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Conserved domains on  [gi|240255320|ref|NP_187666|]
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Myotubularin-like phosphatases II superfamily [Arabidopsis thaliana]

Protein Classification

myotubularin family protein( domain architecture ID 10651461)

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 ...
 218-591 1.05e-159

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: 468.11  E-value: 1.05e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  218 SNELWRISDLNSNYNLCQTYPFAFMIPKSISDAELLQACSFRARCRLPVITWCQPGSGAVIARSSQPLVGLMMNmRSNLD 297
Cdd:pfam06602  21 SKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVITRSSQPLVGLNGK-RSIED 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  298 EKLVAAFCSQlpGAKGERRKLYIADARPRKNALANGAMGGGSESSSNYFQSEIVFFGIDNIHAMRESFSRVRDYLDMhgt 377
Cdd:pfam06602 100 EKLLQAIFKS--SNPYSAKKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACND--- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  378 tssdgrssflrhggwtwgggNLSSMSASVSLLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLA 457
Cdd:pfam06602 175 --------------------RSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  458 CLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGMPNISGSgnfdfprqsssagsfpsspvrqssgsaasqssssshgHN 537
Cdd:pfam06602 235 QLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGFTD-------------------------------------SK 277

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240255320  538 NYSPIFMQWIDSVSQLMRMYPCAFEFSPTFLVDFMDCLLSCRFGNFLCNSEKER 591
Cdd:pfam06602 278 ERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKER 331
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
52-111 1.76e-08

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


:

Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 51.44  E-value: 1.76e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240255320    52 CLLESERVIVEgYGVVLINT-DEAGTLLVTNFRILFLSEGTRKVIpLGTIPLATIEKFNKM 111
Cdd:smart00568   1 KLPEEEKLIAD-YSCYLSRTgPVQGRLYISNYRLCFRSNLPGKLT-KVVIPLADITRIEKS 59
 
Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 218-591 1.05e-159

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: 468.11  E-value: 1.05e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  218 SNELWRISDLNSNYNLCQTYPFAFMIPKSISDAELLQACSFRARCRLPVITWCQPGSGAVIARSSQPLVGLMMNmRSNLD 297
Cdd:pfam06602  21 SKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVITRSSQPLVGLNGK-RSIED 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  298 EKLVAAFCSQlpGAKGERRKLYIADARPRKNALANGAMGGGSESSSNYFQSEIVFFGIDNIHAMRESFSRVRDYLDMhgt 377
Cdd:pfam06602 100 EKLLQAIFKS--SNPYSAKKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACND--- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  378 tssdgrssflrhggwtwgggNLSSMSASVSLLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLA 457
Cdd:pfam06602 175 --------------------RSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  458 CLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGMPNISGSgnfdfprqsssagsfpsspvrqssgsaasqssssshgHN 537
Cdd:pfam06602 235 QLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGFTD-------------------------------------SK 277

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240255320  538 NYSPIFMQWIDSVSQLMRMYPCAFEFSPTFLVDFMDCLLSCRFGNFLCNSEKER 591
Cdd:pfam06602 278 ERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKER 331
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
 262-552 5.42e-107

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: 327.97  E-value: 5.42e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 262 CRLPVITWCQPGSGAVIARSSQPLVGLMmNMRSNLDEKLVAAFCSQLPGAKgerrKLYIADARPRKNALANGAMGGGSES 341
Cdd:cd14507    1 GRIPVLSWRHPRNGAVICRSSQPLVGLT-GSRSKEDEKLLNAIRKASPSSK----KLYIVDARPKLNAVANRAKGGGYEN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 342 SSNYFQSEIVFFGIDNIHAMRESFSRVRDYLDMHGttssdgrssflrhggwtwgggnlSSMSASVSLLGDSGWLIHIQSV 421
Cdd:cd14507   76 TEYYPNCELEFLNIENIHAMRDSLNKLRDACLSPN-----------------------DEESNWLSALESSGWLEHIRLI 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 422 LAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGMPNISGSgnf 501
Cdd:cd14507  133 LKGAVRVADLLEKEGTSVLVHCSDGWDRTSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDKNSS--- 209

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 240255320 502 dfprqsssagsfpsspvrqssgsaasqssssshgHNNYSPIFMQWIDSVSQ 552
Cdd:cd14507  210 ----------------------------------DEERSPIFLQFLDCVWQ 226
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
52-111 1.76e-08

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 51.44  E-value: 1.76e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240255320    52 CLLESERVIVEgYGVVLINT-DEAGTLLVTNFRILFLSEGTRKVIpLGTIPLATIEKFNKM 111
Cdd:smart00568   1 KLPEEEKLIAD-YSCYLSRTgPVQGRLYISNYRLCFRSNLPGKLT-KVVIPLADITRIEKS 59
PH-GRAM_MTM-like cd13223
Myotubularian 1 and related proteins Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase; ...
 75-161 7.76e-07

Myotubularian 1 and related proteins Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase; MTM1, MTMR1, and MTMR2 are members of the myotubularin protein phosphatase gene family. They contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. In addition MTMR1 (Myotubularian related 1 protein) and MTMR2 (Myotubularian related 2 protein) contain a C-terminal PDZ domain. Mutations in MTMR2 are a cause of Charcot-Marie-Tooth disease type 4B, an autosomal recessive demyelinating neuropathy. The protein can self-associate and form heteromers with MTMR5 and MTMR12. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date.


Pssm-ID: 275407  Cd Length: 100  Bit Score: 48.00  E-value: 7.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  75 GTLLVTNFRILFLSE--GTRKV--IPLGTIplATIEKfnkmvlkVQSSPRQSDKIpprRLLQVTGKDMRIIVYGFRPRTK 150
Cdd:cd13223   18 GTLYITNYRLYFKSRdrEPNFVldVPLGVI--SRVEK-------VGGATSRGENS---YGLEIHCKDMRNLRFAHKQENH 85

                         90
                 ....*....|.
gi 240255320 151 QRRNVFDALLK 161
Cdd:cd13223   86 SRRKLYETLQK 96
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
434-467 1.06e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 45.04  E-value: 1.06e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 240255320   434 MESASVLVHCSDGWDRTTQLVSLACLLLDPYYRT 467
Cdd:smart00404  37 ESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA 70
 
Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 218-591 1.05e-159

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: 468.11  E-value: 1.05e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  218 SNELWRISDLNSNYNLCQTYPFAFMIPKSISDAELLQACSFRARCRLPVITWCQPGSGAVIARSSQPLVGLMMNmRSNLD 297
Cdd:pfam06602  21 SKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVITRSSQPLVGLNGK-RSIED 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  298 EKLVAAFCSQlpGAKGERRKLYIADARPRKNALANGAMGGGSESSSNYFQSEIVFFGIDNIHAMRESFSRVRDYLDMhgt 377
Cdd:pfam06602 100 EKLLQAIFKS--SNPYSAKKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACND--- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  378 tssdgrssflrhggwtwgggNLSSMSASVSLLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLA 457
Cdd:pfam06602 175 --------------------RSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  458 CLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGMPNISGSgnfdfprqsssagsfpsspvrqssgsaasqssssshgHN 537
Cdd:pfam06602 235 QLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGFTD-------------------------------------SK 277

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240255320  538 NYSPIFMQWIDSVSQLMRMYPCAFEFSPTFLVDFMDCLLSCRFGNFLCNSEKER 591
Cdd:pfam06602 278 ERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKER 331
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
 262-552 5.42e-107

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: 327.97  E-value: 5.42e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 262 CRLPVITWCQPGSGAVIARSSQPLVGLMmNMRSNLDEKLVAAFCSQLPGAKgerrKLYIADARPRKNALANGAMGGGSES 341
Cdd:cd14507    1 GRIPVLSWRHPRNGAVICRSSQPLVGLT-GSRSKEDEKLLNAIRKASPSSK----KLYIVDARPKLNAVANRAKGGGYEN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 342 SSNYFQSEIVFFGIDNIHAMRESFSRVRDYLDMHGttssdgrssflrhggwtwgggnlSSMSASVSLLGDSGWLIHIQSV 421
Cdd:cd14507   76 TEYYPNCELEFLNIENIHAMRDSLNKLRDACLSPN-----------------------DEESNWLSALESSGWLEHIRLI 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 422 LAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGMPNISGSgnf 501
Cdd:cd14507  133 LKGAVRVADLLEKEGTSVLVHCSDGWDRTSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDKNSS--- 209

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 240255320 502 dfprqsssagsfpsspvrqssgsaasqssssshgHNNYSPIFMQWIDSVSQ 552
Cdd:cd14507  210 ----------------------------------DEERSPIFLQFLDCVWQ 226
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 217-577 5.71e-99

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: 310.04  E-value: 5.71e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 217 LSNELWRISDLNSNYNLCQTYPFAFMIPKSISDAELLQACSFRARCRLPVITWCQPGSGAVIARSSQPLVGlmMNMRSNL 296
Cdd:cd14532   10 VPNDNWTLSDINKDYELCDTYPRELFVPTSASTPVLVGSSKFRSKGRLPVLSYLHKDNQAAICRCSQPLSG--FSARCVE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 297 DEKLVAAFCSQLPGAKgerrKLYIADARPRKNALANGAMGGGSESSSNYFQSEIVFFGIDNIHAMRESFSRVRDYLDMHG 376
Cdd:cd14532   88 DEQLLQAIRKANPNSK----FMYVVDTRPKINAMANKAAGKGYENEDNYSNIKFQFFGIENIHVMRSSLQKLLEVCELKN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 377 TtssdgrssflrhggwtwgggnlsSMSASVSLLGDSGWLIHIQSVLAGAAWIAARVAmESASVLVHCSDGWDRTTQLVSL 456
Cdd:cd14532  164 P-----------------------SMSAFLSGLESSGWLKHIKAVMDTSVFIAKAVS-EGASVLVHCSDGWDRTAQTCSL 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 457 ACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGmpNISGSGnfdfprqsssagsfpsspvrqssgsaasqssssshgh 536
Cdd:cd14532  220 ASLLLDPYYRTIKGFQVLIEKEWLSFGHKFTDRCG--HLQGDA------------------------------------- 260

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 240255320 537 NNYSPIFMQWIDSVSQLMRMYPCAFEFSPTFLVDFMDCLLS 577
Cdd:cd14532  261 KEVSPVFTQFLDCVWQLMQQFPRAFEFNERFLLTLHDHVYS 301
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 207-577 1.88e-79

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: 258.65  E-value: 1.88e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 207 MDMIED-GAFTLSNELWRISDLNSNYNLCQTYPFAFMIPKSISDAELLQACSFRARCRLPVITWCQPGSGAVIARSSQPL 285
Cdd:cd14584    5 IDLKVDfQRMGIPNDYWEITDANKNYEICSTYPPELVVPKSASKATVVGSSKFRSRGRFPVLSYLYKENNAAICRCSQPL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 286 VGLmmNMRSNLDEKLVAAFCSQLPGAKGerrkLYIADARPRKNALANGAMGGGSESSSNYFQSEIVFFGIDNIHAMRESF 365
Cdd:cd14584   85 SGF--SARCVEDEQMLQAISKANPGSPF----MYVVDTRPKLNAMANRAAGKGYENEDNYSNIRFQFIGIENIHVMRSSL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 366 SRVRDYLDMHGttssdgrssflrhggwtwgggnlSSMSASVSLLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSD 445
Cdd:cd14584  159 QKLLEVCEMKS-----------------------PSMSDFLTGLENSGWLRHIKAVMDAGVFLAKAVKEEKASVLVHCSD 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 446 GWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGmpNISGSgnfdfPRQSssagsfpsspvrqssgsa 525
Cdd:cd14584  216 GWDRTAQVCSLASLLLDPFYRTIKGLMVLIEKEWISMGHKFSQRCG--HLDGD-----PKEV------------------ 270

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 240255320 526 asqssssshghnnySPIFMQWIDSVSQLMRMYPCAFEFSPTFLVDFMDCLLS 577
Cdd:cd14584  271 --------------SPVFTQFLECVWQLMEQFPCAFEFNEHFLLEIHDHVFS 308
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 217-569 1.67e-77

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: 253.34  E-value: 1.67e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 217 LSNELWRISDLNSNYNLCQTYPFAFMIPKSISDAELLQACSFRARCRLPVITWCQPGSGAVIARSSQPLVGLmmNMRSNL 296
Cdd:cd14583   10 LPNSLWQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYYCKDNNASICRSSQPLSGF--SARCLE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 297 DEKLVAAFCSQLPGAkgerRKLYIADARPRKNALANGAMGGGSESSSNYFQSEIVFFGIDNIHAMRESFSRVRDYLDMHG 376
Cdd:cd14583   88 DEQMLQAIRKANPGS----DFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELRS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 377 TTSSDgrssFLrhggwtWGggnlssmsasvslLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSL 456
Cdd:cd14583  164 PSMGD----FL------WG-------------LENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSV 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 457 ACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGmpNISGSgnfdfPRQSssagsfpsspvrqssgsaasqssssshgh 536
Cdd:cd14583  221 ASLLLDPYYRTIKGFMVLIEKDWVSFGHKFNHRYG--HLDGD-----PKEV----------------------------- 264

                        330       340       350
                 ....*....|....*....|....*....|...
gi 240255320 537 nnySPIFMQWIDSVSQLMRMYPCAFEFSPTFLV 569
Cdd:cd14583  265 ---SPVIDQFIECVWQLMEQFPCAFEFNERFLI 294
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
 262-575 6.29e-77

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: 249.67  E-value: 6.29e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 262 CRLPVITWCQPGSGAVIARSSQPLVGlMMNMRSNLDEKLVAAFCSqlpgAKGERRKLYIADARPRKNALANGAMGGGSES 341
Cdd:cd14535    1 NRIPVLSWIHPESQATITRCSQPLVG-VSGKRSKDDEKYLQLIMD----ANAQSHKLFIMDARPSVNAVANKAKGGGYES 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 342 SSNYFQSEIVFFGIDNIHAMRESFSRVRDYL-----DMHgttssdgrssflrhggwtWgggnLSSMSASvsllgdsGWLI 416
Cdd:cd14535   76 EDAYQNAELVFLDIHNIHVMRESLRKLKDICfpnidDSH------------------W----LSNLEST-------HWLE 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 417 HIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGmpniS 496
Cdd:cd14535  127 HIKLILAGAVRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIG----H 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 497 GSGNF-DFPRqsssagsfpsspvrqssgsaasqssssshghnnySPIFMQWIDSVSQLMRMYPCAFEFSPTFLVDFMDCL 575
Cdd:cd14535  203 GDKNHsDADR----------------------------------SPVFLQFIDCVWQMTRQFPNAFEFNEHFLITILDHL 248
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 219-573 1.61e-73

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: 242.53  E-value: 1.61e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 219 NELWRISDLNSNYNLCQTYPFAFMIPKSISDAELLQACSFRARCRLPVITWCQPGSGAVIARSSQPLVGLmmNMRSNLDE 298
Cdd:cd14585   12 NDYWQLSDVNRDYKICDTYPRDLYVPITASKPIIVGSSKFRSKGRFPVLSYYHQEKKAAICRCSQPLSGF--SARCLEDE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 299 KLVAAFCSQLPGAkgerRKLYIADARPRKNALANGAMGGGSESSSNYFQSEIVFFGIDNIHAMRESFSRVrdyLDMHGTT 378
Cdd:cd14585   90 HMLQAISKANPNN----RYMYVMDTRPKLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKL---LEVCGTK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 379 SSdgrssflrhggwtwgggnlsSMSASVSLLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLAC 458
Cdd:cd14585  163 AL--------------------SVNDFLSGLESSGWLRHIKAVLDAAVFLAKAVAVEGASVLVHCSDGWDRTAQVCSLGS 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 459 LLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGmpNISGSgnfdfPRQSssagsfpsspvrqssgsaasqssssshghnn 538
Cdd:cd14585  223 LLLDPYYRTIKGFMVLIEKDWISFGHKFSDRCG--QLDGD-----PKEI------------------------------- 264

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 240255320 539 ySPIFMQWIDSVSQLMRMYPCAFEFSPTFLVDFMD 573
Cdd:cd14585  265 -SPVFTQFLECVWQLTEQFPRAFEFSEAFLLQIHE 298
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 249-575 1.62e-72

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: 238.39  E-value: 1.62e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 249 DAELLQACSFRARCRLPVITWCQPGSGAVIARSSQPLVGlMMNMRSNLDEKLVAAFCSqlpgAKGERRKLYIADARPRKN 328
Cdd:cd14590    1 DEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVG-VSGKRSKEDEKYLQAIMD----SNAQSHKIFIFDARPSVN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 329 ALANGAMGGGSESSSNYFQSEIVFFGIDNIHAMRESFSRVRD--YLDMHGTTssdgrssflrhggwtWgggnlssmsasV 406
Cdd:cd14590   76 AVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEivYPNIEESH---------------W-----------L 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 407 SLLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPF 486
Cdd:cd14590  130 SNLESTHWLEHIKLILAGALRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRF 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 487 SDRVGmpniSGSGNFDFPrqsssagsfpsspvrqssgsaasqssssshghnNYSPIFMQWIDSVSQLMRMYPCAFEFSPT 566
Cdd:cd14590  210 QLRVG----HGDKNHADA---------------------------------DRSPVFLQFIDCVWQMTRQFPTAFEFNEY 252


                 ....*....
gi 240255320 567 FLVDFMDCL 575
Cdd:cd14590  253 FLITILDHL 261
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
 263-496 8.59e-71

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: 232.72  E-value: 8.59e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 263 RLPVITWCQPGSGAVIARSSQPLVGLMMNmRSNLDEKLVAA-FCSQLPGAKGERRKLYIADARPRKNALANGAMGGGSES 341
Cdd:cd17666    2 RIPVLTYLHKANGCSITRSSQPLVGLKQN-RSIQDEKLVSEiFNTSINEIYISPQKNLIVDARPTTNAMAQVALGAGTEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 342 SSNYF--QSEIVFFGIDNIHAMRESFSRVRDYLdmhgttSSDGRSSflrhggwtwgggnlSSMSASVSLLGDSGWLIHIQ 419
Cdd:cd17666   81 MDNYKykTAKKIYLGIDNIHVMRDSLNKVTEAL------KDGDDSN--------------PSYPPLINALKKSNWLKYLA 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240255320 420 SVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGMPNIS 496
Cdd:cd17666  141 IILQGADLIAKSIHFNHSHVLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFAERSGHKETS 217
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
 262-575 2.87e-68

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: 226.45  E-value: 2.87e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 262 CRLPVITWCQPGSGAVIARSSQPLVGlMMNMRSNLDEKlvaaFCSQLPGAKGERRKLYIADARPRKNALANGAMGGGSES 341
Cdd:cd14591    1 NRIPVLSWIHPENQAVIMRCSQPLVG-MSGKRNKDDEK----YLDIIREANGQTSKLTIYDARPSVNAVANKATGGGYEG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 342 SSNYFQSEIVFFGIDNIHAMRESFSRVRDYLDMHGTTSSdgrssflrhggwtWgggnLSSMSASvsllgdsGWLIHIQSV 421
Cdd:cd14591   76 DDAYQNAELVFLDIHNIHVMRESLKKLKDIVYPNVEESH-------------W----LSSLEST-------HWLEHIKLV 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 422 LAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGmpniSGSGNF 501
Cdd:cd14591  132 LTGAIQVADKVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIG----HGDKNH 207

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240255320 502 -DFPRqsssagsfpsspvrqssgsaasqssssshghnnySPIFMQWIDSVSQLMRMYPCAFEFSPTFLVDFMDCL 575
Cdd:cd14591  208 aDADR----------------------------------SPIFLQFIDCVWQMSKQFPTAFEFNEQFLITILDHL 248
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 222-552 1.49e-65

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: 221.44  E-value: 1.49e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 222 WRISDLNSNYNLCQTYPFAFMIPKSISDAELLQACSFRARCRLPVITWCQPGSGAVIARSSQPLVGlMMNMRSNLDEKLV 301
Cdd:cd14587    3 WRVSEINSNYKLCSSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAVIARCSQPEIS-WWGWRNADDEYLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 302 ---AAFCSQLPGAK----------------------------------GERRKLYIADARPRKNALANGAMGGGSESSSN 344
Cdd:cd14587   82 tsiAKACALDPGTRapggspskgnsdgsdasdtdfdssltacsavesgAAPQKLLILDARSYTAAVANRAKGGGCECEEY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 345 YFQSEIVFFGIDNIHAMRESFSRVRDYLdmhgttssdgrSSFLRHGGWtwgggnlssmsasVSLLGDSGWLIHIQSVLAG 424
Cdd:cd14587  162 YPNCEVMFMGMANIHSIRNSFQYLRAVC-----------SQMPDPGNW-------------LSALESTKWLQHLSVMLKA 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 425 AAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGmpnisgsgnfdfp 504
Cdd:cd14587  218 AVLVASAVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCG------------- 284

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 240255320 505 rqsssagsfpsspvrqssgsaasqSSSSSHGHNNYSPIFMQWIDSVSQ 552
Cdd:cd14587  285 ------------------------HQENVEDQNEQCPVFLQWLDCVHQ 308
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 263-552 5.19e-61

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: 206.10  E-value: 5.19e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 263 RLPVITWCQPGSGAVIARSSQPLVGLMmNMRSNLDEKLVAAFCSQLPGAkGERRKLYIADARPRKNALANGAMGGGSESS 342
Cdd:cd14533    3 RIPSVVWRHQRNGAVIARCSQPEVGWL-GWRNAEDENLLQAIAEACASN-ASPKKLLIVDARSYAAAVANRAKGGGCECP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 343 SNYFQSEIVFFGIDNIHAMRESFSRVRdyldMHGTTSSDGRSSFlrhggwtwgggnlssmsasvSLLGDSGWLIHIQSVL 422
Cdd:cd14533   81 EYYPNCEVVFMNLANIHAIRKSFHSLR----ALCSSAPDQPNWL--------------------SNLESTKWLHHLSGLL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 423 AGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGmpNISGSGNfd 502
Cdd:cd14533  137 KAALLVVNAVDEEGRPVLVHCSDGWDRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFGHKFADRCG--HGVNSED-- 212

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 240255320 503 fprqsssagsfpsspvrqssgsaasqssssshgHNNYSPIFMQWIDSVSQ 552
Cdd:cd14533  213 ---------------------------------INERCPVFLQWLDCVHQ 229
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 263-575 3.26e-60

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: 204.83  E-value: 3.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 263 RLPVITWCQPGSGAVIARSSQPLVGlMMNMRSNLDEKlvaaFCSQLPGAKGERRKLYIADARPRKNALANGAMGGGSESS 342
Cdd:cd14592    2 RVPVLSWIHPESQATITRCSQPLVG-PNDKRCKEDEK----YLQTIMDANAQSHKLIIFDARQNSVADTNKTKGGGYESE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 343 SNYFQSEIVFFGIDNIHAMRESFSRVRDYLdmhgttssdgrSSFLRHGGWtwgggnLSSMSASvsllgdsGWLIHIQSVL 422
Cdd:cd14592   77 SAYPNAELVFLEIHNIHVMRESLRKLKEIV-----------YPSIDEARW------LSNVDGT-------HWLEYIRMLL 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 423 AGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGmpniSGSGNFd 502
Cdd:cd14592  133 AGAVRIADKIESGKTSVVVHCSDGWDRTAQLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVG----HGDDNH- 207

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240255320 503 fprqsssagsfpsspvrqssgsaasqssssshGHNNYSPIFMQWIDSVSQLMRMYPCAFEFSPTFLVDFMDCL 575
Cdd:cd14592  208 --------------------------------ADADRSPIFLQFIDCVWQMTRQFPSAFEFNELFLITILDHL 248
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 219-552 9.14e-58

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: 200.25  E-value: 9.14e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 219 NELWRISDLNSNYNLCQTYPFAFMIPKSISDAELLQACSFRARCRLPVITWCQPGSGAVIARSSQPLVGlMMNMRSNLDE 298
Cdd:cd14586    5 QNAWRISNINEKYKLCGSYPQELIVPAWITDKELESVASFRSWKRIPAVVYRHQSNGAVIARCGQPEVS-WWGWRNADDE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 299 KLVAA-----------------------------------FCSQLPGAKG------ERRKLYIADARPRKNALANGAMGG 337
Cdd:cd14586   84 HLVQSvakacasdssscksvlmtgncsrdfpnggdlsdveFDSSMSNASGveslaiQPQKLLILDARSYAAAVANRAKGG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 338 GSESSSNYFQSEIVFFGIDNIHAMRESFSRVRdyldMHGTTSSDGrssflrhGGWtwgggnlssmsasVSLLGDSGWLIH 417
Cdd:cd14586  164 GCECPEYYPNCEVVFMGMANIHSIRKSFQSLR----LLCTQMPDP-------ANW-------------LSALESTKWLQH 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 418 IQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGmpniSG 497
Cdd:cd14586  220 LSMLLKSALLVVHAVDRDQRPVLVHCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRCG----HG 295

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 240255320 498 SGNFDFprqsssagsfpsspvrqssgsaasqssssshghNNYSPIFMQWIDSVSQ 552
Cdd:cd14586  296 ENSDDL---------------------------------NERCPVFLQWLDCVHQ 317
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 222-555 5.90e-46

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: 166.00  E-value: 5.90e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 222 WRISDLNSNYNLCQTYPFAFMIPKSISDAELLQAcsfrARC----RLPVITWCQPGSGAVIARSSQPLVGLMMNMRSNLD 297
Cdd:cd14534    1 FRISTANRDYSICRSYPALVVVPQSVSDESLRKV----ARCyrqgRFPVVTWRHPRTKALLLRSGGFHGKGVMGMLKSAN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 298 EKLVAAFCSQLPGAKGERRKLYIAdarprknALANGAMGGGSE----SSSNYFQSEIVFFGIDNIHAMRESFSRVRDYLd 373
Cdd:cd14534   77 TSTSSPTVSSSETSSSLEQEKYLS-------ALVLYVLGEKSQmkgvKAESDPKCEFIPVEYPEVRQVKASFKKLLRAC- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 374 MHGTTSSDGRSSFLRhggwtwgggnlssmsasvsLLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQL 453
Cdd:cd14534  149 VPSSAPTEPEQSFLK-------------------AVEDSEWLQQLQCLMQLSGAVVDLLDVQGSSVLLCLEDGWDVTTQV 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 454 VSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGMPNISGSGNFdfprqsssagsfpsspvrqssgsaasqsssss 533
Cdd:cd14534  210 SSLSQLLLDPYYRTLEGFRVLVEKEWLAFGHRFSHRSNLTAASQSSGF-------------------------------- 257

                        330       340
                 ....*....|....*....|..
gi 240255320 534 hghnnySPIFMQWIDSVSQLMR 555
Cdd:cd14534  258 ------APVFLQFLDAVHQIHR 273
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 263-489 2.87e-41

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: 150.95  E-value: 2.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 263 RLPVITWCQPGSGAVIARSSQPLVGlMMNMRSNLDEKLVAAFCSqlPGAKGerrklYIADARPRKNALANGAMGGGSESS 342
Cdd:cd14536    2 RFPVLSYYHKKNGMVLMRSSQPLTG-PNGKRCKEDEKLLNAVLG--GGKRG-----YIIDTRSKNVAQQARAKGGGFEPE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 343 SNYFQSEIVFFGIDNIHAMRESFSR-VRDYLDmhgttssdgrssflrhggwtwgggNLSSMSASVSLLGDSGWLIHIQSV 421
Cdd:cd14536   74 AHYPQWRRIHKPIERYNVLQESLIKlVEACND------------------------QGHSMDKWLSKLESSNWLSHVKEI 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240255320 422 LAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDR 489
Cdd:cd14536  130 LTTACLVAQCIDREGASVLVHGSEGMDSTLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSR 197
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 222-553 4.42e-34

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: 132.74  E-value: 4.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 222 WRISDLNSNYNLCQTYPFAFMIPKSISDAELLQAcsfrARC----RLPVITWCQPGSGAVIARS----SQPLVGLMMNMR 293
Cdd:cd14589    1 FRITAVNRMYSLCRSYPGLLVVPQSVQDSSLQKV----ARCyrhnRLPVVCWKNSKTKAVLLRSggfhGKGVVGLFKSQN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 294 SNL-------------DEKLVAAFCSQLPGAKGERRKLYIADARPRKNALANGAMGGGSESSSNYFQ----SEIVFFGID 356
Cdd:cd14589   77 PHSaapassessssieQEKYLQALLNAISVHQKMNGNSTLLQSQLLKRQAALYIFGEKSQLRGFKLDfalnCEFVPVEFH 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 357 NIHAMRESFSRVRDYLdMHGTTSSDGRSSFLRhggwtwgggnlssmsasvsLLGDSGWLIHIQSVLAGAAwIAARVAMES 436
Cdd:cd14589  157 DIRQVKASFKKLMRAC-VPSTIPTDSEVTFLK-------------------ALGESEWFLQLHRIMQLAV-VISELLESG 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 437 ASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGM-PNISGSGnfdfprqsssagsfps 515
Cdd:cd14589  216 SSVMVCLEDGWDITTQVVSLVQLLSDPFYRTLEGFQMLVEKEWLSFGHKFSQRSNLtPNSQGSG---------------- 279

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 240255320 516 spvrqssgsaasqssssshghnnYSPIFMQWIDSVSQL 553
Cdd:cd14589  280 -----------------------FAPIFLQFLDCVHQI 294
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 222-501 6.04e-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: 126.24  E-value: 6.04e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 222 WRISDLNSNYNLCQTYPFAFMIPKSISDAELLQACSFRARCRLPVITWCQPGSGAVIARS----SQPLVGLMMNM----- 292
Cdd:cd14588    1 FRISTVNRMYAVCRSYPGLLIVPQSIQDNTIQRISRCYRQNRFPVVCWRNSRTKAVLLRSgglhGKGVVGLFKSQnapaa 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 293 -RSNLD------EKLVAAFCSQLP---------GAKGERRKLYIADARPRknalangaMGGGSESSSNyfQSEIVFFGID 356
Cdd:cd14588   81 gQSQTDstsleqEKYLQAVINSMPryadasgrnTLSGFRAALYIIGDKSQ--------LKGVKQDPLQ--QWEVVPIEVF 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 357 NIHAMRESFSRVRDYLdMHGTTSSDGRSSFLRHggwtwgggnlssmsasvslLGDSGWLIHIQSVLAGAAWIAARVAMES 436
Cdd:cd14588  151 DVRQVKASFKKLMKAC-VPSCPSTDPSQTYLRT-------------------LEESEWLSQLHKLLQVSVLVVELLDSGS 210

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240255320 437 aSVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGMPNISGSGNF 501
Cdd:cd14588  211 -SVLVSLEDGWDITTQVVSLVQLLSDPYYRTIEGFRLLVEKEWLSFGHRFSHRGAQTLASQSSGF 274
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 403-491 7.52e-19

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: 85.47  E-value: 7.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 403 SASVSLLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAF 482
Cdd:cd14537   88 SKWYSLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQESDGRDLSCVVSSLVQLLLDPHFRTITGFQSLIQKEWVAL 167


                 ....*....
gi 240255320 483 GHPFSDRVG 491
Cdd:cd14537  168 GHPFCDRLG 176
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 405-491 2.12e-13

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: 69.47  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 405 SVSLLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGH 484
Cdd:cd14595   86 WLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEWVVAGH 165


                 ....*..
gi 240255320 485 PFSDRVG 491
Cdd:cd14595  166 PFLQRLN 172
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 407-489 3.63e-12

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: 66.40  E-value: 3.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 407 SLLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPF 486
Cdd:cd14594   96 SSLESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQSLIQKEWVMGGHCF 175


                 ...
gi 240255320 487 SDR 489
Cdd:cd14594  176 LDR 178
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 407-489 2.55e-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: 63.76  E-value: 2.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320 407 SLLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPF 486
Cdd:cd14593   89 SSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLVQVMLDPYFRTITGFQSLIQKEWVMAGYRF 168


                 ...
gi 240255320 487 SDR 489
Cdd:cd14593  169 LDR 171
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
52-111 1.76e-08

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 51.44  E-value: 1.76e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240255320    52 CLLESERVIVEgYGVVLINT-DEAGTLLVTNFRILFLSEGTRKVIpLGTIPLATIEKFNKM 111
Cdd:smart00568   1 KLPEEEKLIAD-YSCYLSRTgPVQGRLYISNYRLCFRSNLPGKLT-KVVIPLADITRIEKS 59
PH-GRAM_MTM-like cd13223
Myotubularian 1 and related proteins Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase; ...
 75-161 7.76e-07

Myotubularian 1 and related proteins Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase; MTM1, MTMR1, and MTMR2 are members of the myotubularin protein phosphatase gene family. They contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. In addition MTMR1 (Myotubularian related 1 protein) and MTMR2 (Myotubularian related 2 protein) contain a C-terminal PDZ domain. Mutations in MTMR2 are a cause of Charcot-Marie-Tooth disease type 4B, an autosomal recessive demyelinating neuropathy. The protein can self-associate and form heteromers with MTMR5 and MTMR12. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date.


Pssm-ID: 275407  Cd Length: 100  Bit Score: 48.00  E-value: 7.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  75 GTLLVTNFRILFLSE--GTRKV--IPLGTIplATIEKfnkmvlkVQSSPRQSDKIpprRLLQVTGKDMRIIVYGFRPRTK 150
Cdd:cd13223   18 GTLYITNYRLYFKSRdrEPNFVldVPLGVI--SRVEK-------VGGATSRGENS---YGLEIHCKDMRNLRFAHKQENH 85

                         90
                 ....*....|.
gi 240255320 151 QRRNVFDALLK 161
Cdd:cd13223   86 SRRKLYETLQK 96
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
434-467 1.06e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 45.04  E-value: 1.06e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 240255320   434 MESASVLVHCSDGWDRTTQLVSLACLLLDPYYRT 467
Cdd:smart00404  37 ESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA 70
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 434-467 1.06e-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: 45.04  E-value: 1.06e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 240255320   434 MESASVLVHCSDGWDRTTQLVSLACLLLDPYYRT 467
Cdd:smart00012  37 ESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA 70
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 75-159 1.99e-04

Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275393  Cd Length: 94  Bit Score: 41.21  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  75 GTLLVTNFRILFLSEGTRKVIPLGtIPLATIEKFNKMVLKVQSSPRqsdkipprrlLQVTGKDMRIIVYGFRPRTKQRRN 154
Cdd:cd10570   21 GTLYLSTYRLIFSSKADGDETKLV-IPLVDITDVEKIAGASFLPSG----------LIITCKDFRTIKFSFDSEDEAVKV 89


                 ....*
gi 240255320 155 VFDAL 159
Cdd:cd10570   90 IARVL 94
PH-GRAM_MTM1 cd13355
Myotubularian 1 protein (MTM1) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 75-165 3.56e-04

Myotubularian 1 protein (MTM1) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTM1 is a member of the myotubularin protein phosphatase gene family. It is required for muscle cell differentiation and mutations in this gene have been identified as being responsible for X-linked myotubular myopathy, a severe congenital muscle disorder characterized by defective muscle cell development. Since its initial discovery, there have been an additional 14 myotubularin-related proteins identified. MTM1 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The protein can self-associate and form heteromers with MTMR12. MTM1 contains a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. All MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE and PH domains C-terminal to the coiled-coil region.


Pssm-ID: 270162  Cd Length: 100  Bit Score: 40.61  E-value: 3.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255320  75 GTLLVTNFRILFLSEGTRKVIPLgTIPLATIEKFNKMVlkvQSSPRQSDKIPprrlLQVTGKDMRIIVYGFRPRTKQRRN 154
Cdd:cd13355   18 GRVYITNYRLYFKSTESEPPVTL-DVPLGVISRIEKMG---GASSRGENSYG----LDITCKDMRNLRFALKQEGHSRRD 89

                         90
                 ....*....|.
gi 240255320 155 VFDALLKCTKP 165
Cdd:cd13355   90 IFEILTKYAFP 100
 
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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