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Conserved domains on  [gi|1985373282|ref|XP_039395147|]
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myotubularin-related protein 7 isoform X2 [Mauremys reevesii]

Protein Classification

PH-like and PTP-MTMR7 domain-containing protein( domain architecture ID 13117768)

PH-like and PTP-MTMR7 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 132-433 0e+00

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: 673.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 132 LNEEYNRMGVPNNYWQISDVNRDYQVCDSYPTEVYVPKSATAHIIVGSSKFRSRRRFPALSYYCKDNNASICRSSQPLSG 211
Cdd:cd14583     1 LKAEYNRMGLPNSLWQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYYCKDNNASICRSSQPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 212 FSARCLEDEQMLQAIRKANPGSNFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRSSLQKMLEVCE 291
Cdd:cd14583    81 FSARCLEDEQMLQAIRKANPGSDFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 292 LKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWDRTAQVCSVASLLLDPFYRTIKGFMVLIE 371
Cdd:cd14583   161 LRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985373282 372 KDWVSFGHKFNHRYGYLDGDPKEISPVIDQFIECIWQLMEQFPCAFEFNERFLIHIQHHIYS 433
Cdd:cd14583   241 KDWVSFGHKFNHRYGHLDGDPKEVSPVIDQFIECVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 8-103 9.29e-64

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13344:

Pssm-ID: 473070  Cd Length: 103  Bit Score: 205.93  E-value: 9.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282   8 KVENVRLIDRISSRKAALGTLYLTATHVIFVDNVSETRKETWILHSQISSIEKQATTVTGCPLLIRCKNFQIIQLIIPQE 87
Cdd:cd13344     8 KVENVRLVDRISSKKAALGTLYLTATHVIFVENSSDTRKETWILHSQISSIEKQATTATGCPLLIRCKNFQVIQLIIPQE 87

                          90
                  ....*....|....*.
gi 1985373282  88 RDCHDVYISLIRLARP 103
Cdd:cd13344    88 RDCHDVYISLIRLARP 103
 
Name Accession Description Interval E-value
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 132-433 0e+00

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: 673.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 132 LNEEYNRMGVPNNYWQISDVNRDYQVCDSYPTEVYVPKSATAHIIVGSSKFRSRRRFPALSYYCKDNNASICRSSQPLSG 211
Cdd:cd14583     1 LKAEYNRMGLPNSLWQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYYCKDNNASICRSSQPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 212 FSARCLEDEQMLQAIRKANPGSNFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRSSLQKMLEVCE 291
Cdd:cd14583    81 FSARCLEDEQMLQAIRKANPGSDFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 292 LKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWDRTAQVCSVASLLLDPFYRTIKGFMVLIE 371
Cdd:cd14583   161 LRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985373282 372 KDWVSFGHKFNHRYGYLDGDPKEISPVIDQFIECIWQLMEQFPCAFEFNERFLIHIQHHIYS 433
Cdd:cd14583   241 KDWVSFGHKFNHRYGHLDGDPKEVSPVIDQFIECVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 124-448 0e+00

Myotubularin-like phosphatase domain; This family represents the phosphatase domain within eukaryotic myotubularin-related proteins. Myotubularin is a dual-specific lipid phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bi-phosphate. Mutations in gene encoding myotubularin-related proteins have been associated with disease.


Pssm-ID: 461958 [Multi-domain]  Cd Length: 332  Bit Score: 615.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 124 EQGWKLVGLNEEYNRMGVPNN-YWQISDVNRDYQVCDSYPTEVYVPKSATAHIIVGSSKFRSRRRFPALSYYCKDNNASI 202
Cdd:pfam06602   2 ENGWDLYDPEAEFARQGLPSKdEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 203 CRSSQPLSGF-SARCLEDEQMLQAIRKAN--PGSNFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVM 279
Cdd:pfam06602  82 TRSSQPLVGLnGKRSIEDEKLLQAIFKSSnpYSAKKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVM 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 280 RSSLQKMLEVCELKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWDRTAQVCSVASLLLDPF 359
Cdd:pfam06602 162 RDSLNKLVEACNDRSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 360 YRTIKGFMVLIEKDWVSFGHKFNHRYGYLDG--DPKEISPVIDQFIECIWQLMEQFPCAFEFNERFLIHIQHHIYSCQFG 437
Cdd:pfam06602 242 YRTIEGFQVLIEKEWLSFGHKFADRCGHLAGftDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFG 321

                         330
                  ....*....|.
gi 1985373282 438 NFLCNSQKERR 448
Cdd:pfam06602 322 TFLCNSEKERV 332
PH-GRAM_MTMR7 cd13344
Myotubularian (MTM) related 7 protein (MTMR7) Pleckstrin Homology-Glucosyltransferases, ...
 8-103 9.29e-64

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: 205.93  E-value: 9.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282   8 KVENVRLIDRISSRKAALGTLYLTATHVIFVDNVSETRKETWILHSQISSIEKQATTVTGCPLLIRCKNFQIIQLIIPQE 87
Cdd:cd13344     8 KVENVRLVDRISSKKAALGTLYLTATHVIFVENSSDTRKETWILHSQISSIEKQATTATGCPLLIRCKNFQVIQLIIPQE 87

                          90
                  ....*....|....*.
gi 1985373282  88 RDCHDVYISLIRLARP 103
Cdd:cd13344    88 RDCHDVYISLIRLARP 103
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
333-432 1.67e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 44.27  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282  333 SVLVHCSDGWDRTAQVCSVASLLLDPFYRTIKgfmvliekdwvsfghkfnhrygyldgdpkeispvIDQFiECIWQLMEQ 412
Cdd:smart00404  41 PVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE----------------------------------VDIF-DTVKELRSQ 85

                           90       100
                   ....*....|....*....|
gi 1985373282  413 FPCAFEFNERFLIHIQHHIY 432
Cdd:smart00404  86 RPGMVQTEEQYLFLYRALLE 105
 
Name Accession Description Interval E-value
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 132-433 0e+00

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: 673.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 132 LNEEYNRMGVPNNYWQISDVNRDYQVCDSYPTEVYVPKSATAHIIVGSSKFRSRRRFPALSYYCKDNNASICRSSQPLSG 211
Cdd:cd14583     1 LKAEYNRMGLPNSLWQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYYCKDNNASICRSSQPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 212 FSARCLEDEQMLQAIRKANPGSNFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRSSLQKMLEVCE 291
Cdd:cd14583    81 FSARCLEDEQMLQAIRKANPGSDFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 292 LKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWDRTAQVCSVASLLLDPFYRTIKGFMVLIE 371
Cdd:cd14583   161 LRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985373282 372 KDWVSFGHKFNHRYGYLDGDPKEISPVIDQFIECIWQLMEQFPCAFEFNERFLIHIQHHIYS 433
Cdd:cd14583   241 KDWVSFGHKFNHRYGHLDGDPKEVSPVIDQFIECVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 132-433 0e+00

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: 644.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 132 LNEEYNRMGVPNNYWQISDVNRDYQVCDSYPTEVYVPKSATAHIIVGSSKFRSRRRFPALSYYCKDNNASICRSSQPLSG 211
Cdd:cd14532     1 LESEYTRMGVPNDNWTLSDINKDYELCDTYPRELFVPTSASTPVLVGSSKFRSKGRLPVLSYLHKDNQAAICRCSQPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 212 FSARCLEDEQMLQAIRKANPGSNFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRSSLQKMLEVCE 291
Cdd:cd14532    81 FSARCVEDEQLLQAIRKANPNSKFMYVVDTRPKINAMANKAAGKGYENEDNYSNIKFQFFGIENIHVMRSSLQKLLEVCE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 292 LKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVaEEGMSVLVHCSDGWDRTAQVCSVASLLLDPFYRTIKGFMVLIE 371
Cdd:cd14532   161 LKNPSMSAFLSGLESSGWLKHIKAVMDTSVFIAKAV-SEGASVLVHCSDGWDRTAQTCSLASLLLDPYYRTIKGFQVLIE 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985373282 372 KDWVSFGHKFNHRYGYLDGDPKEISPVIDQFIECIWQLMEQFPCAFEFNERFLIHIQHHIYS 433
Cdd:cd14532   240 KEWLSFGHKFTDRCGHLQGDAKEVSPVFTQFLDCVWQLMQQFPRAFEFNERFLLTLHDHVYS 301
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
 124-448 0e+00

Myotubularin-like phosphatase domain; This family represents the phosphatase domain within eukaryotic myotubularin-related proteins. Myotubularin is a dual-specific lipid phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bi-phosphate. Mutations in gene encoding myotubularin-related proteins have been associated with disease.


Pssm-ID: 461958 [Multi-domain]  Cd Length: 332  Bit Score: 615.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 124 EQGWKLVGLNEEYNRMGVPNN-YWQISDVNRDYQVCDSYPTEVYVPKSATAHIIVGSSKFRSRRRFPALSYYCKDNNASI 202
Cdd:pfam06602   2 ENGWDLYDPEAEFARQGLPSKdEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 203 CRSSQPLSGF-SARCLEDEQMLQAIRKAN--PGSNFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVM 279
Cdd:pfam06602  82 TRSSQPLVGLnGKRSIEDEKLLQAIFKSSnpYSAKKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVM 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 280 RSSLQKMLEVCELKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWDRTAQVCSVASLLLDPF 359
Cdd:pfam06602 162 RDSLNKLVEACNDRSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 360 YRTIKGFMVLIEKDWVSFGHKFNHRYGYLDG--DPKEISPVIDQFIECIWQLMEQFPCAFEFNERFLIHIQHHIYSCQFG 437
Cdd:pfam06602 242 YRTIEGFQVLIEKEWLSFGHKFADRCGHLAGftDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLYHLYSCQFG 321

                         330
                  ....*....|.
gi 1985373282 438 NFLCNSQKERR 448
Cdd:pfam06602 322 TFLCNSEKERV 332
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 126-433 0e+00

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: 606.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 126 GWKLVGLNEEYNRMGVPNNYWQISDVNRDYQVCDSYPTEVYVPKSATAHIIVGSSKFRSRRRFPALSYYCKDNNASICRS 205
Cdd:cd14584     1 GWKLIDLKVDFQRMGIPNDYWEITDANKNYEICSTYPPELVVPKSASKATVVGSSKFRSRGRFPVLSYLYKENNAAICRC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 206 SQPLSGFSARCLEDEQMLQAIRKANPGSNFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRSSLQK 285
Cdd:cd14584    81 SQPLSGFSARCVEDEQMLQAISKANPGSPFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIRFQFIGIENIHVMRSSLQK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 286 MLEVCELKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWDRTAQVCSVASLLLDPFYRTIKG 365
Cdd:cd14584   161 LLEVCEMKSPSMSDFLTGLENSGWLRHIKAVMDAGVFLAKAVKEEKASVLVHCSDGWDRTAQVCSLASLLLDPFYRTIKG 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985373282 366 FMVLIEKDWVSFGHKFNHRYGYLDGDPKEISPVIDQFIECIWQLMEQFPCAFEFNERFLIHIQHHIYS 433
Cdd:cd14584   241 LMVLIEKEWISMGHKFSQRCGHLDGDPKEVSPVFTQFLECVWQLMEQFPCAFEFNEHFLLEIHDHVFS 308
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 132-433 0e+00

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: 564.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 132 LNEEYNRMGVPNNYWQISDVNRDYQVCDSYPTEVYVPKSATAHIIVGSSKFRSRRRFPALSYYCKDNNASICRSSQPLSG 211
Cdd:cd14585     1 LAEEYKRMGVPNDYWQLSDVNRDYKICDTYPRDLYVPITASKPIIVGSSKFRSKGRFPVLSYYHQEKKAAICRCSQPLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 212 FSARCLEDEQMLQAIRKANPGSNFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRSSLQKMLEVCE 291
Cdd:cd14585    81 FSARCLEDEHMLQAISKANPNNRYMYVMDTRPKLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVCG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 292 LKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWDRTAQVCSVASLLLDPFYRTIKGFMVLIE 371
Cdd:cd14585   161 TKALSVNDFLSGLESSGWLRHIKAVLDAAVFLAKAVAVEGASVLVHCSDGWDRTAQVCSLGSLLLDPYYRTIKGFMVLIE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985373282 372 KDWVSFGHKFNHRYGYLDGDPKEISPVIDQFIECIWQLMEQFPCAFEFNERFLIHIQHHIYS 433
Cdd:cd14585   241 KDWISFGHKFSDRCGQLDGDPKEISPVFTQFLECVWQLTEQFPRAFEFSEAFLLQIHEHIHS 302
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
 186-408 1.31e-122

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: 363.02  E-value: 1.31e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 186 RRFPALSYYCKDNNASICRSSQPLSGF-SARCLEDEQMLQAIRKANPGSNFIYVVDTRPKLNAMANRAAGKGYENEDNYS 264
Cdd:cd14507     1 GRIPVLSWRHPRNGAVICRSSQPLVGLtGSRSKEDEKLLNAIRKASPSSKKLYIVDARPKLNAVANRAKGGGYENTEYYP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 265 NIKFQFIGIENIHVMRSSLQKMLEVCELKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWDR 344
Cdd:cd14507    81 NCELEFLNIENIHAMRDSLNKLRDACLSPNDEESNWLSALESSGWLEHIRLILKGAVRVADLLEKEGTSVLVHCSDGWDR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985373282 345 TAQVCSVASLLLDPFYRTIKGFMVLIEKDWVSFGHKFNHRYGYLD--GDPKEISPVIDQFIECIWQ 408
Cdd:cd14507   161 TSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDknSSDEERSPIFLQFLDCVWQ 226
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
 187-432 2.70e-101

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: 309.38  E-value: 2.70e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 187 RFPALSYYCKDNNASICRSSQPLSGFSA-RCLEDEQMLQAIRKANPGSNFIYVVDTRPKLNAMANRAAGKGYENEDNYSN 265
Cdd:cd14535     2 RIPVLSWIHPESQATITRCSQPLVGVSGkRSKDDEKYLQLIMDANAQSHKLFIMDARPSVNAVANKAKGGGYESEDAYQN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 266 IKFQFIGIENIHVMRSSLQKMLEVCelkSPSMSDFLW--GLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWD 343
Cdd:cd14535    82 AELVFLDIHNIHVMRESLRKLKDIC---FPNIDDSHWlsNLESTHWLEHIKLILAGAVRIADKVESGKTSVVVHCSDGWD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 344 RTAQVCSVASLLLDPFYRTIKGFMVLIEKDWVSFGHKFNHRYGYldGDPK----EISPVIDQFIECIWQLMEQFPCAFEF 419
Cdd:cd14535   159 RTAQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGH--GDKNhsdaDRSPVFLQFIDCVWQMTRQFPNAFEF 236

                         250
                  ....*....|...
gi 1985373282 420 NERFLIHIQHHIY 432
Cdd:cd14535   237 NEHFLITILDHLY 249
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 180-432 7.81e-93

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: 288.09  E-value: 7.81e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 180 SKFRSRRRFPALSYYCKDNNASICRSSQPLSGFSA-RCLEDEQMLQAIRKANPGSNFIYVVDTRPKLNAMANRAAGKGYE 258
Cdd:cd14590     8 ASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGkRSKEDEKYLQAIMDSNAQSHKIFIFDARPSVNAVANKAKGGGYE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 259 NEDNYSNIKFQFIGIENIHVMRSSLQKMLEVCelkSPSMSDFLW--GLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLV 336
Cdd:cd14590    88 SEDAYQNAELVFLDIHNIHVMRESLRKLKEIV---YPNIEESHWlsNLESTHWLEHIKLILAGALRIADKVESGKTSVVV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 337 HCSDGWDRTAQVCSVASLLLDPFYRTIKGFMVLIEKDWVSFGHKFNHRYGYLDGDPKEI--SPVIDQFIECIWQLMEQFP 414
Cdd:cd14590   165 HCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADAdrSPVFLQFIDCVWQMTRQFP 244

                         250
                  ....*....|....*...
gi 1985373282 415 CAFEFNERFLIHIQHHIY 432
Cdd:cd14590   245 TAFEFNEYFLITILDHLY 262
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
 187-432 7.96e-88

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: 274.60  E-value: 7.96e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 187 RFPALSYYCKDNNASICRSSQPLSGFSA-RCLEDEQMLQAIRKANPGSNFIYVVDTRPKLNAMANRAAGKGYENEDNYSN 265
Cdd:cd14591     2 RIPVLSWIHPENQAVIMRCSQPLVGMSGkRNKDDEKYLDIIREANGQTSKLTIYDARPSVNAVANKATGGGYEGDDAYQN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 266 IKFQFIGIENIHVMRSSLQKMLEVCelkSPSMSDFLW--GLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWD 343
Cdd:cd14591    82 AELVFLDIHNIHVMRESLKKLKDIV---YPNVEESHWlsSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 344 RTAQVCSVASLLLDPFYRTIKGFMVLIEKDWVSFGHKFNHRYGYLDGDPKEI--SPVIDQFIECIWQLMEQFPCAFEFNE 421
Cdd:cd14591   159 RTAQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGHGDKNHADAdrSPIFLQFIDCVWQMSKQFPTAFEFNE 238

                         250
                  ....*....|.
gi 1985373282 422 RFLIHIQHHIY 432
Cdd:cd14591   239 QFLITILDHLY 249
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
 187-408 1.99e-83

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: 262.38  E-value: 1.99e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 187 RFPALSYYCKDNNASICRSSQPLSGF-SARCLEDEQMLQAI------RKANPGSNFIyVVDTRPKLNAMANRAAGKGYEN 259
Cdd:cd17666     2 RIPVLTYLHKANGCSITRSSQPLVGLkQNRSIQDEKLVSEIfntsinEIYISPQKNL-IVDARPTTNAMAQVALGAGTEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 260 EDNYSN--IKFQFIGIENIHVMRSSLQKMLEV------CELKSPSMSDflwGLENSGWLKHIKAIMDAGIFIAKAVAEEG 331
Cdd:cd17666    81 MDNYKYktAKKIYLGIDNIHVMRDSLNKVTEAlkdgddSNPSYPPLIN---ALKKSNWLKYLAIILQGADLIAKSIHFNH 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985373282 332 MSVLVHCSDGWDRTAQVCSVASLLLDPFYRTIKGFMVLIEKDWVSFGHKFNHRYGYldgdpKEISPVIDQFIECIWQ 408
Cdd:cd17666   158 SHVLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFAERSGH-----KETSPVFHQFLDCVYQ 229
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 186-432 1.23e-79

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: 252.98  E-value: 1.23e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 186 RRFPALSYYCKDNNASICRSSQPLSGFS-ARCLEDEQMLQAIRKANPGSNFIYVVDTRPKLNAMANRAAGKGYENEDNYS 264
Cdd:cd14592     1 GRVPVLSWIHPESQATITRCSQPLVGPNdKRCKEDEKYLQTIMDANAQSHKLIIFDARQNSVADTNKTKGGGYESESAYP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 265 NIKFQFIGIENIHVMRSSLQKMLEVCelkSPSMSDFLW--GLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGW 342
Cdd:cd14592    81 NAELVFLEIHNIHVMRESLRKLKEIV---YPSIDEARWlsNVDGTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGW 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 343 DRTAQVCSVASLLLDPFYRTIKGFMVLIEKDWVSFGHKFNHRYGYLDGD--PKEISPVIDQFIECIWQLMEQFPCAFEFN 420
Cdd:cd14592   158 DRTAQLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGHGDDNhaDADRSPIFLQFIDCVWQMTRQFPSAFEFN 237

                         250
                  ....*....|..
gi 1985373282 421 ERFLIHIQHHIY 432
Cdd:cd14592   238 ELFLITILDHLY 249
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 144-408 1.12e-70

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: 231.85  E-value: 1.12e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 144 NYWQISDVNRDYQVCDSYPTEVYVPKSATAHIIVGSSKFRSRRRFPALSYYCKDNNASICRSSQP-LSGFSARCLEDEQM 222
Cdd:cd14587     1 NVWRVSEINSNYKLCSSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAVIARCSQPeISWWGWRNADDEYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 223 LQAIRKA---NPGSNF--------------------------------------IYVVDTRPKLNAMANRAAGKGYENED 261
Cdd:cd14587    81 VTSIAKAcalDPGTRApggspskgnsdgsdasdtdfdssltacsavesgaapqkLLILDARSYTAAVANRAKGGGCECEE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 262 NYSNIKFQFIGIENIHVMRSSLQKMLEVCElKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDG 341
Cdd:cd14587   161 YYPNCEVMFMGMANIHSIRNSFQYLRAVCS-QMPDPGNWLSALESTKWLQHLSVMLKAAVLVASAVDREGRPVLVHCSDG 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985373282 342 WDRTAQVCSVASLLLDPFYRTIKGFMVLIEKDWVSFGHKFNHRYGYLDG--DPKEISPVIDQFIECIWQ 408
Cdd:cd14587   240 WDRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHQENveDQNEQCPVFLQWLDCVHQ 308
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
 186-408 4.78e-65

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: 213.80  E-value: 4.78e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 186 RRFPALSYYCKDNNASICRSSQPLSGF-SARCLEDEQMLQAIRKANPGSN---FIYVVDTRPKLNAMANRAAGKGYENED 261
Cdd:cd14533     2 KRIPSVVWRHQRNGAVIARCSQPEVGWlGWRNAEDENLLQAIAEACASNAspkKLLIVDARSYAAAVANRAKGGGCECPE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 262 NYSNIKFQFIGIENIHVMRSSLQKMLEVCElKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDG 341
Cdd:cd14533    82 YYPNCEVVFMNLANIHAIRKSFHSLRALCS-SAPDQPNWLSNLESTKWLHHLSGLLKAALLVVNAVDEEGRPVLVHCSDG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985373282 342 WDRTAQVCSVASLLLDPFYRTIKGFMVLIEKDWVSFGHKFNHRYGYLDG--DPKEISPVIDQFIECIWQ 408
Cdd:cd14533   161 WDRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFGHKFADRCGHGVNseDINERCPVFLQWLDCVHQ 229
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 187-408 7.67e-64

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: 210.66  E-value: 7.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 187 RFPALSYYCKDNNASICRSSQPLSGFSA-RCLEDEQMLQA-IRKANPGsnfiYVVDTRPKLNAMANRAAGKGYENEDNYS 264
Cdd:cd14536     2 RFPVLSYYHKKNGMVLMRSSQPLTGPNGkRCKEDEKLLNAvLGGGKRG----YIIDTRSKNVAQQARAKGGGFEPEAHYP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 265 NIKFQFIGIENIHVMRSSLQKMLEVCELKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWDR 344
Cdd:cd14536    78 QWRRIHKPIERYNVLQESLIKLVEACNDQGHSMDKWLSKLESSNWLSHVKEILTTACLVAQCIDREGASVLVHGSEGMDS 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985373282 345 TAQVCSVASLLLDPFYRTIKGFMVLIEKDWVSFGHKFNHRY---GYLDGDPKEISPVIDQFIECIWQ 408
Cdd:cd14536   158 TLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRCaksAYSNSKQKFESPVFLLFLDCVWQ 224
PH-GRAM_MTMR7 cd13344
Myotubularian (MTM) related 7 protein (MTMR7) Pleckstrin Homology-Glucosyltransferases, ...
 8-103 9.29e-64

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: 205.93  E-value: 9.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282   8 KVENVRLIDRISSRKAALGTLYLTATHVIFVDNVSETRKETWILHSQISSIEKQATTVTGCPLLIRCKNFQIIQLIIPQE 87
Cdd:cd13344     8 KVENVRLVDRISSKKAALGTLYLTATHVIFVENSSDTRKETWILHSQISSIEKQATTATGCPLLIRCKNFQVIQLIIPQE 87

                          90
                  ....*....|....*.
gi 1985373282  88 RDCHDVYISLIRLARP 103
Cdd:cd13344    88 RDCHDVYISLIRLARP 103
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
 143-408 5.59e-63

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: 211.80  E-value: 5.59e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 143 NNYWQISDVNRDYQVCDSYPTEVYVPKSATAHIIVGSSKFRSRRRFPALSYYCKDNNASICRSSQP-LSGFSARCLEDEQ 221
Cdd:cd14586     5 QNAWRISNINEKYKLCGSYPQELIVPAWITDKELESVASFRSWKRIPAVVYRHQSNGAVIARCGQPeVSWWGWRNADDEH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 222 MLQAIRKA--------NPGSNF-------------------------------------IYVVDTRPKLNAMANRAAGKG 256
Cdd:cd14586    85 LVQSVAKAcasdssscKSVLMTgncsrdfpnggdlsdvefdssmsnasgveslaiqpqkLLILDARSYAAAVANRAKGGG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 257 YENEDNYSNIKFQFIGIENIHVMRSSLQKMLEVCElKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLV 336
Cdd:cd14586   165 CECPEYYPNCEVVFMGMANIHSIRKSFQSLRLLCT-QMPDPANWLSALESTKWLQHLSMLLKSALLVVHAVDRDQRPVLV 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985373282 337 HCSDGWDRTAQVCSVASLLLDPFYRTIKGFMVLIEKDWVSFGHKFNHRYGYLDG--DPKEISPVIDQFIECIWQ 408
Cdd:cd14586   244 HCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRCGHGENsdDLNERCPVFLQWLDCVHQ 317
PH-GRAM_MTMR6-like cd13210
Myotubularian (MTM) related (MTMR) 7 and 8 proteins Pleckstrin Homology-Glucosyltransferases, ...
 8-103 5.41e-57

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: 187.87  E-value: 5.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282   8 KVENVRLIDRISSRKAALGTLYLTATHVIFVDNVSetRKETWILHSQISSIEKQATTVTGCPLLIRCKNFQIIQLIIPQE 87
Cdd:cd13210     5 KVENVRLLDRFSSRKPAVGTLYLTATHLIFVEPSG--KKETWILHSHIASVEKLPLTTAGCPLVIRCKNFQVITFVIPRE 82

                          90
                  ....*....|....*.
gi 1985373282  88 RDCHDVYISLIRLARP 103
Cdd:cd13210    83 RDCHDVYTSLLRLSRP 98
PH-GRAM_MTMR8 cd13345
Myotubularian (MTM) related 8 protein (MTMR8) Pleckstrin Homology-Glucosyltransferases, ...
 8-103 7.55e-45

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: 155.12  E-value: 7.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282   8 KVENVRLIDRISSRKAALGTLYLTATHVIFVDNVSETRKETWILHSQISSIEKQATTVTGCPLLIRCKNFQIIQLIIPQE 87
Cdd:cd13345     8 KVENVKLLDRYTNKKPANGTLYLTATHLIYVEASGAARKETWILHHHIATVEKLPLTSLGCPLLIRCKNFRVAHFVLDSE 87

                          90
                  ....*....|....*.
gi 1985373282  88 RDCHDVYISLIRLARP 103
Cdd:cd13345    88 RDCHEVYISLLKLSQP 103
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 146-412 6.10e-42

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: 153.29  E-value: 6.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 146 WQISDVNRDYQVCDSYPTEVYVPKSATAHIIVGSSKFRSRRRFPALSYYCKDNNASICRS-------------SQPLSGF 212
Cdd:cd14534     1 FRISTANRDYSICRSYPALVVVPQSVSDESLRKVARCYRQGRFPVVTWRHPRTKALLLRSggfhgkgvmgmlkSANTSTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 213 SARC--------LEDEQMLQAIrkanpgsnFIYVvdtrpklnaMANRAAGKGYENEdnySNIKFQFIGIE--NIHVMRSS 282
Cdd:cd14534    81 SPTVsssetsssLEQEKYLSAL--------VLYV---------LGEKSQMKGVKAE---SDPKCEFIPVEypEVRQVKAS 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 283 LQKMLEVCELKSPSMSD---FLWGLENSGWLKHIKAIMDagifIAKAVAE----EGMSVLVHCSDGWDRTAQVCSVASLL 355
Cdd:cd14534   141 FKKLLRACVPSSAPTEPeqsFLKAVEDSEWLQQLQCLMQ----LSGAVVDlldvQGSSVLLCLEDGWDVTTQVSSLSQLL 216

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1985373282 356 LDPFYRTIKGFMVLIEKDWVSFGHKFNHRYGYLDGDPKE-ISPVIDQFIECIWQLMEQ 412
Cdd:cd14534   217 LDPYYRTLEGFRVLVEKEWLAFGHRFSHRSNLTAASQSSgFAPVFLQFLDAVHQIHRQ 274
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 146-412 4.66e-40

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: 148.58  E-value: 4.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 146 WQISDVNRDYQVCDSYPTEVYVPKSATAHIIVGSSKFRSRRRFPALSYYCKDNNASICRS---------------SQPLS 210
Cdd:cd14588     1 FRISTVNRMYAVCRSYPGLLIVPQSIQDNTIQRISRCYRQNRFPVVCWRNSRTKAVLLRSgglhgkgvvglfksqNAPAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 211 GFS---ARCLEDEQMLQAIRKANP------GSNFIYVVdtRPKLNAMANRAAGKGYEnEDNYSNIKFQFIGIENIHVMRS 281
Cdd:cd14588    81 GQSqtdSTSLEQEKYLQAVINSMPryadasGRNTLSGF--RAALYIIGDKSQLKGVK-QDPLQQWEVVPIEVFDVRQVKA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 282 SLQKMLEVC---ELKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVaEEGMSVLVHCSDGWDRTAQVCSVASLLLDP 358
Cdd:cd14588   158 SFKKLMKACvpsCPSTDPSQTYLRTLEESEWLSQLHKLLQVSVLVVELL-DSGSSVLVSLEDGWDITTQVVSLVQLLSDP 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1985373282 359 FYRTIKGFMVLIEKDWVSFGHKFNHRYGY-LDGDPKEISPVIDQFIECIWQLMEQ 412
Cdd:cd14588   237 YYRTIEGFRLLVEKEWLSFGHRFSHRGAQtLASQSSGFTPVFLQFLDCVHQIHLQ 291
PH-GRAM_MTMR6 cd13343
Myotubularian (MTM) related (MTMR) 6 protein Pleckstrin Homology-Glucosyltransferases, ...
 1-103 8.80e-39

Myotubularian (MTM) related (MTMR) 6 protein Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR6 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR6 binds to phosphoinositide lipids through its PH-GRAM domain. It acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4+ T-cells possibly by decreasing intracellular levels of phosphatidylinositol-3 phosphatase and negatively regulates proliferation of reactivated CD4+ T-cells MTMR6 interacts with MTMR7, MTMR8 and MTMR9. MTMR6 contains a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, and a C-terminal coiled-coil region. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date.


Pssm-ID: 270151  Cd Length: 101  Bit Score: 138.22  E-value: 8.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282   1 MEDDPWMKVENVRLIDRIS-SRKAALGTLYLTATHVIFVDNvseTRKETWILHSQISSIEKQATTVTGCPLLIRCKNFQI 79
Cdd:cd13343     1 MEHIRTTKVEQVKLLDRFStSNKSLTGTLYLTATHLLFIDN---SQQETWILHHHIAPVEKLSLTTSGCPLVIQCKNFRV 77

                          90       100
                  ....*....|....*....|....
gi 1985373282  80 IQLIIPQERDCHDVYISLIRLARP 103
Cdd:cd13343    78 VHFVVPRERDCHDIYNSLLQLSRP 101
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 146-412 7.36e-38

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: 142.37  E-value: 7.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 146 WQISDVNRDYQVCDSYPTEVYVPKSATAHIIVGSSKFRSRRRFPALSYYCKDNNASICRS-------------SQ----- 207
Cdd:cd14589     1 FRITAVNRMYSLCRSYPGLLVVPQSVQDSSLQKVARCYRHNRLPVVCWKNSKTKAVLLRSggfhgkgvvglfkSQnphsa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 208 -PLSGFSARCLEDEQMLQAIRKANPGSNFIYVVDTRPKLNAMANRAAGKGYENEDNYSNIKF------QFIGIE--NIHV 278
Cdd:cd14589    81 aPASSESSSSIEQEKYLQALLNAISVHQKMNGNSTLLQSQLLKRQAALYIFGEKSQLRGFKLdfalncEFVPVEfhDIRQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 279 MRSSLQKMLEVC---ELKSPSMSDFLWGLENSGWLKHIKAIMDAGIFIAKaVAEEGMSVLVHCSDGWDRTAQVCSVASLL 355
Cdd:cd14589   161 VKASFKKLMRACvpsTIPTDSEVTFLKALGESEWFLQLHRIMQLAVVISE-LLESGSSVMVCLEDGWDITTQVVSLVQLL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1985373282 356 LDPFYRTIKGFMVLIEKDWVSFGHKFNHRYGY-LDGDPKEISPVIDQFIECIWQLMEQ 412
Cdd:cd14589   240 SDPFYRTLEGFQMLVEKEWLSFGHKFSQRSNLtPNSQGSGFAPIFLQFLDCVHQIHNQ 297
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 186-408 3.62e-28

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: 112.05  E-value: 3.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 186 RRFPALSYYCKdNNASICRSSQPLSGFSARCLEdEQMLQAIRKANPGSNFIYVVDTrpklnamanraagkgyenEDNYSN 265
Cdd:cd14537     1 GRPPVWCWSHP-NGAALVRMAELLPTITDRTQE-NKMLEAIRKSHPNLKKPKVIDL------------------DKLLPS 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 266 IKfqfigieNIHVmrsSLQKMLEVCELKSPS---MSDFLW--GLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSD 340
Cdd:cd14537    61 LQ-------DVQA---AYLKLRELCTPDSSEqfwVQDSKWysLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQESD 130

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 341 GWDRTAQVCSVASLLLDPFYRTIKGFMVLIEKDWVSFGHKFNHRYG--YLDGDPKEISPVIDQFIECIWQ 408
Cdd:cd14537   131 GRDLSCVVSSLVQLLLDPHFRTITGFQSLIQKEWVALGHPFCDRLGhvKPNKTESEESPVFLLFLDCVWQ 200
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 296-409 7.21e-23

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 11; Myotubularin related phosphoinositide phosphatase 11 (MTMR11), also called cisplatin resistance-associated protein (hCRA) in humans, is enzymatically inactive and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR11 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket.


Pssm-ID: 350443  Cd Length: 195  Bit Score: 96.82  E-value: 7.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 296 SMSDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWDRTAQVCSVASLLLDPFYRTIKGFMVLIEKDWV 375
Cdd:cd14595    82 SDEKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEWV 161

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1985373282 376 SFGHKFNHRYGYLDGDPKEISPVIDQFIECIWQL 409
Cdd:cd14595   162 VAGHPFLQRLNLTRESDKEESPVFLLFLDCVWQL 195
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 298-409 1.67e-18

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: 84.12  E-value: 1.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 298 SDFLW--GLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWDRTAQVCSVASLLLDPFYRTIKGFMVLIEKDWV 375
Cdd:cd14594    90 TDVKWfsSLESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQSLIQKEWV 169

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1985373282 376 SFGHKFNHRYGYLDGDPKEISPVIDQFIECIWQL 409
Cdd:cd14594   170 MGGHCFLDRCNHLRQNDKEEVPVFLLFLDCVWQL 203
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
 275-408 3.00e-17

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: 80.32  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 275 NIHVMRSSLQKMLEVCELKSPSMSDFLW--GLENSGWLKHIKAIMDAGIFIAKAVAEEGMSVLVHCSDGWDRTAQVCSVA 352
Cdd:cd14593    60 NIQEIQAAFVKLKQLCVNEPFEETEEKWlsSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLV 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1985373282 353 SLLLDPFYRTIKGFMVLIEKDWVSFGHKFNHRYGYLDGDPKEISPVIDQFIECIWQ 408
Cdd:cd14593   140 QVMLDPYFRTITGFQSLIQKEWVMAGYRFLDRCNHLKKSSKKESPLFLLFLDCVWQ 195
PH-GRAM_MTMR9 cd13211
Myotubularian (MTM) related 9 protein (MTMR9) Pleckstrin Homology-Glucosyltransferases, ...
 8-97 1.02e-15

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: 73.08  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282   8 KVENVRLidRISSRKAALGTLYLTATHVIFVDNvSETRKETWILHSQISSIEK-QATTVTGCPLLIRCKNFQIIQLIIPQ 86
Cdd:cd13211    11 KVDNVVL--HRPPRPAVEGTLCITGHHLILSSR-QDNAEELWLLHSNIDSVEKkFVGKSSGGTLTLKCKDFRIIQLDIPD 87

                          90
                  ....*....|.
gi 1985373282  87 ERDCHDVYISL 97
Cdd:cd13211    88 MEECLNIASSI 98
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 12-93 7.45e-11

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: 58.93  E-value: 7.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282  12 VRLIDRISSRKAAL-GTLYLTATHVIFVDNVSETRKETWILHSQISSIEKQATTVT-GCPLLIRCKNFQIIQLIIPQERD 89
Cdd:cd10570     6 VRFCCALRPRKLPLeGTLYLSTYRLIFSSKADGDETKLVIPLVDITDVEKIAGASFlPSGLIITCKDFRTIKFSFDSEDE 85


                  ....
gi 1985373282  90 CHDV 93
Cdd:cd10570    86 AVKV 89
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
333-432 1.67e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 44.27  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282  333 SVLVHCSDGWDRTAQVCSVASLLLDPFYRTIKgfmvliekdwvsfghkfnhrygyldgdpkeispvIDQFiECIWQLMEQ 412
Cdd:smart00404  41 PVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE----------------------------------VDIF-DTVKELRSQ 85

                           90       100
                   ....*....|....*....|
gi 1985373282  413 FPCAFEFNERFLIHIQHHIY 432
Cdd:smart00404  86 RPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 333-432 1.67e-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: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282  333 SVLVHCSDGWDRTAQVCSVASLLLDPFYRTIKgfmvliekdwvsfghkfnhrygyldgdpkeispvIDQFiECIWQLMEQ 412
Cdd:smart00012  41 PVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE----------------------------------VDIF-DTVKELRSQ 85

                           90       100
                   ....*....|....*....|
gi 1985373282  413 FPCAFEFNERFLIHIQHHIY 432
Cdd:smart00012  86 RPGMVQTEEQYLFLYRALLE 105
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 245-356 1.81e-03

dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is composed of dual specificity protein phosphatase 3 (DUSP3, also known as VHR), 13B (DUSP13B, also known as TMDP), 26 (DUSP26, also known as MPK8), 13A (DUSP13A, also known as MDSP), dual specificity phosphatase and pro isomerase domain containing 1 (DUPD1), and inactive DUSP27. In general, DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Members of this family are atypical DUSPs; they contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Inactive DUSP27 contains a dual specificity phosphatase-like domain with the active site cysteine substituted to serine.


Pssm-ID: 350365 [Multi-domain]  Cd Length: 148  Bit Score: 39.12  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985373282 245 LNAMANRAAGKGYENEDNYSNIKFQFIGIEnihvmrsslqkmleVCELKSPSMSDFLWglensgwlkhikaimDAGIFIA 324
Cdd:cd14515    31 LNAAEGKKNGEVNTNAKFYKGSGIIYLGIP--------------ASDLPTFDISQYFD---------------EAADFID 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1985373282 325 KAVAEEGMSVLVHCSDGWDRTAqVCSVASLLL 356
Cdd:cd14515    82 KALSDPGGKVLVHCVEGVSRSA-TLVLAYLMI 112
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 293-350 9.95e-03

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 36.56  E-value: 9.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985373282 293 KSPSMSDFLWGLENsgwlKHI----KAIMDAGIFIAKAVAEEGMSVLVHCSDGWDRTAQVCS 350
Cdd:cd14494    18 PLEADSRFLKQLGV----TTIvdltLAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVA 75
 
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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