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Conserved domains on  [gi|402594737|gb|EJW88663|]
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hypothetical protein WUBG_00426 [Wuchereria bancrofti]

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)

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 ...
127-455 1.56e-170

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: 429026 [Multi-domain]  Cd Length: 331  Bit Score: 485.82  E-value: 1.56e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737  127 NGWTAFDAEQEYAKLVIRCKDGWRISAVNKGFRVCSTYPEMVIVPKGIGDDYLRISATFRDGGRFPILSFYHGETKSCLI 206
Cdd:pfam06602   3 NGWDLYDPEAEFARQGLPNKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVIT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737  207 RCGQPLVGPTNRRCKEDETILNSLLSSTS----KGVIVDTRTKAVAQSAKNKGGGCESQMFYSQWKYIYGGTPRIKEIHD 282
Cdd:pfam06602  83 RSSQPLVGLNGKRCIEDEKLLNAIFKSNPysakKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737  283 ALAKLVELCTETNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEGSaevPVVVHGAEGTDSTLLVTSLAQLLLDS 362
Cdd:pfam06602 163 SLNKLVEACNDRSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGS---SVLVHCSDGWDRTAQLTSLAQLLLDP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737  363 DSRTIRGFESLIEREWISAGHPFSYRCAHSAFATGGItgpHESPMFLCFLDCVWQVYQQFPCSFEFTEEFLIFLFEHAYA 442
Cdd:pfam06602 240 YYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGFSDSK---ERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLDHLYS 316
                         330
                  ....*....|...
gi 402594737  443 SEFGSFLGNSEKE 455
Cdd:pfam06602 317 CQFGTFLCNSEKE 329
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
1-111 3.12e-38

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 cd13211:

Pssm-ID: 450165  Cd Length: 99  Bit Score: 135.87  E-value: 3.12e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737   1 MELSEAIERPRVDNVFLRKGPRQPQPGSLALIGHHMIFSPSssstnspsgKEHSSELWLLHRAVDRVIVEPIVKDSfnrS 80
Cdd:cd13211    1 MEFAELIKTPKVDNVVLHRPPRPAVEGTLCITGHHLILSSR---------QDNAEELWLLHSNIDSVEKKFVGKSS---G 68
                         90       100       110
                 ....*....|....*....|....*....|.
gi 402594737  81 GKLILKCKNFMICIFEIDDLDDCLAVAQGIQ 111
Cdd:cd13211   69 GTLTLKCKDFRIIQLDIPDMEECLNIASSIE 99
 
Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
127-455 1.56e-170

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: 429026 [Multi-domain]  Cd Length: 331  Bit Score: 485.82  E-value: 1.56e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737  127 NGWTAFDAEQEYAKLVIRCKDGWRISAVNKGFRVCSTYPEMVIVPKGIGDDYLRISATFRDGGRFPILSFYHGETKSCLI 206
Cdd:pfam06602   3 NGWDLYDPEAEFARQGLPNKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVIT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737  207 RCGQPLVGPTNRRCKEDETILNSLLSSTS----KGVIVDTRTKAVAQSAKNKGGGCESQMFYSQWKYIYGGTPRIKEIHD 282
Cdd:pfam06602  83 RSSQPLVGLNGKRCIEDEKLLNAIFKSNPysakKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737  283 ALAKLVELCTETNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEGSaevPVVVHGAEGTDSTLLVTSLAQLLLDS 362
Cdd:pfam06602 163 SLNKLVEACNDRSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGS---SVLVHCSDGWDRTAQLTSLAQLLLDP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737  363 DSRTIRGFESLIEREWISAGHPFSYRCAHSAFATGGItgpHESPMFLCFLDCVWQVYQQFPCSFEFTEEFLIFLFEHAYA 442
Cdd:pfam06602 240 YYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGFSDSK---ERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLDHLYS 316
                         330
                  ....*....|...
gi 402594737  443 SEFGSFLGNSEKE 455
Cdd:pfam06602 317 CQFGTFLCNSEKE 329
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
189-417 1.07e-124

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: 365.12  E-value: 1.07e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 189 GRFPILSFYHGETKSCLIRCGQPLVGPTNRRCKEDETILNSLLSSTSKGVIVDTRTKAVAQSAKNKGGGCESQMFYSQWK 268
Cdd:cd14536    1 GRFPVLSYYHKKNGMVLMRSSQPLTGPNGKRCKEDEKLLNAVLGGGKRGYIIDTRSKNVAQQARAKGGGFEPEAHYPQWR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 269 YIYGGTPRIKEIHDALAKLVELCTETNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEGsaeVPVVVHGAEGTDS 348
Cdd:cd14536   81 RIHKPIERYNVLQESLIKLVEACNDQGHSMDKWLSKLESSNWLSHVKEILTTACLVAQCIDREG---ASVLVHGSEGMDS 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402594737 349 TLLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHSAFATGgiTGPHESPMFLCFLDCVWQ 417
Cdd:cd14536  158 TLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRCAKSAYSNS--KQKFESPVFLLFLDCVWQ 224
PH-GRAM_MTMR9 cd13211
Myotubularian (MTM) related 9 protein (MTMR9) Pleckstrin Homology-Glucosyltransferases, ...
1-111 3.12e-38

Myotubularian (MTM) related 9 protein (MTMR9) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR9 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR9 contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, a SET interaction domain, and a C-terminal coiled-coil 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. 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: 275398  Cd Length: 99  Bit Score: 135.87  E-value: 3.12e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737   1 MELSEAIERPRVDNVFLRKGPRQPQPGSLALIGHHMIFSPSssstnspsgKEHSSELWLLHRAVDRVIVEPIVKDSfnrS 80
Cdd:cd13211    1 MEFAELIKTPKVDNVVLHRPPRPAVEGTLCITGHHLILSSR---------QDNAEELWLLHSNIDSVEKKFVGKSS---G 68
                         90       100       110
                 ....*....|....*....|....*....|.
gi 402594737  81 GKLILKCKNFMICIFEIDDLDDCLAVAQGIQ 111
Cdd:cd13211   69 GTLTLKCKDFRIIQLDIPDMEECLNIASSIE 99
 
Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
127-455 1.56e-170

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: 429026 [Multi-domain]  Cd Length: 331  Bit Score: 485.82  E-value: 1.56e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737  127 NGWTAFDAEQEYAKLVIRCKDGWRISAVNKGFRVCSTYPEMVIVPKGIGDDYLRISATFRDGGRFPILSFYHGETKSCLI 206
Cdd:pfam06602   3 NGWDLYDPEAEFARQGLPNKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVIT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737  207 RCGQPLVGPTNRRCKEDETILNSLLSSTS----KGVIVDTRTKAVAQSAKNKGGGCESQMFYSQWKYIYGGTPRIKEIHD 282
Cdd:pfam06602  83 RSSQPLVGLNGKRCIEDEKLLNAIFKSNPysakKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737  283 ALAKLVELCTETNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEGSaevPVVVHGAEGTDSTLLVTSLAQLLLDS 362
Cdd:pfam06602 163 SLNKLVEACNDRSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGS---SVLVHCSDGWDRTAQLTSLAQLLLDP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737  363 DSRTIRGFESLIEREWISAGHPFSYRCAHSAFATGGItgpHESPMFLCFLDCVWQVYQQFPCSFEFTEEFLIFLFEHAYA 442
Cdd:pfam06602 240 YYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGFSDSK---ERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLDHLYS 316
                         330
                  ....*....|...
gi 402594737  443 SEFGSFLGNSEKE 455
Cdd:pfam06602 317 CQFGTFLCNSEKE 329
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
189-417 1.07e-124

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: 365.12  E-value: 1.07e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 189 GRFPILSFYHGETKSCLIRCGQPLVGPTNRRCKEDETILNSLLSSTSKGVIVDTRTKAVAQSAKNKGGGCESQMFYSQWK 268
Cdd:cd14536    1 GRFPVLSYYHKKNGMVLMRSSQPLTGPNGKRCKEDEKLLNAVLGGGKRGYIIDTRSKNVAQQARAKGGGFEPEAHYPQWR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 269 YIYGGTPRIKEIHDALAKLVELCTETNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEGsaeVPVVVHGAEGTDS 348
Cdd:cd14536   81 RIHKPIERYNVLQESLIKLVEACNDQGHSMDKWLSKLESSNWLSHVKEILTTACLVAQCIDREG---ASVLVHGSEGMDS 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402594737 349 TLLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHSAFATGgiTGPHESPMFLCFLDCVWQ 417
Cdd:cd14536  158 TLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRCAKSAYSNS--KQKFESPVFLLFLDCVWQ 224
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
134-441 1.62e-89

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: 277.69  E-value: 1.62e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 134 AEQEYAKLVIRCkDGWRISAVNKGFRVCSTYPEMVIVPKGIGDDYLRISATFRDGGRFPILSFYHGETKSCLIRCGQPLV 213
Cdd:cd14532    1 LESEYTRMGVPN-DNWTLSDINKDYELCDTYPRELFVPTSASTPVLVGSSKFRSKGRLPVLSYLHKDNQAAICRCSQPLS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 214 GpTNRRCKEDETILNSLLSSTSKG---VIVDTRTKAVAQSAKNKGGGCESQMFYSQWKYIYGGtprIKEIH---DALAKL 287
Cdd:cd14532   80 G-FSARCVEDEQLLQAIRKANPNSkfmYVVDTRPKINAMANKAAGKGYENEDNYSNIKFQFFG---IENIHvmrSSLQKL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 288 VELCTETNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVhCEGsaeVPVVVHGAEGTDSTLLVTSLAQLLLDSDSRTI 367
Cdd:cd14532  156 LEVCELKNPSMSAFLSGLESSGWLKHIKAVMDTSVFIAKAV-SEG---ASVLVHCSDGWDRTAQTCSLASLLLDPYYRTI 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402594737 368 RGFESLIEREWISAGHPFSYRCAHSAfatggiTGPHE-SPMFLCFLDCVWQVYQQFPCSFEFTEEFLIFLFEHAY 441
Cdd:cd14532  232 KGFQVLIEKEWLSFGHKFTDRCGHLQ------GDAKEvSPVFTQFLDCVWQLMQQFPRAFEFNERFLLTLHDHVY 300
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
189-417 5.47e-76

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: 240.14  E-value: 5.47e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 189 GRFPILSFYHGETKSCLIRCGQPLVGPTNRRCKEDETILNSLL---SSTSKGVIVDTRTKAVAQSAKNKGGGCESQMFYS 265
Cdd:cd14507    1 GRIPVLSWRHPRNGAVICRSSQPLVGLTGSRSKEDEKLLNAIRkasPSSKKLYIVDARPKLNAVANRAKGGGYENTEYYP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 266 QWKYIYGGTPRIKEIHDALAKLVELCTETNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEGSaevPVVVHGAEG 345
Cdd:cd14507   81 NCELEFLNIENIHAMRDSLNKLRDACLSPNDEESNWLSALESSGWLEHIRLILKGAVRVADLLEKEGT---SVLVHCSDG 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402594737 346 TDSTLLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHsafatGGITGPHE--SPMFLCFLDCVWQ 417
Cdd:cd14507  158 WDRTSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGH-----GDKNSSDEerSPIFLQFLDCVWQ 226
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
128-442 4.91e-74

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: 237.85  E-value: 4.91e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 128 GWTAFDAEQEYAKLVIRcKDGWRISAVNKGFRVCSTYPEMVIVPKGIGDDYLRISATFRDGGRFPILSFYHGETKSCLIR 207
Cdd:cd14584    1 GWKLIDLKVDFQRMGIP-NDYWEITDANKNYEICSTYPPELVVPKSASKATVVGSSKFRSRGRFPVLSYLYKENNAAICR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 208 CGQPLVGpTNRRCKEDETILNSlLSSTSKG----VIVDTRTKAVAQSAKNKGGGCESQMFYSQWKYIYGGTPRIKEIHDA 283
Cdd:cd14584   80 CSQPLSG-FSARCVEDEQMLQA-ISKANPGspfmYVVDTRPKLNAMANRAAGKGYENEDNYSNIRFQFIGIENIHVMRSS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 284 LAKLVELCTETNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEGSAevpVVVHGAEGTDSTLLVTSLAQLLLDSD 363
Cdd:cd14584  158 LQKLLEVCEMKSPSMSDFLTGLENSGWLRHIKAVMDAGVFLAKAVKEEKAS---VLVHCSDGWDRTAQVCSLASLLLDPF 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 364 SRTIRGFESLIEREWISAGHPFSYRCAHSAfatggiTGPHE-SPMFLCFLDCVWQVYQQFPCSFEFTEEFLIFLFEHAYA 442
Cdd:cd14584  235 YRTIKGLMVLIEKEWISMGHKFSQRCGHLD------GDPKEvSPVFTQFLECVWQLMEQFPCAFEFNEHFLLEIHDHVFS 308
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
136-442 2.50e-70

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: 228.28  E-value: 2.50e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 136 QEYAKLVIRCkDGWRISAVNKGFRVCSTYPEMVIVPKGIGDDYLRISATFRDGGRFPILSFYHGETKSCLIRCGQPLVGp 215
Cdd:cd14585    3 EEYKRMGVPN-DYWQLSDVNRDYKICDTYPRDLYVPITASKPIIVGSSKFRSKGRFPVLSYYHQEKKAAICRCSQPLSG- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 216 TNRRCKEDETILNSLLSSTSKG---VIVDTRTKAVAQSAKNKGGGCESQMFYSQWKYIYGGTPRIKEIHDALAKLVELCT 292
Cdd:cd14585   81 FSARCLEDEHMLQAISKANPNNrymYVMDTRPKLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 293 ETNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEGSAevpVVVHGAEGTDSTLLVTSLAQLLLDSDSRTIRGFES 372
Cdd:cd14585  161 TKALSVNDFLSGLESSGWLRHIKAVLDAAVFLAKAVAVEGAS---VLVHCSDGWDRTAQVCSLGSLLLDPYYRTIKGFMV 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402594737 373 LIEREWISAGHPFSYRCahsafatGGITG-PHE-SPMFLCFLDCVWQVYQQFPCSFEFTEEFLIFLFEHAYA 442
Cdd:cd14585  238 LIEKDWISFGHKFSDRC-------GQLDGdPKEiSPVFTQFLECVWQLTEQFPRAFEFSEAFLLQIHEHIHS 302
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
189-441 1.40e-69

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: 224.47  E-value: 1.40e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 189 GRFPILSFYHGETKSCLIRCGQPLVGPTNRRCKEDETILNSLLSSTS---KGVIVDTRTKAVAQSAKNKGGGCESQMFYS 265
Cdd:cd14592    1 GRVPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYLQTIMDANAqshKLIIFDARQNSVADTNKTKGGGYESESAYP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 266 QWKYIYGGTPRIKEIHDALAKLVELCTETnISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHcegSAEVPVVVHGAEG 345
Cdd:cd14592   81 NAELVFLEIHNIHVMRESLRKLKEIVYPS-IDEARWLSNVDGTHWLEYIRMLLAGAVRIADKIE---SGKTSVVVHCSDG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 346 TDSTLLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHsafATGGITGPHESPMFLCFLDCVWQVYQQFPCS 425
Cdd:cd14592  157 WDRTAQLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGH---GDDNHADADRSPIFLQFIDCVWQMTRQFPSA 233
                        250
                 ....*....|....*.
gi 402594737 426 FEFTEEFLIFLFEHAY 441
Cdd:cd14592  234 FEFNELFLITILDHLY 249
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
176-441 1.55e-67

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: 219.52  E-value: 1.55e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 176 DDYLRISATFRDGGRFPILSFYHGETKSCLIRCGQPLVGPTNRRCKEDETILNSLLSSTS---KGVIVDTRTKAVAQSAK 252
Cdd:cd14590    1 DEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAqshKIFIFDARPSVNAVANK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 253 NKGGGCESQMFYSQWKYIYGGTPRIKEIHDALAKLVELcTETNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHceg 332
Cdd:cd14590   81 AKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEI-VYPNIEESHWLSNLESTHWLEHIKLILAGALRIADKVE--- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 333 SAEVPVVVHGAEGTDSTLLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHsafATGGITGPHESPMFLCFL 412
Cdd:cd14590  157 SGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGH---GDKNHADADRSPVFLQFI 233
                        250       260
                 ....*....|....*....|....*....
gi 402594737 413 DCVWQVYQQFPCSFEFTEEFLIFLFEHAY 441
Cdd:cd14590  234 DCVWQMTRQFPTAFEFNEYFLITILDHLY 262
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
149-442 3.22e-66

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: 217.52  E-value: 3.22e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 149 WRISAVNKGFRVCSTYPEMVIVPKGIGDDYLRISATFRDGGRFPILSFYHGETKSCLIRCGQPLVGpTNRRCKEDETILN 228
Cdd:cd14583   15 WQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYYCKDNNASICRSSQPLSG-FSARCLEDEQMLQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 229 SLLSSTSKG---VIVDTRTKAVAQSAKNKGGGCESQMFYSQWKYIYGGTPRIKEIHDALAKLVELCTETNISVDRWISRL 305
Cdd:cd14583   94 AIRKANPGSdfmYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELRSPSMGDFLWGL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 306 GSCGWLQFVSDMLTCAATVAQCVHCEGSAevpVVVHGAEGTDSTLLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPF 385
Cdd:cd14583  174 ENSGWLKHIKAIMDAGIFIAKAVAEEGAS---VLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKF 250
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 402594737 386 SYRCAHsafatggITG-PHE-SPMFLCFLDCVWQVYQQFPCSFEFTEEFLIFLFEHAYA 442
Cdd:cd14583  251 NHRYGH-------LDGdPKEvSPVIDQFIECVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
189-441 2.07e-63

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: 208.07  E-value: 2.07e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 189 GRFPILSFYHGETKSCLIRCGQPLVGPTNRRCKEDETILNSLLSS---TSKGVIVDTRTKAVAQSAKNKGGGCESQMFYS 265
Cdd:cd14535    1 NRIPVLSWIHPESQATITRCSQPLVGVSGKRSKDDEKYLQLIMDAnaqSHKLFIMDARPSVNAVANKAKGGGYESEDAYQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 266 QWKYIYGGTPRIKEIHDALAKLVELCTeTNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHcegSAEVPVVVHGAEG 345
Cdd:cd14535   81 NAELVFLDIHNIHVMRESLRKLKDICF-PNIDDSHWLSNLESTHWLEHIKLILAGAVRIADKVE---SGKTSVVVHCSDG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 346 TDSTLLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHsafATGGITGPHESPMFLCFLDCVWQVYQQFPCS 425
Cdd:cd14535  157 WDRTAQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGH---GDKNHSDADRSPVFLQFIDCVWQMTRQFPNA 233
                        250
                 ....*....|....*.
gi 402594737 426 FEFTEEFLIFLFEHAY 441
Cdd:cd14535  234 FEFNEHFLITILDHLY 249
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
190-441 1.72e-59

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: 197.94  E-value: 1.72e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 190 RFPILSFYHGETKSCLIRCGQPLVGPTNRRCKEDETILNSLLSS---TSKGVIVDTRTKAVAQSAKNKGGGCESQMFYSQ 266
Cdd:cd14591    2 RIPVLSWIHPENQAVIMRCSQPLVGMSGKRNKDDEKYLDIIREAngqTSKLTIYDARPSVNAVANKATGGGYEGDDAYQN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 267 WKYIYGGTPRIKEIHDALAKLVELcTETNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEGSAevpVVVHGAEGT 346
Cdd:cd14591   82 AELVFLDIHNIHVMRESLKKLKDI-VYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSS---VLVHCSDGW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 347 DSTLLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHsafATGGITGPHESPMFLCFLDCVWQVYQQFPCSF 426
Cdd:cd14591  158 DRTAQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGH---GDKNHADADRSPIFLQFIDCVWQMSKQFPTAF 234
                        250
                 ....*....|....*
gi 402594737 427 EFTEEFLIFLFEHAY 441
Cdd:cd14591  235 EFNEQFLITILDHLY 249
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
149-417 2.86e-48

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: 170.21  E-value: 2.86e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 149 WRISAVNKGFRVCSTYPEMVIVPKGIGDDYLRISATFRDGGRFPILSFYHGETKSCLIRCGQPLVGPTNRRCKEDETILN 228
Cdd:cd14587    3 WRVSEINSNYKLCSSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAVIARCSQPEISWWGWRNADDEYLVT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 229 SLL-------------SSTSKG-------------------------------VIVDTRTKAVAQSAKNKGGGCESQMFY 264
Cdd:cd14587   83 SIAkacaldpgtrapgGSPSKGnsdgsdasdtdfdssltacsavesgaapqklLILDARSYTAAVANRAKGGGCECEEYY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 265 SQWKYIYGGTPRIKEIHDALAKLVELCTETNiSVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEGSaevPVVVHGAE 344
Cdd:cd14587  163 PNCEVMFMGMANIHSIRNSFQYLRAVCSQMP-DPGNWLSALESTKWLQHLSVMLKAAVLVASAVDREGR---PVLVHCSD 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 402594737 345 GTDSTLLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHSafaTGGITGPHESPMFLCFLDCVWQ 417
Cdd:cd14587  239 GWDRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHQ---ENVEDQNEQCPVFLQWLDCVHQ 308
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
146-417 1.10e-47

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: 168.66  E-value: 1.10e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 146 KDGWRISAVNKGFRVCSTYPEMVIVPKGIGDDYLRISATFRDGGRFPILSFYHGETKSCLIRCGQPLVGPTNRRCKEDET 225
Cdd:cd14586    5 QNAWRISNINEKYKLCGSYPQELIVPAWITDKELESVASFRSWKRIPAVVYRHQSNGAVIARCGQPEVSWWGWRNADDEH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 226 ILNSLL------SSTSKGV------------------------------------------IVDTRTKAVAQSAKNKGGG 257
Cdd:cd14586   85 LVQSVAkacasdSSSCKSVlmtgncsrdfpnggdlsdvefdssmsnasgveslaiqpqkllILDARSYAAAVANRAKGGG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 258 CESQMFYSQWKYIYGGTPRIKEIHDALAKLVELCTETNISVDrWISRLGSCGWLQFVSDMLTCAATVaqcVHCEGSAEVP 337
Cdd:cd14586  165 CECPEYYPNCEVVFMGMANIHSIRKSFQSLRLLCTQMPDPAN-WLSALESTKWLQHLSMLLKSALLV---VHAVDRDQRP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 338 VVVHGAEGTDSTLLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHSAFATggiTGPHESPMFLCFLDCVWQ 417
Cdd:cd14586  241 VLVHCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRCGHGENSD---DLNERCPVFLQWLDCVHQ 317
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
189-417 1.24e-46

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: 162.96  E-value: 1.24e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 189 GRFPILSFYHGETKSCLIRCGQPLVGPTNRRCKEDETILNSLLSS------TSKGVIVDTRTKAVAQSAKNKGGGCESQM 262
Cdd:cd14533    2 KRIPSVVWRHQRNGAVIARCSQPEVGWLGWRNAEDENLLQAIAEAcasnasPKKLLIVDARSYAAAVANRAKGGGCECPE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 263 FYSQWKYIYGGTPRIKEIHDALAKLVELCTeTNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEGSaevPVVVHG 342
Cdd:cd14533   82 YYPNCEVVFMNLANIHAIRKSFHSLRALCS-SAPDQPNWLSNLESTKWLHHLSGLLKAALLVVNAVDEEGR---PVLVHC 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402594737 343 AEGTDSTLLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHSafatGGITGPHE-SPMFLCFLDCVWQ 417
Cdd:cd14533  158 SDGWDRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFGHKFADRCGHG----VNSEDINErCPVFLQWLDCVHQ 229
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
189-417 8.21e-43

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: 152.60  E-value: 8.21e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 189 GRFPILSFYHGETKSCLIRCGQPLVGPTNRRCKEDE--------TILNSLLSSTSKGVIVDTR--TKAVAQSAknKGGGC 258
Cdd:cd17666    1 QRIPVLTYLHKANGCSITRSSQPLVGLKQNRSIQDEklvseifnTSINEIYISPQKNLIVDARptTNAMAQVA--LGAGT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 259 ES--QMFYSQWKYIYGGTPRIKEIHDALAKLVELCTETNISVDRW---ISRLGSCGWLQFVSDMLTCAATVAQCVHCEGS 333
Cdd:cd17666   79 ENmdNYKYKTAKKIYLGIDNIHVMRDSLNKVTEALKDGDDSNPSYpplINALKKSNWLKYLAIILQGADLIAKSIHFNHS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 334 AevpVVVHGAEGTDSTLLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHSafatggitgpHESPMFLCFLD 413
Cdd:cd17666  159 H---VLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFAERSGHK----------ETSPVFHQFLD 225

                 ....
gi 402594737 414 CVWQ 417
Cdd:cd17666  226 CVYQ 229
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
149-421 3.92e-40

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: 146.74  E-value: 3.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 149 WRISAVNKGFRVCSTYPEMVIVPKGIGDDYL-RISATFRdGGRFPILSFYHGETKSCLIRCGQP----LVGptnrrcked 223
Cdd:cd14534    1 FRISTANRDYSICRSYPALVVVPQSVSDESLrKVARCYR-QGRFPVVTWRHPRTKALLLRSGGFhgkgVMG--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 224 etILNSLLSSTSKGVIVDTRTKAVAQSAKNKGG------GCESQM------FYSQWKYIYGGTPRIKEIHDALAKLVELC 291
Cdd:cd14534   71 --MLKSANTSTSSPTVSSSETSSSLEQEKYLSAlvlyvlGEKSQMkgvkaeSDPKCEFIPVEYPEVRQVKASFKKLLRAC 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 292 TETNISVDRWISRL---GSCGWLQFVSDMLTCAATVAQCVHCEGSAevpVVVHGAEGTDSTLLVTSLAQLLLDSDSRTIR 368
Cdd:cd14534  149 VPSSAPTEPEQSFLkavEDSEWLQQLQCLMQLSGAVVDLLDVQGSS---VLLCLEDGWDVTTQVSSLSQLLLDPYYRTLE 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 402594737 369 GFESLIEREWISAGHPFSYRCAHSAFATG-GITgphesPMFLCFLDCVWQVYQQ 421
Cdd:cd14534  226 GFRVLVEKEWLAFGHRFSHRSNLTAASQSsGFA-----PVFLQFLDAVHQIHRQ 274
PH-GRAM_MTMR9 cd13211
Myotubularian (MTM) related 9 protein (MTMR9) Pleckstrin Homology-Glucosyltransferases, ...
1-111 3.12e-38

Myotubularian (MTM) related 9 protein (MTMR9) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR9 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR9 contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, a SET interaction domain, and a C-terminal coiled-coil 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. 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: 275398  Cd Length: 99  Bit Score: 135.87  E-value: 3.12e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737   1 MELSEAIERPRVDNVFLRKGPRQPQPGSLALIGHHMIFSPSssstnspsgKEHSSELWLLHRAVDRVIVEPIVKDSfnrS 80
Cdd:cd13211    1 MEFAELIKTPKVDNVVLHRPPRPAVEGTLCITGHHLILSSR---------QDNAEELWLLHSNIDSVEKKFVGKSS---G 68
                         90       100       110
                 ....*....|....*....|....*....|.
gi 402594737  81 GKLILKCKNFMICIFEIDDLDDCLAVAQGIQ 111
Cdd:cd13211   69 GTLTLKCKDFRIIQLDIPDMEECLNIASSIE 99
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
275-417 2.46e-37

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: 136.70  E-value: 2.46e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 275 PRIKEIHDALAKLVELCTETNISV-----DRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEGsaeVPVVVHGAEGTDST 349
Cdd:cd14537   59 PSLQDVQAAYLKLRELCTPDSSEQfwvqdSKWYSLLENTKWLHYVSACLKKASEAAEALESRG---RSVVLQESDGRDLS 135
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 402594737 350 LLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHsafATGGITGPHESPMFLCFLDCVWQ 417
Cdd:cd14537  136 CVVSSLVQLLLDPHFRTITGFQSLIQKEWVALGHPFCDRLGH---VKPNKTESEESPVFLLFLDCVWQ 200
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
149-421 3.49e-32

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: 125.47  E-value: 3.49e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 149 WRISAVNKGFRVCSTYPEMVIVPKGIGDDYL-RISATFRDgGRFPILSFYHGETKSCLIRCG---------------QPL 212
Cdd:cd14588    1 FRISTVNRMYAVCRSYPGLLIVPQSIQDNTIqRISRCYRQ-NRFPVVCWRNSRTKAVLLRSGglhgkgvvglfksqnAPA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 213 VGP--TNRRCKEDETILNSLLSSTSKGVIVDTRTK---------AVAQSAKNKGGGCESqmfYSQWKYIYGGTPRIKEIH 281
Cdd:cd14588   80 AGQsqTDSTSLEQEKYLQAVINSMPRYADASGRNTlsgfraalyIIGDKSQLKGVKQDP---LQQWEVVPIEVFDVRQVK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 282 DALAKLVELCTETNISVD---RWISRLGSCGWLQFVSDMLTCAATVAQCVHcEGSAevpVVVHGAEGTDSTLLVTSLAQL 358
Cdd:cd14588  157 ASFKKLMKACVPSCPSTDpsqTYLRTLEESEWLSQLHKLLQVSVLVVELLD-SGSS---VLVSLEDGWDITTQVVSLVQL 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402594737 359 LLDSDSRTIRGFESLIEREWISAGHPFSYRCAHS-AFATGGITgphesPMFLCFLDCVWQVYQQ 421
Cdd:cd14588  233 LSDPYYRTIEGFRLLVEKEWLSFGHRFSHRGAQTlASQSSGFT-----PVFLQFLDCVHQIHLQ 291
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
149-421 1.83e-28

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: 115.02  E-value: 1.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 149 WRISAVNKGFRVCSTYPEMVIVPKGIGDDYL-RISATFRDGgRFPILSFYHGETKSCLIRCG---------------QPL 212
Cdd:cd14589    1 FRITAVNRMYSLCRSYPGLLVVPQSVQDSSLqKVARCYRHN-RLPVVCWKNSKTKAVLLRSGgfhgkgvvglfksqnPHS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 213 VGPTNRRCK---EDETILNSLLSSTSkgvivdtrtkaVAQSAKNKGGGCESQMFYSQWK-YIYGGTPRIK---------- 278
Cdd:cd14589   80 AAPASSESSssiEQEKYLQALLNAIS-----------VHQKMNGNSTLLQSQLLKRQAAlYIFGEKSQLRgfkldfalnc 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 279 -----EIHD------ALAKLVELCTETNISVD---RWISRLGSCGWLQFVSDMLTCAATVAQCVHcEGSAevpVVVHGAE 344
Cdd:cd14589  149 efvpvEFHDirqvkaSFKKLMRACVPSTIPTDsevTFLKALGESEWFLQLHRIMQLAVVISELLE-SGSS---VMVCLED 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 345 GTDSTLLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYR------CAHSAFAtggitgphesPMFLCFLDCVWQV 418
Cdd:cd14589  225 GWDITTQVVSLVQLLSDPFYRTLEGFQMLVEKEWLSFGHKFSQRsnltpnSQGSGFA----------PIFLQFLDCVHQI 294

                 ...
gi 402594737 419 YQQ 421
Cdd:cd14589  295 HNQ 297
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
275-417 3.35e-27

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: 108.44  E-value: 3.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 275 PRIKEIHDALAKLVELCTETNI--SVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEgsaEVPVVVHGAEGTDSTLLV 352
Cdd:cd14593   59 PNIQEIQAAFVKLKQLCVNEPFeeTEEKWLSSLESTRWLEYVRAFLKHSAELVYMLESK---HVSVILQEEEGRDLSCVV 135
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402594737 353 TSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHSAFATggitgPHESPMFLCFLDCVWQ 417
Cdd:cd14593  136 ASLVQVMLDPYFRTITGFQSLIQKEWVMAGYRFLDRCNHLKKSS-----KKESPLFLLFLDCVWQ 195
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
275-418 4.51e-23

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: 96.82  E-value: 4.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 275 PRIKEIHDALAKLVELC---TETNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCegsAEVPVVVHGAEGTDSTLL 351
Cdd:cd14595   57 PSPADIQLAYLKLRTLClpdISVSVSDEKWLSNLEGTRWLDHVRACLRKASEVSCLLAE---RHRSVILQESEDRDLNCL 133
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 402594737 352 VTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHSafatgGITGPHESPMFLCFLDCVWQV 418
Cdd:cd14595  134 LSSLVQLLSDPHARTISGFQSLVQKEWVVAGHPFLQRLNLT-----RESDKEESPVFLLFLDCVWQL 195
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
275-418 8.14e-22

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: 93.37  E-value: 8.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737 275 PRIKEIHDALAK-----LVELCTETNISVDRWISRLGSCGWLQFVSDMLTCAATVAQCVHCEgsaEVPVVVHGAEGTDST 349
Cdd:cd14594   63 PSLQEIQTAYNRfkqlfLIDNSTDFWDTDVKWFSSLESSNWLEIIRQCLKKAVEVVECLEKQ---NTNVLLTEEEATDLC 139
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402594737 350 LLVTSLAQLLLDSDSRTIRGFESLIEREWISAGHPFSYRCAHSAfatggITGPHESPMFLCFLDCVWQV 418
Cdd:cd14594  140 CVISSLVQIMMDPYCRTKSGFQSLIQKEWVMGGHCFLDRCNHLR-----QNDKEEVPVFLLFLDCVWQL 203
PH-GRAM_MTMR7 cd13344
Myotubularian (MTM) related 7 protein (MTMR7) Pleckstrin Homology-Glucosyltransferases, ...
5-103 5.05e-09

Myotubularian (MTM) related 7 protein (MTMR7) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR7 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR6 binds to phosphoinositide lipids through its PH-GRAM domain and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate. MTMR7 interacts with MTMR6, MTMR8 and MTMR9. MTMR7 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. 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: 270152  Cd Length: 103  Bit Score: 53.77  E-value: 5.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737   5 EAIERPRVDNVFL--RKGPRQPQPGSLALIGHHMIFspsssstnSPSGKEHSSELWLLHRavdrvIVEPIVKDSFNRSG- 81
Cdd:cd13344    2 EHIRMPKVENVRLvdRISSKKAALGTLYLTATHVIF--------VENSSDTRKETWILHS-----QISSIEKQATTATGc 68
                         90       100
                 ....*....|....*....|..
gi 402594737  82 KLILKCKNFMICIFEIDDLDDC 103
Cdd:cd13344   69 PLLIRCKNFQVIQLIIPQERDC 90
PH-GRAM_MTMR6-like cd13210
Myotubularian (MTM) related (MTMR) 7 and 8 proteins Pleckstrin Homology-Glucosyltransferases, ...
7-103 2.85e-07

Myotubularian (MTM) related (MTMR) 7 and 8 proteins Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR6, MTMR7, and MRMR8 are all member of the myotubularin dual specificity protein phosphatase gene family. They bind to phosphoinositide lipids through its PH-GRAM domain. These proteins also interact with each other as well as MTMR9. 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. 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 lipid-binding FYVE domain has been shown to bind phosphotidylinositol-3-phosphate. 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: 270030  Cd Length: 98  Bit Score: 48.82  E-value: 2.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737   7 IERPRVDNVFL--RKGPRQPQPGSLALIGHHMIFSpsssstnspsGKEHSSELWLLHRAVDRVivepiVKDSFNRSG-KL 83
Cdd:cd13210    1 IRTPKVENVRLldRFSSRKPAVGTLYLTATHLIFV----------EPSGKKETWILHSHIASV-----EKLPLTTAGcPL 65
                         90       100
                 ....*....|....*....|
gi 402594737  84 ILKCKNFMICIFEIDDLDDC 103
Cdd:cd13210   66 VIRCKNFQVITFVIPRERDC 85
PH-GRAM_MTMR8 cd13345
Myotubularian (MTM) related 8 protein (MTMR8) Pleckstrin Homology-Glucosyltransferases, ...
5-110 2.94e-04

Myotubularian (MTM) related 8 protein (MTMR8) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR8 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR8 binds to phosphoinositide lipids through its PH-GRAM domain. MTMR8 can self associate and interacts with MTMR6, MTMR7 and MTMR9. MTMR8 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. 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: 270153  Cd Length: 103  Bit Score: 40.33  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737   5 EAIERPRVDNVFL--RKGPRQPQPGSLALIGHHMIFSPSSSstnspsgkEHSSELWLLHRAVDRVIVEPIVKdsfnrSG- 81
Cdd:cd13345    2 EHITTPKVENVKLldRYTNKKPANGTLYLTATHLIYVEASG--------AARKETWILHHHIATVEKLPLTS-----LGc 68
                         90       100
                 ....*....|....*....|....*....
gi 402594737  82 KLILKCKNFMICIFEIDDLDDCLAVAQGI 110
Cdd:cd13345   69 PLLIRCKNFRVAHFVLDSERDCHEVYISL 97
PH-GRAM_MTMR6 cd13343
Myotubularian (MTM) related (MTMR) 6 protein Pleckstrin Homology-Glucosyltransferases, ...
5-103 1.92e-03

Myotubularian (MTM) related (MTMR) 6 protein Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR6 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR6 binds to phosphoinositide lipids through its PH-GRAM domain. It acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4+ T-cells possibly by decreasing intracellular levels of phosphatidylinositol-3 phosphatase and negatively regulates proliferation of reactivated CD4+ T-cells MTMR6 interacts with MTMR7, MTMR8 and MTMR9. MTMR6 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. 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: 270151  Cd Length: 101  Bit Score: 38.07  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402594737   5 EAIERPRVDNVFLR---KGPRQPQPGSLALIGHHMIFSpsssstnspsgKEHSSELWLLHRAVdrvivEPIVKDSFNRSG 81
Cdd:cd13343    2 EHIRTTKVEQVKLLdrfSTSNKSLTGTLYLTATHLLFI-----------DNSQQETWILHHHI-----APVEKLSLTTSG 65
                         90       100
                 ....*....|....*....|...
gi 402594737  82 -KLILKCKNFMICIFEIDDLDDC 103
Cdd:cd13343   66 cPLVIQCKNFRVVHFVVPRERDC 88
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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