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Conserved domains on  [gi|6322570|ref|NP_012644|]
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phosphatidylinositol-3-phosphatase YMR1 [Saccharomyces cerevisiae S288C]

Protein Classification

myotubularin family protein( domain architecture ID 10352270)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 152-570 6.86e-174

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: 499.31  E-value: 6.86e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    152 SPDSWDIYDPIKEFRRQGLDSKDetcPWRLSTVNEHYEFCPTYPSKLFVPRSTSDILLKHASKFRSQKRIPVLTYHHKAT 231
Cdd:pfam06602   1 EENGWDLYDPEAEFARQGLPSKD---EWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKEN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    232 DCNILRSSQPLPGLINQRSIQDEKLVWESFNSFCNKDIRrtKHVIVDARPRTNALAQMALGGGTENMDNYnffladnnmg 311
Cdd:pfam06602  78 GAVITRSSQPLVGLNGKRSIEDEKLLQAIFKSSNPYSAK--KLYIVDARPKLNAMANRAKGGGYENEDNY---------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    312 vdkslklPTVTRLFLGIDNIHIVSNTAAYMTEViCQGGDLNLPLEQNLIRSqkfSNWLKLNTLILKSVDMLLKSIIFNHS 391
Cdd:pfam06602 146 -------PNCKKIFLGIENIHVMRDSLNKLVEA-CNDRSPSMDKWLSRLES---SGWLKHIKAILDGACLIAQAVDLEGS 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    392 NVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHLNSdirfhdntmhsnfndvdtngdd 471
Cdd:pfam06602 215 SVLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAG---------------------- 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    472 ldigvntqddyaeddeggedetnlinlsriskkfnenfklnKKSLKFVSPVFQQFLDCVYQLLTQNPDLFEFNERFLRRL 551
Cdd:pfam06602 273 -----------------------------------------FTDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRL 311

                         410
                  ....*....|....*....
gi 6322570    552 VYHLYSCQYGTFLSNSEKE 570
Cdd:pfam06602 312 LYHLYSCQFGTFLCNSEKE 330
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 1-44 1.97e-08

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: 473070  Cd Length: 99  Bit Score: 52.28  E-value: 1.97e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 6322570    1 MEYIKIAKVSNVVLHRRGTATQ-GTLHLTTHHLIFESPQL-STEFW 44
Cdd:cd13211   4 AELIKTPKVDNVVLHRPPRPAVeGTLCITGHHLILSSRQDnAEELW 49
 
Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 152-570 6.86e-174

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: 499.31  E-value: 6.86e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    152 SPDSWDIYDPIKEFRRQGLDSKDetcPWRLSTVNEHYEFCPTYPSKLFVPRSTSDILLKHASKFRSQKRIPVLTYHHKAT 231
Cdd:pfam06602   1 EENGWDLYDPEAEFARQGLPSKD---EWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKEN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    232 DCNILRSSQPLPGLINQRSIQDEKLVWESFNSFCNKDIRrtKHVIVDARPRTNALAQMALGGGTENMDNYnffladnnmg 311
Cdd:pfam06602  78 GAVITRSSQPLVGLNGKRSIEDEKLLQAIFKSSNPYSAK--KLYIVDARPKLNAMANRAKGGGYENEDNY---------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    312 vdkslklPTVTRLFLGIDNIHIVSNTAAYMTEViCQGGDLNLPLEQNLIRSqkfSNWLKLNTLILKSVDMLLKSIIFNHS 391
Cdd:pfam06602 146 -------PNCKKIFLGIENIHVMRDSLNKLVEA-CNDRSPSMDKWLSRLES---SGWLKHIKAILDGACLIAQAVDLEGS 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    392 NVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHLNSdirfhdntmhsnfndvdtngdd 471
Cdd:pfam06602 215 SVLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAG---------------------- 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    472 ldigvntqddyaeddeggedetnlinlsriskkfnenfklnKKSLKFVSPVFQQFLDCVYQLLTQNPDLFEFNERFLRRL 551
Cdd:pfam06602 273 -----------------------------------------FTDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRL 311

                         410
                  ....*....|....*....
gi 6322570    552 VYHLYSCQYGTFLSNSEKE 570
Cdd:pfam06602 312 LYHLYSCQFGTFLCNSEKE 330
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
 219-532 1.25e-131

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: 387.18  E-value: 1.25e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  219 KRIPVLTYHHKATDCNILRSSQPLPGLINQRSIQDEKLVWESFNSFCN-KDIRRTKHVIVDARPRTNALAQMALGGGTEN 297
Cdd:cd17666   1 QRIPVLTYLHKANGCSITRSSQPLVGLKQNRSIQDEKLVSEIFNTSINeIYISPQKNLIVDARPTTNAMAQVALGAGTEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  298 MDNYnffladnnmgvdkslKLPTVTRLFLGIDNIHIVSNTAAYMTEVICQGGDLNlPLEQNLIRSQKFSNWLKLNTLILK 377
Cdd:cd17666  81 MDNY---------------KYKTAKKIYLGIDNIHVMRDSLNKVTEALKDGDDSN-PSYPPLINALKKSNWLKYLAIILQ 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  378 SVDMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHlnsdirfhdnt 457
Cdd:cd17666 145 GADLIAKSIHFNHSHVLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFAERSGH----------- 213

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322570  458 mhsnfndvdtngddldigvntqddyaeddeggedetnlinlsriskkfnenfklnkkslKFVSPVFQQFLDCVYQ 532
Cdd:cd17666 214 -----------------------------------------------------------KETSPVFHQFLDCVYQ 229
PH-GRAM_MTMR9 cd13211
Myotubularian (MTM) related 9 protein (MTMR9) Pleckstrin Homology-Glucosyltransferases, ...
 1-44 1.97e-08

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: 52.28  E-value: 1.97e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 6322570    1 MEYIKIAKVSNVVLHRRGTATQ-GTLHLTTHHLIFESPQL-STEFW 44
Cdd:cd13211   4 AELIKTPKVDNVVLHRPPRPAVeGTLCITGHHLILSSRQDnAEELW 49
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
350-421 1.58e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 44.27  E-value: 1.58e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322570     350 DLNLPLEQNLIRSqkfsnwlklntlILKSVDMLLKSIIFNHSnVLVHCSDGWDRTSQVVSLLEICLDPFYRT 421
Cdd:smart00404  12 DHGVPESPDSILE------------LLRAVKKNLNQSESSGP-VVVHCSAGVGRTGTFVAIDILLQQLEAEA 70
 
Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 152-570 6.86e-174

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: 499.31  E-value: 6.86e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    152 SPDSWDIYDPIKEFRRQGLDSKDetcPWRLSTVNEHYEFCPTYPSKLFVPRSTSDILLKHASKFRSQKRIPVLTYHHKAT 231
Cdd:pfam06602   1 EENGWDLYDPEAEFARQGLPSKD---EWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKEN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    232 DCNILRSSQPLPGLINQRSIQDEKLVWESFNSFCNKDIRrtKHVIVDARPRTNALAQMALGGGTENMDNYnffladnnmg 311
Cdd:pfam06602  78 GAVITRSSQPLVGLNGKRSIEDEKLLQAIFKSSNPYSAK--KLYIVDARPKLNAMANRAKGGGYENEDNY---------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    312 vdkslklPTVTRLFLGIDNIHIVSNTAAYMTEViCQGGDLNLPLEQNLIRSqkfSNWLKLNTLILKSVDMLLKSIIFNHS 391
Cdd:pfam06602 146 -------PNCKKIFLGIENIHVMRDSLNKLVEA-CNDRSPSMDKWLSRLES---SGWLKHIKAILDGACLIAQAVDLEGS 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    392 NVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHLNSdirfhdntmhsnfndvdtngdd 471
Cdd:pfam06602 215 SVLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAG---------------------- 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570    472 ldigvntqddyaeddeggedetnlinlsriskkfnenfklnKKSLKFVSPVFQQFLDCVYQLLTQNPDLFEFNERFLRRL 551
Cdd:pfam06602 273 -----------------------------------------FTDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRL 311

                         410
                  ....*....|....*....
gi 6322570    552 VYHLYSCQYGTFLSNSEKE 570
Cdd:pfam06602 312 LYHLYSCQFGTFLCNSEKE 330
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
 219-532 1.25e-131

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: 387.18  E-value: 1.25e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  219 KRIPVLTYHHKATDCNILRSSQPLPGLINQRSIQDEKLVWESFNSFCN-KDIRRTKHVIVDARPRTNALAQMALGGGTEN 297
Cdd:cd17666   1 QRIPVLTYLHKANGCSITRSSQPLVGLKQNRSIQDEKLVSEIFNTSINeIYISPQKNLIVDARPTTNAMAQVALGAGTEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  298 MDNYnffladnnmgvdkslKLPTVTRLFLGIDNIHIVSNTAAYMTEVICQGGDLNlPLEQNLIRSQKFSNWLKLNTLILK 377
Cdd:cd17666  81 MDNY---------------KYKTAKKIYLGIDNIHVMRDSLNKVTEALKDGDDSN-PSYPPLINALKKSNWLKYLAIILQ 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  378 SVDMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHlnsdirfhdnt 457
Cdd:cd17666 145 GADLIAKSIHFNHSHVLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFAERSGH----------- 213

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322570  458 mhsnfndvdtngddldigvntqddyaeddeggedetnlinlsriskkfnenfklnkkslKFVSPVFQQFLDCVYQ 532
Cdd:cd17666 214 -----------------------------------------------------------KETSPVFHQFLDCVYQ 229
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 161-557 3.28e-98

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: 303.88  E-value: 3.28e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  161 PIKEFRRQGLDSKDetcpWRLSTVNEHYEFCPTYPSKLFVPRSTSDILLKHASKFRSQKRIPVLTYHHKATDCNILRSSQ 240
Cdd:cd14532   1 LESEYTRMGVPNDN----WTLSDINKDYELCDTYPRELFVPTSASTPVLVGSSKFRSKGRLPVLSYLHKDNQAAICRCSQ 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  241 PLPGlINQRSIQDEKLVWESFNSFCNKDIrrtkHVIVDARPRTNALAQMALGGGTENMDNYnffladnnmgvdkslklPT 320
Cdd:cd14532  77 PLSG-FSARCVEDEQLLQAIRKANPNSKF----MYVVDTRPKINAMANKAAGKGYENEDNY-----------------SN 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  321 VTRLFLGIDNIHIVSNTAAYMTEVIcqggDLNLPLEQNLIRSQKFSNWLKLNTLILKSVDMLLKSIIFNHSnVLVHCSDG 400
Cdd:cd14532 135 IKFQFFGIENIHVMRSSLQKLLEVC----ELKNPSMSAFLSGLESSGWLKHIKAVMDTSVFIAKAVSEGAS-VLVHCSDG 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  401 WDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHLNSDIrfhdntmhsnfndvdtngddldigvntqd 480
Cdd:cd14532 210 WDRTAQTCSLASLLLDPYYRTIKGFQVLIEKEWLSFGHKFTDRCGHLQGDA----------------------------- 260

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322570  481 dyaeddeggedetnlinlsriskkfnenfklnkkslKFVSPVFQQFLDCVYQLLTQNPDLFEFNERFLRRLVYHLYS 557
Cdd:cd14532 261 ------------------------------------KEVSPVFTQFLDCVWQLMQQFPRAFEFNERFLLTLHDHVYS 301
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
 219-532 2.00e-95

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: 294.07  E-value: 2.00e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  219 KRIPVLTYHHKATDCNILRSSQPLPGLINQRSIQDEKLVwesfNSFCNKDIRRTKHVIVDARPRTNALAQMALGGGTENM 298
Cdd:cd14507   1 GRIPVLSWRHPRNGAVICRSSQPLVGLTGSRSKEDEKLL----NAIRKASPSSKKLYIVDARPKLNAVANRAKGGGYENT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  299 DNYnffladnnmgvdkslklPTVTRLFLGIDNIHIVSNTAAYMTEVICQGGDLnlplEQNLIRSQKFSNWLKLNTLILKS 378
Cdd:cd14507  77 EYY-----------------PNCELEFLNIENIHAMRDSLNKLRDACLSPNDE----ESNWLSALESSGWLEHIRLILKG 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  379 VDMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHLNSDirfhdntm 458
Cdd:cd14507 136 AVRVADLLEKEGTSVLVHCSDGWDRTSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDKN-------- 207

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322570  459 hsnfndvdtngddldigvntqddyaeddeGGEDETnlinlsriskkfnenfklnkkslkfvSPVFQQFLDCVYQ 532
Cdd:cd14507 208 -----------------------------SSDEER--------------------------SPIFLQFLDCVWQ 226
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 156-557 9.56e-77

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: 248.25  E-value: 9.56e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  156 WDIYDPIKEFRRQGLDSKDetcpWRLSTVNEHYEFCPTYPSKLFVPRSTSDILLKHASKFRSQKRIPVLTYHHKATDCNI 235
Cdd:cd14584   2 WKLIDLKVDFQRMGIPNDY----WEITDANKNYEICSTYPPELVVPKSASKATVVGSSKFRSRGRFPVLSYLYKENNAAI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  236 LRSSQPLPGLiNQRSIQDEKLVwesfnsfcnKDIRRTK-----HVIVDARPRTNALAQMALGGGTENMDNYnffladnnm 310
Cdd:cd14584  78 CRCSQPLSGF-SARCVEDEQML---------QAISKANpgspfMYVVDTRPKLNAMANRAAGKGYENEDNY--------- 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  311 gvdkslklPTVTRLFLGIDNIHIVSNTAAYMTEViCQggdLNLPLEQNLIRSQKFSNWLKLNTLILKSVDMLLKSIIFNH 390
Cdd:cd14584 139 --------SNIRFQFIGIENIHVMRSSLQKLLEV-CE---MKSPSMSDFLTGLENSGWLRHIKAVMDAGVFLAKAVKEEK 206

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  391 SNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHLNSDIrfhdntmhsnfndvdtngd 470
Cdd:cd14584 207 ASVLVHCSDGWDRTAQVCSLASLLLDPFYRTIKGLMVLIEKEWISMGHKFSQRCGHLDGDP------------------- 267

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  471 dldigvntqddyaeddeggedetnlinlsriskkfnenfklnkkslKFVSPVFQQFLDCVYQLLTQNPDLFEFNERFLRR 550
Cdd:cd14584 268 ----------------------------------------------KEVSPVFTQFLECVWQLMEQFPCAFEFNEHFLLE 301


                ....*..
gi 6322570  551 LVYHLYS 557
Cdd:cd14584 302 IHDHVFS 308
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 164-557 6.42e-75

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: 243.33  E-value: 6.42e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  164 EFRRQGLDSKdetcPWRLSTVNEHYEFCPTYPSKLFVPRSTSDILLKHASKFRSQKRIPVLTYHHKATDCNILRSSQPLP 243
Cdd:cd14583   4 EYNRMGLPNS----LWQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYYCKDNNASICRSSQPLS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  244 GLiNQRSIQDEKLVWESFNSFCNKDIRrtkhVIVDARPRTNALAQMALGGGTENMDNYNffladnnmgvdkslklpTVTR 323
Cdd:cd14583  80 GF-SARCLEDEQMLQAIRKANPGSDFM----YVVDTRPKLNAMANRAAGKGYENEDNYS-----------------NIKF 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  324 LFLGIDNIHIVSNTAAYMTEViCQggdLNLPLEQNLIRSQKFSNWLKLNTLILKSVDMLLKSIIFNHSNVLVHCSDGWDR 403
Cdd:cd14583 138 QFIGIENIHVMRNSLQKMLEV-CE---LRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDR 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  404 TSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHLNSDIrfhdntmhsnfndvdtngddldigvntqddya 483
Cdd:cd14583 214 TAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKFNHRYGHLDGDP-------------------------------- 261

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322570  484 eddeggedetnlinlsriskkfnenfklnkkslKFVSPVFQQFLDCVYQLLTQNPDLFEFNERFLRRLVYHLYS 557
Cdd:cd14583 262 ---------------------------------KEVSPVIDQFIECVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 163-557 7.65e-72

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: 235.21  E-value: 7.65e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  163 KEFRRQGLDSKDetcpWRLSTVNEHYEFCPTYPSKLFVPRSTSDILLKHASKFRSQKRIPVLTYHHKATDCNILRSSQPL 242
Cdd:cd14585   3 EEYKRMGVPNDY----WQLSDVNRDYKICDTYPRDLYVPITASKPIIVGSSKFRSKGRFPVLSYYHQEKKAAICRCSQPL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  243 PGLiNQRSIQDEKLVwesfnsfcnKDIRRTKHV-----IVDARPRTNALAQMALGGGTENMDNYNffladnnmgvdkslk 317
Cdd:cd14585  79 SGF-SARCLEDEHML---------QAISKANPNnrymyVMDTRPKLNAMANRAAGKGYENEDNYS--------------- 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  318 lpTVTRLFLGIDNIHIVSNTAAYMTEVIcqgGDLNLPLeQNLIRSQKFSNWLKLNTLILKSVDMLLKSIIFNHSNVLVHC 397
Cdd:cd14585 134 --NIRFQFVGIENIHVMRSSLQKLLEVC---GTKALSV-NDFLSGLESSGWLRHIKAVLDAAVFLAKAVAVEGASVLVHC 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  398 SDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHLNSDIrfhdntmhsnfndvdtngddldigvn 477
Cdd:cd14585 208 SDGWDRTAQVCSLGSLLLDPYYRTIKGFMVLIEKDWISFGHKFSDRCGQLDGDP-------------------------- 261

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  478 tqddyaeddeggedetnlinlsriskkfnenfklnkkslKFVSPVFQQFLDCVYQLLTQNPDLFEFNERFLRRLVYHLYS 557
Cdd:cd14585 262 ---------------------------------------KEISPVFTQFLECVWQLTEQFPRAFEFSEAFLLQIHEHIHS 302
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 209-556 1.33e-56

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: 193.33  E-value: 1.33e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  209 LKHASKFRSQKRIPVLTYHHKATDCNILRSSQPLPGLINQRSIQDEKLVwesfNSFCNKDIRRTKHVIVDARPRTNALAQ 288
Cdd:cd14590   4 LKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYL----QAIMDSNAQSHKIFIFDARPSVNAVAN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  289 MALGGGTENMDNYNffladnnmgvdkslklpTVTRLFLGIDNIHIVSNTAAYMTEVICQGGDlnlplEQNLIRSQKFSNW 368
Cdd:cd14590  80 KAKGGGYESEDAYQ-----------------NAELVFLDIHNIHVMRESLRKLKEIVYPNIE-----ESHWLSNLESTHW 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  369 LKLNTLILKSVDMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHLN 448
Cdd:cd14590 138 LEHIKLILAGALRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGD 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  449 sdirfhdntmhSNFNDVDTngddldigvntqddyaeddeggedetnlinlsriskkfnenfklnkkslkfvSPVFQQFLD 528
Cdd:cd14590 218 -----------KNHADADR----------------------------------------------------SPVFLQFID 234

                       330       340
                ....*....|....*....|....*...
gi 6322570  529 CVYQLLTQNPDLFEFNERFLRRLVYHLY 556
Cdd:cd14590 235 CVWQMTRQFPTAFEFNEYFLITILDHLY 262
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 179-446 9.32e-56

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: 192.56  E-value: 9.32e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  179 WRLSTVNEHYEFCPTYPSKLFVPRSTSDILLKHASKFRSQKRIPVLTYHHKATDCNILRSSQPLPGLINQRSIQDEKLV- 257
Cdd:cd14587   3 WRVSEINSNYKLCSSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAVIARCSQPEISWWGWRNADDEYLVt 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  258 ----------------------WESFNSFCNKDIRRT--------------KHVIVDARPRTNALAQMALGGGTENMDNY 301
Cdd:cd14587  83 siakacaldpgtrapggspskgNSDGSDASDTDFDSSltacsavesgaapqKLLILDARSYTAAVANRAKGGGCECEEYY 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  302 nffladnnmgvdkslklPTVTRLFLGIDNIHIVSNTAAYMTEVICQggdlnLPLEQNLIRSQKFSNWLKLNTLILKSVDM 381
Cdd:cd14587 163 -----------------PNCEVMFMGMANIHSIRNSFQYLRAVCSQ-----MPDPGNWLSALESTKWLQHLSVMLKAAVL 220

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322570  382 LLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGH 446
Cdd:cd14587 221 VASAVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGH 285
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
 220-556 9.54e-54

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: 184.96  E-value: 9.54e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  220 RIPVLTYHHKATDCNILRSSQPLPGLINQRSIQDEKLVwesfNSFCNKDIRRTKHVIVDARPRTNALAQMALGGGTENMD 299
Cdd:cd14535   2 RIPVLSWIHPESQATITRCSQPLVGVSGKRSKDDEKYL----QLIMDANAQSHKLFIMDARPSVNAVANKAKGGGYESED 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  300 NYnffladnnmgvdkslklPTVTRLFLGIDNIHIVSNTAAYMTEVICQGGDlnlplEQNLIRSQKFSNWLKLNTLILKSV 379
Cdd:cd14535  78 AY-----------------QNAELVFLDIHNIHVMRESLRKLKDICFPNID-----DSHWLSNLESTHWLEHIKLILAGA 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  380 DMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHlnsdirfhdntmh 459
Cdd:cd14535 136 VRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGH------------- 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  460 snfndvdtnGDdldigvntqDDYAEDDEggedetnlinlsriskkfnenfklnkkslkfvSPVFQQFLDCVYQLLTQNPD 539
Cdd:cd14535 203 ---------GD---------KNHSDADR--------------------------------SPVFLQFIDCVWQMTRQFPN 232

                       330
                ....*....|....*..
gi 6322570  540 LFEFNERFLRRLVYHLY 556
Cdd:cd14535 233 AFEFNEHFLITILDHLY 249
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 179-450 5.35e-53

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: 185.22  E-value: 5.35e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  179 WRLSTVNEHYEFCPTYPSKLFVPRSTSDILLKHASKFRSQKRIPVLTYHHKATDCNILRSSQPLPGLINQRSIQDEKLVw 258
Cdd:cd14586   8 WRISNINEKYKLCGSYPQELIVPAWITDKELESVASFRSWKRIPAVVYRHQSNGAVIARCGQPEVSWWGWRNADDEHLV- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  259 ESFNSFCNKDIRRTKHV------------------------------------------IVDARPRTNALAQMALGGGTE 296
Cdd:cd14586  87 QSVAKACASDSSSCKSVlmtgncsrdfpnggdlsdvefdssmsnasgveslaiqpqkllILDARSYAAAVANRAKGGGCE 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  297 NMDNYnffladnnmgvdkslklPTVTRLFLGIDNIHIVSNTAAYMTEVICQggdlnLPLEQNLIRSQKFSNWLKLNTLIL 376
Cdd:cd14586 167 CPEYY-----------------PNCEVVFMGMANIHSIRKSFQSLRLLCTQ-----MPDPANWLSALESTKWLQHLSMLL 224

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322570  377 KSVDMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGH-LNSD 450
Cdd:cd14586 225 KSALLVVHAVDRDQRPVLVHCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRCGHgENSD 299
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
 220-556 9.96e-52

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: 179.45  E-value: 9.96e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  220 RIPVLTYHHKATDCNILRSSQPLPGLINQRSIQDEK---LVWESfnsfcNKDIrrTKHVIVDARPRTNALAQMALGGGTE 296
Cdd:cd14591   2 RIPVLSWIHPENQAVIMRCSQPLVGMSGKRNKDDEKyldIIREA-----NGQT--SKLTIYDARPSVNAVANKATGGGYE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  297 NMDNYnffladnnmgvdkslklPTVTRLFLGIDNIHIvsntaayMTEVICQGGDLNLPL--EQNLIRSQKFSNWLKLNTL 374
Cdd:cd14591  75 GDDAY-----------------QNAELVFLDIHNIHV-------MRESLKKLKDIVYPNveESHWLSSLESTHWLEHIKL 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  375 ILKSVDMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHlnsdirfh 454
Cdd:cd14591 131 VLTGAIQVADKVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGH-------- 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  455 dntmhsnfndvdtnGDdldigvntqDDYAEDDEggedetnlinlsriskkfnenfklnkkslkfvSPVFQQFLDCVYQLL 534
Cdd:cd14591 203 --------------GD---------KNHADADR--------------------------------SPIFLQFIDCVWQMS 227

                       330       340
                ....*....|....*....|..
gi 6322570  535 TQNPDLFEFNERFLRRLVYHLY 556
Cdd:cd14591 228 KQFPTAFEFNEQFLITILDHLY 249
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 219-532 1.58e-49

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: 172.97  E-value: 1.58e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  219 KRIPVLTYHHKATDCNILRSSQPLPGLINQRSIQDEKLVwESFNSFCNKDIRRTKHVIVDARPRTNALAQMALGGGTENM 298
Cdd:cd14533   2 KRIPSVVWRHQRNGAVIARCSQPEVGWLGWRNAEDENLL-QAIAEACASNASPKKLLIVDARSYAAAVANRAKGGGCECP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  299 DNYnffladnnmgvdkslklPTVTRLFLGIDNIHIVSNTAAYMTEVICQGGDlnlplEQNLIRSQKFSNWLKLNTLILKS 378
Cdd:cd14533  81 EYY-----------------PNCEVVFMNLANIHAIRKSFHSLRALCSSAPD-----QPNWLSNLESTKWLHHLSGLLKA 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  379 VDMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHlnsdirfhdntm 458
Cdd:cd14533 139 ALLVVNAVDEEGRPVLVHCSDGWDRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFGHKFADRCGH------------ 206

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322570  459 hsnfndvdtngddldiGVNTQDDyaeddeggedetnlinlsriskkfNENfklnkkslkfvSPVFQQFLDCVYQ 532
Cdd:cd14533 207 ----------------GVNSEDI------------------------NER-----------CPVFLQWLDCVHQ 229
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 220-556 1.84e-45

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: 162.46  E-value: 1.84e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  220 RIPVLTYHHKATDCNILRSSQPLPGLINQRSIQDEKLVwesfNSFCNKDIRRTKHVIVDARPRTNALAQMALGGGTENMD 299
Cdd:cd14592   2 RVPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYL----QTIMDANAQSHKLIIFDARQNSVADTNKTKGGGYESES 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  300 NYnffladnnmgvdkslklPTVTRLFLGIDNIHIVSNTAAYMTEVICQGGDlnlplEQNLIRSQKFSNWLKLNTLILKSV 379
Cdd:cd14592  78 AY-----------------PNAELVFLEIHNIHVMRESLRKLKEIVYPSID-----EARWLSNVDGTHWLEYIRMLLAGA 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  380 DMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHlnsdirfhdntmh 459
Cdd:cd14592 136 VRIADKIESGKTSVVVHCSDGWDRTAQLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGH------------- 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  460 snfndvdtnGDdldigvntqDDYAEDDEggedetnlinlsriskkfnenfklnkkslkfvSPVFQQFLDCVYQLLTQNPD 539
Cdd:cd14592 203 ---------GD---------DNHADADR--------------------------------SPIFLQFIDCVWQMTRQFPS 232

                       330
                ....*....|....*..
gi 6322570  540 LFEFNERFLRRLVYHLY 556
Cdd:cd14592 233 AFEFNELFLITILDHLY 249
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 179-536 6.96e-37

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: 139.42  E-value: 6.96e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  179 WRLSTVNEHYEFCPTYPSKLFVPRSTSDILLKHASKFRSQKRIPVLTYHHKATDCNILRSSQP-LPGLINQRSIQDeklv 257
Cdd:cd14534   1 FRISTANRDYSICRSYPALVVVPQSVSDESLRKVARCYRQGRFPVVTWRHPRTKALLLRSGGFhGKGVMGMLKSAN---- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  258 weSFNSFCNKDIRRTKHVIVDARpRTNALAQMALGggtenmdnynffladnnmgvDKSLKLPTVTRLFLGIDNIHI---- 333
Cdd:cd14534  77 --TSTSSPTVSSSETSSSLEQEK-YLSALVLYVLG--------------------EKSQMKGVKAESDPKCEFIPVeype 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  334 VSNTAAYMTEVI--CQGGDLNLPLEQNLIRSQKFSNWL-KLNTLILKS---VDMllksIIFNHSNVLVHCSDGWDRTSQV 407
Cdd:cd14534 134 VRQVKASFKKLLraCVPSSAPTEPEQSFLKAVEDSEWLqQLQCLMQLSgavVDL----LDVQGSSVLLCLEDGWDVTTQV 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  408 VSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHLNsdirfhdNTMHSNFndvdtngddldigvntqddyaedde 487
Cdd:cd14534 210 SSLSQLLLDPYYRTLEGFRVLVEKEWLAFGHRFSHRSNLTA-------ASQSSGF------------------------- 257

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 6322570  488 ggedetnlinlsriskkfnenfklnkkslkfvSPVFQQFLDCVYQLLTQ 536
Cdd:cd14534 258 --------------------------------APVFLQFLDAVHQIHRQ 274
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 179-446 1.13e-30

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: 122.00  E-value: 1.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  179 WRLSTVNEHYEFCPTYPSKLFVPRSTSDILLKHASKFRSQKRIPVLTYHHKATDCNILRS----SQPLPGLINQrsiQDE 254
Cdd:cd14588   1 FRISTVNRMYAVCRSYPGLLIVPQSIQDNTIQRISRCYRQNRFPVVCWRNSRTKAVLLRSgglhGKGVVGLFKS---QNA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  255 KLVWESFNSFCNKDIRRTKHVIVDARPR-TNALAQMALGGgtenMDNYNFFLADNNM--GVdKSLKLPTVTRLFLGIDNI 331
Cdd:cd14588  78 PAAGQSQTDSTSLEQEKYLQAVINSMPRyADASGRNTLSG----FRAALYIIGDKSQlkGV-KQDPLQQWEVVPIEVFDV 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  332 HIVSNTAAYMTEViCQGGDLNLPLEQNLIRSQKFSNWLKLNTLILKsVDMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLL 411
Cdd:cd14588 153 RQVKASFKKLMKA-CVPSCPSTDPSQTYLRTLEESEWLSQLHKLLQ-VSVLVVELLDSGSSVLVSLEDGWDITTQVVSLV 230

                       250       260       270
                ....*....|....*....|....*....|....*
gi 6322570  412 EICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGH 446
Cdd:cd14588 231 QLLSDPYYRTIEGFRLLVEKEWLSFGHRFSHRGAQ 265
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 220-446 9.46e-27

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: 108.96  E-value: 9.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  220 RIPVLTYHHKATDCNILRSSQPLPGLINQRSIQDEKLVwesfnsfcNKDIRRTKH-VIVDARPRTNALAQMALGGGTENM 298
Cdd:cd14536   2 RFPVLSYYHKKNGMVLMRSSQPLTGPNGKRCKEDEKLL--------NAVLGGGKRgYIIDTRSKNVAQQARAKGGGFEPE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  299 DNYnffladnnmgvdkslklPTVTRLFLGIDNIHIVSNTaayMTEVICQGGDLNLPLEQNLIRSQKfSNWLKLNTLILKS 378
Cdd:cd14536  74 AHY-----------------PQWRRIHKPIERYNVLQES---LIKLVEACNDQGHSMDKWLSKLES-SNWLSHVKEILTT 132

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322570  379 VDMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGH 446
Cdd:cd14536 133 ACLVAQCIDREGASVLVHGSEGMDSTLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRCAK 200
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 179-536 5.94e-25

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: 105.77  E-value: 5.94e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  179 WRLSTVNEHYEFCPTYPSKLFVPRSTSDILLKHASKFRSQKRIPVLTYHHKATDCNILRS----SQPLPGLINQR----- 249
Cdd:cd14589   1 FRITAVNRMYSLCRSYPGLLVVPQSVQDSSLQKVARCYRHNRLPVVCWKNSKTKAVLLRSggfhGKGVVGLFKSQnphsa 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  250 ---------SIQDEKLVWESFNSFCNKDIRRTKHVIVDARPRTNAlAQMALGGGTENMDNYNFfladnnmgvDKSLKLPT 320
Cdd:cd14589  81 apassesssSIEQEKYLQALLNAISVHQKMNGNSTLLQSQLLKRQ-AALYIFGEKSQLRGFKL---------DFALNCEF 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  321 VTRLFlgidniHIVSNTAAYMTEVI--CQGGDLNLPLEQNLIRSQKFSNW-LKLNTLILKSVdmLLKSIIFNHSNVLVHC 397
Cdd:cd14589 151 VPVEF------HDIRQVKASFKKLMraCVPSTIPTDSEVTFLKALGESEWfLQLHRIMQLAV--VISELLESGSSVMVCL 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  398 SDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSghlnsdirfhdntmhsnfndvdtngddldigvn 477
Cdd:cd14589 223 EDGWDITTQVVSLVQLLSDPFYRTLEGFQMLVEKEWLSFGHKFSQRS--------------------------------- 269

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6322570  478 tqddyaeddeggedetnlinlsriskkfneNFKLNKKSLKFVsPVFQQFLDCVYQLLTQ 536
Cdd:cd14589 270 ------------------------------NLTPNSQGSGFA-PIFLQFLDCVHQIHNQ 297
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 366-450 9.17e-12

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: 64.67  E-value: 9.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  366 SNWLKLNTLILKSVDMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSG 445
Cdd:cd14537  97 TKWLHYVSACLKKASEAAEALESRGRSVVLQESDGRDLSCVVSSLVQLLLDPHFRTITGFQSLIQKEWVALGHPFCDRLG 176


                ....*
gi 6322570  446 HLNSD 450
Cdd:cd14537 177 HVKPN 181
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 366-454 3.38e-11

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: 62.94  E-value: 3.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  366 SNWLKLNTLILKSVDMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSG 445
Cdd:cd14594 101 SNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQSLIQKEWVMGGHCFLDRCN 180


                ....*....
gi 6322570  446 HLNSDIRFH 454
Cdd:cd14594 181 HLRQNDKEE 189
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 356-447 5.20e-11

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: 62.22  E-value: 5.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  356 EQNLIRSQKFSNWLKLNTLILKSVDMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCS 435
Cdd:cd14593  84 EEKWLSSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLVQVMLDPYFRTITGFQSLIQKEWVM 163

                        90
                ....*....|..
gi 6322570  436 FGHRFLERSGHL 447
Cdd:cd14593 164 AGYRFLDRCNHL 175
PH-GRAM_MTMR9 cd13211
Myotubularian (MTM) related 9 protein (MTMR9) Pleckstrin Homology-Glucosyltransferases, ...
 1-44 1.97e-08

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: 52.28  E-value: 1.97e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 6322570    1 MEYIKIAKVSNVVLHRRGTATQ-GTLHLTTHHLIFESPQL-STEFW 44
Cdd:cd13211   4 AELIKTPKVDNVVLHRPPRPAVeGTLCITGHHLILSSRQDnAEELW 49
PH-GRAM_MTMR6-like cd13210
Myotubularian (MTM) related (MTMR) 7 and 8 proteins Pleckstrin Homology-Glucosyltransferases, ...
 4-66 3.86e-08

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: 51.51  E-value: 3.86e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322570    4 IKIAKVSNVVL---HRRGTATQGTLHLTTHHLIFESPQLSTEFWFPYPLIYGVHKNPGSTLLSKLT 66
Cdd:cd13210   1 IRTPKVENVRLldrFSSRKPAVGTLYLTATHLIFVEPSGKKETWILHSHIASVEKLPLTTAGCPLV 66
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 366-450 6.06e-07

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: 50.60  E-value: 6.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322570  366 SNWLKLNTLILK---SVDMLLKSiifNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLE 442
Cdd:cd14595  93 TRWLDHVRACLRkasEVSCLLAE---RHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEWVVAGHPFLQ 169


                ....*....
gi 6322570  443 R-SGHLNSD 450
Cdd:cd14595 170 RlNLTRESD 178
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
350-421 1.58e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 44.27  E-value: 1.58e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322570     350 DLNLPLEQNLIRSqkfsnwlklntlILKSVDMLLKSIIFNHSnVLVHCSDGWDRTSQVVSLLEICLDPFYRT 421
Cdd:smart00404  12 DHGVPESPDSILE------------LLRAVKKNLNQSESSGP-VVVHCSAGVGRTGTFVAIDILLQQLEAEA 70
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 350-421 1.58e-05

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: 44.27  E-value: 1.58e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322570     350 DLNLPLEQNLIRSqkfsnwlklntlILKSVDMLLKSIIFNHSnVLVHCSDGWDRTSQVVSLLEICLDPFYRT 421
Cdd:smart00012  12 DHGVPESPDSILE------------LLRAVKKNLNQSESSGP-VVVHCSAGVGRTGTFVAIDILLQQLEAEA 70
PH-GRAM_MTMR7 cd13344
Myotubularian (MTM) related 7 protein (MTMR7) Pleckstrin Homology-Glucosyltransferases, ...
 1-60 6.37e-05

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: 42.60  E-value: 6.37e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322570    1 MEYIKIAKVSNVVLHRRGT---ATQGTLHLTTHHLIF--ESPQLSTEFWFPYPLIYGVHKNPGST 60
Cdd:cd13344   1 MEHIRMPKVENVRLVDRISskkAALGTLYLTATHVIFveNSSDTRKETWILHSQISSIEKQATTA 65
PH-GRAM_MTMR8 cd13345
Myotubularian (MTM) related 8 protein (MTMR8) Pleckstrin Homology-Glucosyltransferases, ...
 1-66 1.27e-03

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: 38.79  E-value: 1.27e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322570    1 MEYIKIAKVSNVVLHRRGT---ATQGTLHLTTHHLIF--ESPQLSTEFWFPYPLIYGVHKNPGSTLLSKLT 66
Cdd:cd13345   1 MEHITTPKVENVKLLDRYTnkkPANGTLYLTATHLIYveASGAARKETWILHHHIATVEKLPLTSLGCPLL 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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