdnkhsdad 455
Cdd:smart00404  25 LLRAVKKNLNQsesSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA---------------------------------- 70

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 17737395    456 rspVFLQFIDSVWQVSQQFNNAFEFNEHFLITIVDHLY 493
Cdd:smart00404  71 ---GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 379-493 5.00e-08

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: 51.21  E-value: 5.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395    379 AVRIVDKVETM---STSVVVHCSDGWDRTAQLTALSMLLLDPHYRTvrgfevliekewlsfghkfqqrighgdnkhsdad 455
Cdd:smart00012  25 LLRAVKKNLNQsesSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA---------------------------------- 70

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 17737395    456 rspVFLQFIDSVWQVSQQFNNAFEFNEHFLITIVDHLY 493
Cdd:smart00012  71 ---GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 367-444 1.23e-07

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: 50.43  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395 367 LWLKHIRCI-------LAGAVRIVDKVETMSTSVVVHCSDGWDRTAQLTALSMLLldpHYRtvRGFEVLIEKEWLSFGHK 439
Cdd:cd14494  26 LKQLGVTTIvdltlamVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVL---LGG--MSAEEAVRIVRLIRPGG 100


                ....*
gi 17737395 440 FQQRI 444
Cdd:cd14494 101 IPQTI 105
PH-like cd00900
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 57-147 1.07e-04

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: 1.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737395  57 DQKNDVTYVCPYRGPVFGALTITNYRLYFRslplRDQEPPVVVDVPLGVIARVEKIGGatsrGENSYGIEIFCKDMRN-L 135
Cdd:cd00900   1 LKFRAVRVYREPTKRVEGTLYITSDRLILR----DKNDGGLELSIPISDIVNVNVSPQ----GPSSRYLVLVLKDRGEfV 72

                        90
                ....*....|..
gi 17737395 136 RFAHKQQNHSRR 147
Cdd:cd00900  73 GFSFPKEEDAIE 84
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH