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Conserved domains on  [gi|94536956|ref|NP_001035406|]
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Protein Classification

PH-GRAM_MTMR7 and PTP_DSP_cys domain-containing protein (domain architecture ID 12988795)

PH-GRAM_MTMR7 and PTP_DSP_cys domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
132-433 0e+00

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.


The actual alignment was detected with superfamily member cd14583:

Pssm-ID: 421693  Cd Length: 302  Bit Score: 657.42  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 132 LKAEYSRMGLPNKLWHVTPINRDYRVCDTYPADLFVPKSVTLPVIVGSSKFRSRGRFPTLSYYCKENHATICRSSQPLSG 211
Cdd:cd14583   1 LKAEYNRMGLPNSLWQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYYCKDNNASICRSSQPLSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 212 FSARCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYCNIKFQFIGIENIHVMRNSQQKLIEVSA 291
Cdd:cd14583  81 FSARCLEDEQMLQAIRKANPGSDFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 292 LRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYRTIKGMMVLIE 371
Cdd:cd14583 161 LRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIE 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 94536956 372 KDWVSFGHKFSHRCGHLDGEAKEVSPVLDQFLECVWQLMDQFPCAFEYNEKFLISIHNHVYS 433
Cdd:cd14583 241 KDWVSFGHKFNHRYGHLDGDPKEVSPVIDQFIECVWQLMEQFPCAFEFNERFLIHIHHHIYS 302
PH-GRAM_MTMR7 cd13344
Myotubularian (MTM) related 7 protein (MTMR7) Pleckstrin Homology-Glucosyltransferases, ...
1-103 9.19e-66

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: 210.93  E-value: 9.19e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   1 MEHIRMPKVENVRLVDRSSSRKSQVGTLYLTATHTIFVGKGSEDRNELWVLHSLVCNIVKHKASQSGYPLLIHCKNFQVI 80
Cdd:cd13344   1 MEHIRMPKVENVRLVDRISSKKAALGTLYLTATHVIFVENSSDTRKETWILHSQISSIEKQATTATGCPLLIRCKNFQVI 80
                        90       100
                ....*....|....*....|...
gi 94536956  81 QFIILQESDLHNVYISLTRLSRP 103
Cdd:cd13344  81 QLIIPQERDCHDVYISLIRLARP 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  Cd Length: 302  Bit Score: 657.42  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 132 LKAEYSRMGLPNKLWHVTPINRDYRVCDTYPADLFVPKSVTLPVIVGSSKFRSRGRFPTLSYYCKENHATICRSSQPLSG 211
Cdd:cd14583   1 LKAEYNRMGLPNSLWQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYYCKDNNASICRSSQPLSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 212 FSARCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYCNIKFQFIGIENIHVMRNSQQKLIEVSA 291
Cdd:cd14583  81 FSARCLEDEQMLQAIRKANPGSDFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 292 LRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYRTIKGMMVLIE 371
Cdd:cd14583 161 LRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIE 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 94536956 372 KDWVSFGHKFSHRCGHLDGEAKEVSPVLDQFLECVWQLMDQFPCAFEYNEKFLISIHNHVYS 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: 399535  Cd Length: 330  Bit Score: 599.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   124 QHSWDFIDLKAEYSRMGLPNK-LWHVTPINRDYRVCDTYPADLFVPKSVTLPVIVGSSKFRSRGRFPTLSYYCKENHATI 202
Cdd:pfam06602   2 ENGWDLYDPEAEFARQGLPSKdEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   203 CRSSQPLSGF-SARCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYCNIKFQFIGIENIHVMRN 281
Cdd:pfam06602  82 TRSSQPLVGLnGKRCIEDEKLLNAIFKSNPYSKKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   282 SQQKLIEVSALRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYR 361
Cdd:pfam06602 162 SLNKLVEACNDRSSSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYYR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   362 TIKGMMVLIEKDWVSFGHKFSHRCGHLDG--EAKEVSPVLDQFLECVWQLMDQFPCAFEYNEKFLISIHNHVYSSHYGNF 439
Cdd:pfam06602 242 TIEGFQVLIEKEWLSFGHKFADRCGHLAYfsDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLDHLYSCQFGTF 321

                  ....*....
gi 94536956   440 ICNSQKERK 448
Cdd:pfam06602 322 LCNSEKERV 330
PH-GRAM_MTMR7 cd13344
Myotubularian (MTM) related 7 protein (MTMR7) Pleckstrin Homology-Glucosyltransferases, ...
1-103 9.19e-66

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: 210.93  E-value: 9.19e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   1 MEHIRMPKVENVRLVDRSSSRKSQVGTLYLTATHTIFVGKGSEDRNELWVLHSLVCNIVKHKASQSGYPLLIHCKNFQVI 80
Cdd:cd13344   1 MEHIRMPKVENVRLVDRISSKKAALGTLYLTATHVIFVENSSDTRKETWILHSQISSIEKQATTATGCPLLIRCKNFQVI 80
                        90       100
                ....*....|....*....|...
gi 94536956  81 QFIILQESDLHNVYISLTRLSRP 103
Cdd:cd13344  81 QLIIPQERDCHDVYISLIRLARP 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
310-428 3.76e-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: 43.12  E-value: 3.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956    310 LKHIRSIMEagifiSKAVADEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYRTIKgmmvliekdwvsfghkfshrcghld 389
Cdd:smart00012  23 LELLRAVKK-----NLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE------------------------- 72
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 94536956    390 geakevspvlDQFLECVWQLMDQFPCAFEYNEKFLISIH 428
Cdd:smart00012  73 ----------VDIFDTVKELRSQRPGMVQTEEQYLFLYR 101
 
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  Cd Length: 302  Bit Score: 657.42  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 132 LKAEYSRMGLPNKLWHVTPINRDYRVCDTYPADLFVPKSVTLPVIVGSSKFRSRGRFPTLSYYCKENHATICRSSQPLSG 211
Cdd:cd14583   1 LKAEYNRMGLPNSLWQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYYCKDNNASICRSSQPLSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 212 FSARCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYCNIKFQFIGIENIHVMRNSQQKLIEVSA 291
Cdd:cd14583  81 FSARCLEDEQMLQAIRKANPGSDFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 292 LRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYRTIKGMMVLIE 371
Cdd:cd14583 161 LRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIAKAVAEEGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIE 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 94536956 372 KDWVSFGHKFSHRCGHLDGEAKEVSPVLDQFLECVWQLMDQFPCAFEYNEKFLISIHNHVYS 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  Cd Length: 301  Bit Score: 618.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 132 LKAEYSRMGLPNKLWHVTPINRDYRVCDTYPADLFVPKSVTLPVIVGSSKFRSRGRFPTLSYYCKENHATICRSSQPLSG 211
Cdd:cd14532   1 LESEYTRMGVPNDNWTLSDINKDYELCDTYPRELFVPTSASTPVLVGSSKFRSKGRLPVLSYLHKDNQAAICRCSQPLSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 212 FSARCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYCNIKFQFIGIENIHVMRNSQQKLIEVSA 291
Cdd:cd14532  81 FSARCVEDEQLLQAIRKANPNSKFMYVVDTRPKINAMANKAAGKGYENEDNYSNIKFQFFGIENIHVMRSSLQKLLEVCE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 292 LRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVaDEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYRTIKGMMVLIE 371
Cdd:cd14532 161 LKNPSMSAFLSGLESSGWLKHIKAVMDTSVFIAKAV-SEGASVLVHCSDGWDRTAQTCSLASLLLDPYYRTIKGFQVLIE 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 94536956 372 KDWVSFGHKFSHRCGHLDGEAKEVSPVLDQFLECVWQLMDQFPCAFEYNEKFLISIHNHVYS 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: 399535  Cd Length: 330  Bit Score: 599.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   124 QHSWDFIDLKAEYSRMGLPNK-LWHVTPINRDYRVCDTYPADLFVPKSVTLPVIVGSSKFRSRGRFPTLSYYCKENHATI 202
Cdd:pfam06602   2 ENGWDLYDPEAEFARQGLPSKdEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   203 CRSSQPLSGF-SARCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYCNIKFQFIGIENIHVMRN 281
Cdd:pfam06602  82 TRSSQPLVGLnGKRCIEDEKLLNAIFKSNPYSKKLYIVDARPKLNAMANRAKGGGYENEDNYPNCKKIFLGIENIHVMRD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   282 SQQKLIEVSALRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYR 361
Cdd:pfam06602 162 SLNKLVEACNDRSSSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDLEGSSVLVHCSDGWDRTAQLTSLAQLLLDPYYR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   362 TIKGMMVLIEKDWVSFGHKFSHRCGHLDG--EAKEVSPVLDQFLECVWQLMDQFPCAFEYNEKFLISIHNHVYSSHYGNF 439
Cdd:pfam06602 242 TIEGFQVLIEKEWLSFGHKFADRCGHLAYfsDSKERSPVFLQFLDCVWQLLRQFPCAFEFNERFLIRLLDHLYSCQFGTF 321

                  ....*....
gi 94536956   440 ICNSQKERK 448
Cdd:pfam06602 322 LCNSEKERV 330
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
127-433 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  Cd Length: 308  Bit Score: 573.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 127 WDFIDLKAEYSRMGLPNKLWHVTPINRDYRVCDTYPADLFVPKSVTLPVIVGSSKFRSRGRFPTLSYYCKENHATICRSS 206
Cdd:cd14584   2 WKLIDLKVDFQRMGIPNDYWEITDANKNYEICSTYPPELVVPKSASKATVVGSSKFRSRGRFPVLSYLYKENNAAICRCS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 207 QPLSGFSARCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYCNIKFQFIGIENIHVMRNSQQKL 286
Cdd:cd14584  82 QPLSGFSARCVEDEQMLQAISKANPGSPFMYVVDTRPKLNAMANRAAGKGYENEDNYSNIRFQFIGIENIHVMRSSLQKL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 287 IEVSALRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYRTIKGM 366
Cdd:cd14584 162 LEVCEMKSPSMSDFLTGLENSGWLRHIKAVMDAGVFLAKAVKEEKASVLVHCSDGWDRTAQVCSLASLLLDPFYRTIKGL 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94536956 367 MVLIEKDWVSFGHKFSHRCGHLDGEAKEVSPVLDQFLECVWQLMDQFPCAFEYNEKFLISIHNHVYS 433
Cdd:cd14584 242 MVLIEKEWISMGHKFSQRCGHLDGDPKEVSPVFTQFLECVWQLMEQFPCAFEFNEHFLLEIHDHVFS 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  Cd Length: 302  Bit Score: 541.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 132 LKAEYSRMGLPNKLWHVTPINRDYRVCDTYPADLFVPKSVTLPVIVGSSKFRSRGRFPTLSYYCKENHATICRSSQPLSG 211
Cdd:cd14585   1 LAEEYKRMGVPNDYWQLSDVNRDYKICDTYPRDLYVPITASKPIIVGSSKFRSKGRFPVLSYYHQEKKAAICRCSQPLSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 212 FSARCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYCNIKFQFIGIENIHVMRNSQQKLIEVSA 291
Cdd:cd14585  81 FSARCLEDEHMLQAISKANPNNRYMYVMDTRPKLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 292 LRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYRTIKGMMVLIE 371
Cdd:cd14585 161 TKALSVNDFLSGLESSGWLRHIKAVLDAAVFLAKAVAVEGASVLVHCSDGWDRTAQVCSLGSLLLDPYYRTIKGFMVLIE 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 94536956 372 KDWVSFGHKFSHRCGHLDGEAKEVSPVLDQFLECVWQLMDQFPCAFEYNEKFLISIHNHVYS 433
Cdd:cd14585 241 KDWISFGHKFSDRCGQLDGDPKEISPVFTQFLECVWQLTEQFPRAFEFSEAFLLQIHEHIHS 302
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
186-408 6.77e-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: 361.09  E-value: 6.77e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 186 GRFPTLSYYCKENHATICRSSQPLSGF-SARCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYC 264
Cdd:cd14507   1 GRIPVLSWRHPRNGAVICRSSQPLVGLtGSRSKEDEKLLNAIRKASPSSKKLYIVDARPKLNAVANRAKGGGYENTEYYP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 265 NIKFQFIGIENIHVMRNSQQKLIEVSALRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWDR 344
Cdd:cd14507  81 NCELEFLNIENIHAMRDSLNKLRDACLSPNDEESNWLSALESSGWLEHIRLILKGAVRVADLLEKEGTSVLVHCSDGWDR 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94536956 345 TSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFGHKFSHRCGHLDGEA--KEVSPVLDQFLECVWQ 408
Cdd:cd14507 161 TSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHGDKNSsdEERSPIFLQFLDCVWQ 226
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
186-432 3.54e-95

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: 293.20  E-value: 3.54e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 186 GRFPTLSYYCKENHATICRSSQPLSGFSA-RCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYC 264
Cdd:cd14535   1 NRIPVLSWIHPESQATITRCSQPLVGVSGkRSKDDEKYLQLIMDANAQSHKLFIMDARPSVNAVANKAKGGGYESEDAYQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 265 NIKFQFIGIENIHVMRNSQQKLIEVSAlrsPSMGE--FLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGW 342
Cdd:cd14535  81 NAELVFLDIHNIHVMRESLRKLKDICF---PNIDDshWLSNLESTHWLEHIKLILAGAVRIADKVESGKTSVVVHCSDGW 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 343 DRTSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFGHKFSHRCGHLDGEAKEV--SPVLDQFLECVWQLMDQFPCAFEYN 420
Cdd:cd14535 158 DRTAQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRIGHGDKNHSDAdrSPVFLQFIDCVWQMTRQFPNAFEFN 237
                       250
                ....*....|..
gi 94536956 421 EKFLISIHNHVY 432
Cdd:cd14535 238 EHFLITILDHLY 249
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
180-432 2.35e-94

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: 291.55  E-value: 2.35e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 180 SKFRSRGRFPTLSYYCKENHATICRSSQPLSGFSA-RCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYE 258
Cdd:cd14590   8 ASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGkRSKEDEKYLQAIMDSNAQSHKIFIFDARPSVNAVANKAKGGGYE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 259 NEDNYCNIKFQFIGIENIHVMRNSQQKLIEVSalrSPSMGE--FLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLV 336
Cdd:cd14590  88 SEDAYQNAELVFLDIHNIHVMRESLRKLKEIV---YPNIEEshWLSNLESTHWLEHIKLILAGALRIADKVESGKTSVVV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 337 HCSDGWDRTSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFGHKFSHRCGHLDGEAKEV--SPVLDQFLECVWQLMDQFP 414
Cdd:cd14590 165 HCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADAdrSPVFLQFIDCVWQMTRQFP 244
                       250
                ....*....|....*...
gi 94536956 415 CAFEYNEKFLISIHNHVY 432
Cdd:cd14590 245 TAFEFNEYFLITILDHLY 262
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
187-432 1.37e-84

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: 265.74  E-value: 1.37e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 187 RFPTLSYYCKENHATICRSSQPLSGFSA-RCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYCN 265
Cdd:cd14591   2 RIPVLSWIHPENQAVIMRCSQPLVGMSGkRNKDDEKYLDIIREANGQTSKLTIYDARPSVNAVANKATGGGYEGDDAYQN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 266 IKFQFIGIENIHVMRNSQQKLIEVSalrSPSMGE--FLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWD 343
Cdd:cd14591  82 AELVFLDIHNIHVMRESLKKLKDIV---YPNVEEshWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 344 RTSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFGHKFSHRCGHLDGEAKEV--SPVLDQFLECVWQLMDQFPCAFEYNE 421
Cdd:cd14591 159 RTAQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRIGHGDKNHADAdrSPIFLQFIDCVWQMSKQFPTAFEFNE 238
                       250
                ....*....|.
gi 94536956 422 KFLISIHNHVY 432
Cdd:cd14591 239 QFLITILDHLY 249
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
186-408 1.76e-81

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: 256.99  E-value: 1.76e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 186 GRFPTLSYYCKENHATICRSSQPLSGF-SARCLEDEQMLQAIMKS------NPGSRFMyVVDTRPKLNAMANRAAGKGYE 258
Cdd:cd17666   1 QRIPVLTYLHKANGCSITRSSQPLVGLkQNRSIQDEKLVSEIFNTsineiyISPQKNL-IVDARPTTNAMAQVALGAGTE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 259 NEDNYCN--IKFQFIGIENIHVMRNSQQKLIEV------SALRSPSMGEFLLgleNSDWLKHIRSIMEAGIFISKAVADE 330
Cdd:cd17666  80 NMDNYKYktAKKIYLGIDNIHVMRDSLNKVTEAlkdgddSNPSYPPLINALK---KSNWLKYLAIILQGADLIAKSIHFN 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 94536956 331 GVSVLVHCSDGWDRTSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFGHKFSHRCGHldgeaKEVSPVLDQFLECVWQ 408
Cdd:cd17666 157 HSHVLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSFGHRFAERSGH-----KETSPVFHQFLDCVYQ 229
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
186-432 3.22e-80

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: 254.52  E-value: 3.22e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 186 GRFPTLSYYCKENHATICRSSQPLSGFS-ARCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYC 264
Cdd:cd14592   1 GRVPVLSWIHPESQATITRCSQPLVGPNdKRCKEDEKYLQTIMDANAQSHKLIIFDARQNSVADTNKTKGGGYESESAYP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 265 NIKFQFIGIENIHVMRNSQQKLIEVSalrSPSMGE--FLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGW 342
Cdd:cd14592  81 NAELVFLEIHNIHVMRESLRKLKEIV---YPSIDEarWLSNVDGTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGW 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 343 DRTSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFGHKFSHRCGHLDGEAKEV--SPVLDQFLECVWQLMDQFPCAFEYN 420
Cdd:cd14592 158 DRTAQLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRVGHGDDNHADAdrSPIFLQFIDCVWQMTRQFPSAFEFN 237
                       250
                ....*....|..
gi 94536956 421 EKFLISIHNHVY 432
Cdd:cd14592 238 ELFLITILDHLY 249
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
146-408 1.64e-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  Cd Length: 308  Bit Score: 231.07  E-value: 1.64e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 146 WHVTPINRDYRVCDTYPADLFVPKSVTLPVIVGSSKFRSRGRFPTLSYYCKENHATICRSSQP-LSGFSARCLEDEQMLQ 224
Cdd:cd14587   3 WRVSEINSNYKLCSSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAVIARCSQPeISWWGWRNADDEYLVT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 225 AIMKS---NPGSRF--------------------------------------MYVVDTRPKLNAMANRAAGKGYENEDNY 263
Cdd:cd14587  83 SIAKAcalDPGTRApggspskgnsdgsdasdtdfdssltacsavesgaapqkLLILDARSYTAAVANRAKGGGCECEEYY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 264 CNIKFQFIGIENIHVMRNSQQKLIEVSAlRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWD 343
Cdd:cd14587 163 PNCEVMFMGMANIHSIRNSFQYLRAVCS-QMPDPGNWLSALESTKWLQHLSVMLKAAVLVASAVDREGRPVLVHCSDGWD 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94536956 344 RTSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFGHKFSHRCGHLDG--EAKEVSPVLDQFLECVWQ 408
Cdd:cd14587 242 RTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHQENveDQNEQCPVFLQWLDCVHQ 308
PH-GRAM_MTMR7 cd13344
Myotubularian (MTM) related 7 protein (MTMR7) Pleckstrin Homology-Glucosyltransferases, ...
1-103 9.19e-66

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: 210.93  E-value: 9.19e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   1 MEHIRMPKVENVRLVDRSSSRKSQVGTLYLTATHTIFVGKGSEDRNELWVLHSLVCNIVKHKASQSGYPLLIHCKNFQVI 80
Cdd:cd13344   1 MEHIRMPKVENVRLVDRISSKKAALGTLYLTATHVIFVENSSDTRKETWILHSQISSIEKQATTATGCPLLIRCKNFQVI 80
                        90       100
                ....*....|....*....|...
gi 94536956  81 QFIILQESDLHNVYISLTRLSRP 103
Cdd:cd13344  81 QLIIPQERDCHDVYISLIRLARP 103
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
186-408 1.71e-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: 214.96  E-value: 1.71e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 186 GRFPTLSYYCKENHATICRSSQPLSGF-SARCLEDEQMLQAIMKSNPGS---RFMYVVDTRPKLNAMANRAAGKGYENED 261
Cdd:cd14533   2 KRIPSVVWRHQRNGAVIARCSQPEVGWlGWRNAEDENLLQAIAEACASNaspKKLLIVDARSYAAAVANRAKGGGCECPE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 262 NYCNIKFQFIGIENIHVMRNSQQKLIEVSAlRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDG 341
Cdd:cd14533  82 YYPNCEVVFMNLANIHAIRKSFHSLRALCS-SAPDQPNWLSNLESTKWLHHLSGLLKAALLVVNAVDEEGRPVLVHCSDG 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 94536956 342 WDRTSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFGHKFSHRCGHLDG--EAKEVSPVLDQFLECVWQ 408
Cdd:cd14533 161 WDRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFGHKFADRCGHGVNseDINERCPVFLQWLDCVHQ 229
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
186-408 7.12e-63

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: 207.96  E-value: 7.12e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 186 GRFPTLSYYCKENHATICRSSQPLSGFSA-RCLEDEQMLQAIMKsnpGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYC 264
Cdd:cd14536   1 GRFPVLSYYHKKNGMVLMRSSQPLTGPNGkRCKEDEKLLNAVLG---GGKRGYIIDTRSKNVAQQARAKGGGFEPEAHYP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 265 NIKFQFIGIENIHVMRNSQQKLIEVSALRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWDR 344
Cdd:cd14536  78 QWRRIHKPIERYNVLQESLIKLVEACNDQGHSMDKWLSKLESSNWLSHVKEILTTACLVAQCIDREGASVLVHGSEGMDS 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94536956 345 TSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFGHKFSHRCGHL---DGEAKEVSPVLDQFLECVWQ 408
Cdd:cd14536 158 TLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPFQSRCAKSaysNSKQKFESPVFLLFLDCVWQ 224
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
143-408 1.06e-61

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: 207.95  E-value: 1.06e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 143 NKLWHVTPINRDYRVCDTYPADLFVPKSVTLPVIVGSSKFRSRGRFPTLSYYCKENHATICRSSQP-LSGFSARCLEDEQ 221
Cdd:cd14586   5 QNAWRISNINEKYKLCGSYPQELIVPAWITDKELESVASFRSWKRIPAVVYRHQSNGAVIARCGQPeVSWWGWRNADDEH 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 222 MLQAIMK------------SNPGS---------------------------------RFMYVVDTRPKLNAMANRAAGKG 256
Cdd:cd14586  85 LVQSVAKacasdssscksvLMTGNcsrdfpnggdlsdvefdssmsnasgveslaiqpQKLLILDARSYAAAVANRAKGGG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 257 YENEDNYCNIKFQFIGIENIHVMRNSQQKLiEVSALRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLV 336
Cdd:cd14586 165 CECPEYYPNCEVVFMGMANIHSIRKSFQSL-RLLCTQMPDPANWLSALESTKWLQHLSMLLKSALLVVHAVDRDQRPVLV 243
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 94536956 337 HCSDGWDRTSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFGHKFSHRCGHLDG--EAKEVSPVLDQFLECVWQ 408
Cdd:cd14586 244 HCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRCGHGENsdDLNERCPVFLQWLDCVHQ 317
PH-GRAM_MTMR6-like cd13210
Myotubularian (MTM) related (MTMR) 7 and 8 proteins Pleckstrin Homology-Glucosyltransferases, ...
4-103 1.35e-50

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: 170.54  E-value: 1.35e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   4 IRMPKVENVRLVDRSSSRKSQVGTLYLTATHTIFVGKGSedRNELWVLHSLVCNIVKHKASQSGYPLLIHCKNFQVIQFI 83
Cdd:cd13210   1 IRTPKVENVRLLDRFSSRKPAVGTLYLTATHLIFVEPSG--KKETWILHSHIASVEKLPLTTAGCPLVIRCKNFQVITFV 78
                        90       100
                ....*....|....*....|
gi 94536956  84 ILQESDLHNVYISLTRLSRP 103
Cdd:cd13210  79 IPRERDCHDVYTSLLRLSRP 98
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
146-412 1.04e-44

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  Cd Length: 274  Bit Score: 160.61  E-value: 1.04e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 146 WHVTPINRDYRVCDTYPADLFVPKSVTLPVIVGSSKFRSRGRFPTLSYYCKENHATICRS-------------SQPLSGF 212
Cdd:cd14534   1 FRISTANRDYSICRSYPALVVVPQSVSDESLRKVARCYRQGRFPVVTWRHPRTKALLLRSggfhgkgvmgmlkSANTSTS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 213 SARC--------LEDEQMLQAIMksnpgsrfMYVvdtrpklnaMANRAAGKGYENEDNYcniKFQFIGIE--NIHVMRNS 282
Cdd:cd14534  81 SPTVsssetsssLEQEKYLSALV--------LYV---------LGEKSQMKGVKAESDP---KCEFIPVEypEVRQVKAS 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 283 QQKLIEV---SALRSPSMGEFLLGLENSDWLKHIRSIMEagifISKAVAD----EGVSVLVHCSDGWDRTSQVCSVASVL 355
Cdd:cd14534 141 FKKLLRAcvpSSAPTEPEQSFLKAVEDSEWLQQLQCLMQ----LSGAVVDlldvQGSSVLLCLEDGWDVTTQVSSLSQLL 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 94536956 356 LDPYYRTIKGMMVLIEKDWVSFGHKFSHRCGH-LDGEAKEVSPVLDQFLECVWQLMDQ 412
Cdd:cd14534 217 LDPYYRTLEGFRVLVEKEWLAFGHRFSHRSNLtAASQSSGFAPVFLQFLDAVHQIHRQ 274
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
146-412 3.08e-44

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  Cd Length: 291  Bit Score: 160.13  E-value: 3.08e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 146 WHVTPINRDYRVCDTYPADLFVPKSVTLPVIVGSSKFRSRGRFPTLSYYCKENHATICRS---------------SQPLS 210
Cdd:cd14588   1 FRISTVNRMYAVCRSYPGLLIVPQSIQDNTIQRISRCYRQNRFPVVCWRNSRTKAVLLRSgglhgkgvvglfksqNAPAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 211 GFS---ARCLEDEQMLQAIMKSNPGSRFMYVVDT----RPKLNAMANRAAGKGYEnEDNYCNIKFQFIGIENIHVMRNSQ 283
Cdd:cd14588  81 GQSqtdSTSLEQEKYLQAVINSMPRYADASGRNTlsgfRAALYIIGDKSQLKGVK-QDPLQQWEVVPIEVFDVRQVKASF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 284 QKLIEV---SALRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKAVaDEGVSVLVHCSDGWDRTSQVCSVASVLLDPYY 360
Cdd:cd14588 160 KKLMKAcvpSCPSTDPSQTYLRTLEESEWLSQLHKLLQVSVLVVELL-DSGSSVLVSLEDGWDITTQVVSLVQLLSDPYY 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 94536956 361 RTIKGMMVLIEKDWVSFGHKFSHRCGH-LDGEAKEVSPVLDQFLECVWQLMDQ 412
Cdd:cd14588 239 RTIEGFRLLVEKEWLSFGHRFSHRGAQtLASQSSGFTPVFLQFLDCVHQIHLQ 291
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
148-412 1.66e-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: 144.29  E-value: 1.66e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 148 VTPINRDYRVCDTYPADLFVPKSVTLPVIVGSSKFRSRGRFPTLSYYCKENHATICRS-------------SQ------P 208
Cdd:cd14589   3 ITAVNRMYSLCRSYPGLLVVPQSVQDSSLQKVARCYRHNRLPVVCWKNSKTKAVLLRSggfhgkgvvglfkSQnphsaaP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 209 LSGFSARCLEDEQMLQAIMKSNPGSRFMYVVDTRPKLNAMANRAAGKGYENEDNYCNIKFQF--------IGIENIHVMR 280
Cdd:cd14589  83 ASSESSSSIEQEKYLQALLNAISVHQKMNGNSTLLQSQLLKRQAALYIFGEKSQLRGFKLDFalncefvpVEFHDIRQVK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 281 NSQQKLIEV---SALRSPSMGEFLLGLENSDWLKHIRSIMEAGIFISKaVADEGVSVLVHCSDGWDRTSQVCSVASVLLD 357
Cdd:cd14589 163 ASFKKLMRAcvpSTIPTDSEVTFLKALGESEWFLQLHRIMQLAVVISE-LLESGSSVMVCLEDGWDITTQVVSLVQLLSD 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 94536956 358 PYYRTIKGMMVLIEKDWVSFGHKFSHRCG-HLDGEAKEVSPVLDQFLECVWQLMDQ 412
Cdd:cd14589 242 PFYRTLEGFQMLVEKEWLSFGHKFSQRSNlTPNSQGSGFAPIFLQFLDCVHQIHNQ 297
PH-GRAM_MTMR8 cd13345
Myotubularian (MTM) related 8 protein (MTMR8) Pleckstrin Homology-Glucosyltransferases, ...
1-103 9.66e-37

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: 132.77  E-value: 9.66e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   1 MEHIRMPKVENVRLVDRSSSRKSQVGTLYLTATHTIFVGKGSEDRNELWVLHSLVCNIVKHKASQSGYPLLIHCKNFQVI 80
Cdd:cd13345   1 MEHITTPKVENVKLLDRYTNKKPANGTLYLTATHLIYVEASGAARKETWILHHHIATVEKLPLTSLGCPLLIRCKNFRVA 80
                        90       100
                ....*....|....*....|...
gi 94536956  81 QFIILQESDLHNVYISLTRLSRP 103
Cdd:cd13345  81 HFVLDSERDCHEVYISLLKLSQP 103
PH-GRAM_MTMR6 cd13343
Myotubularian (MTM) related (MTMR) 6 protein Pleckstrin Homology-Glucosyltransferases, ...
1-103 2.20e-31

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: 117.81  E-value: 2.20e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   1 MEHIRMPKVENVRLVDR-SSSRKSQVGTLYLTATHTIFVGKGSEdrnELWVLHSLVCNIVKHKASQSGYPLLIHCKNFQV 79
Cdd:cd13343   1 MEHIRTTKVEQVKLLDRfSTSNKSLTGTLYLTATHLLFIDNSQQ---ETWILHHHIAPVEKLSLTTSGCPLVIQCKNFRV 77
                        90       100
                ....*....|....*....|....
gi 94536956  80 IQFIILQESDLHNVYISLTRLSRP 103
Cdd:cd13343  78 VHFVVPRERDCHDIYNSLLQLSRP 101
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
186-408 5.55e-30

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: 117.06  E-value: 5.55e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 186 GRFPTLSYYCKeNHATICRSSQPLSGFSARCLEdEQMLQAIMKSNPGSRFMYVVDTrpklnamanraagkgyeneDNYCN 265
Cdd:cd14537   1 GRPPVWCWSHP-NGAALVRMAELLPTITDRTQE-NKMLEAIRKSHPNLKKPKVIDL-------------------DKLLP 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 266 IkfqfigIENIHVmrnSQQKLIEVSALRSPSMGE-----FLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSD 340
Cdd:cd14537  60 S------LQDVQA---AYLKLRELCTPDSSEQFWvqdskWYSLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQESD 130
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 341 GWDRTSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFGHKFSHRCGHL--DGEAKEVSPVLDQFLECVWQ 408
Cdd:cd14537 131 GRDLSCVVSSLVQLLLDPHFRTITGFQSLIQKEWVALGHPFCDRLGHVkpNKTESEESPVFLLFLDCVWQ 200
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
304-409 4.23e-22

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatase 12; Myotubularin related phosphoinositide phosphatase 12 (MTMR12), also called phosphatidylinositol 3 phosphate 3-phosphatase adapter subunit (3-PAP), is enzymatically inactive and contains a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR12 is a pseudophosphatase that lacks the catalytic cysteine in its catalytic pocket. It functions as an adapter for the catalytically active myotubularin to regulate its intracellular location.


Pssm-ID: 350442  Cd Length: 203  Bit Score: 94.52  E-value: 4.23e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 304 LENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFGHKFSH 383
Cdd:cd14594  98 LESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQSLIQKEWVMGGHCFLD 177
                        90       100
                ....*....|....*....|....*.
gi 94536956 384 RCGHLDGEAKEVSPVLDQFLECVWQL 409
Cdd:cd14594 178 RCNHLRQNDKEEVPVFLLFLDCVWQL 203
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
301-409 1.49e-21

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: 92.97  E-value: 1.49e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 301 LLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFGHK 380
Cdd:cd14595  87 LSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQLLSDPHARTISGFQSLVQKEWVVAGHP 166
                        90       100
                ....*....|....*....|....*....
gi 94536956 381 FSHRCGHLDGEAKEVSPVLDQFLECVWQL 409
Cdd:cd14595 167 FLQRLNLTRESDKEESPVFLLFLDCVWQL 195
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
299-408 1.25e-20

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: 89.95  E-value: 1.25e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956 299 EFLLGLENSDWLKHIRSIMEAGIFISKAVADEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYRTIKGMMVLIEKDWVSFG 378
Cdd:cd14593  86 KWLSSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVASLVQVMLDPYFRTITGFQSLIQKEWVMAG 165
                        90       100       110
                ....*....|....*....|....*....|
gi 94536956 379 HKFSHRCGHLDGEAKEVSPVLDQFLECVWQ 408
Cdd:cd14593 166 YRFLDRCNHLKKSSKKESPLFLLFLDCVWQ 195
PH-GRAM_MTMR9 cd13211
Myotubularian (MTM) related 9 protein (MTMR9) Pleckstrin Homology-Glucosyltransferases, ...
1-97 4.85e-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: 71.15  E-value: 4.85e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956   1 MEHIRMPKVENVRLVDRSssRKSQVGTLYLTATHTIFVGKgSEDRNELWVLHSLVCNIVKH--KASQSGYpLLIHCKNFQ 78
Cdd:cd13211   4 AELIKTPKVDNVVLHRPP--RPAVEGTLCITGHHLILSSR-QDNAEELWLLHSNIDSVEKKfvGKSSGGT-LTLKCKDFR 79
                        90
                ....*....|....*....
gi 94536956  79 VIQFIILQESDLHNVYISL 97
Cdd:cd13211  80 IIQLDIPDMEECLNIASSI 98
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
26-91 3.74e-08

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: 51.23  E-value: 3.74e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94536956  26 GTLYLTATHTIFVGKGSEDRNELWVLHSLVCNIVKHK-ASQSGYPLLIHCKNFQVIQFIILQESDLH 91
Cdd:cd10570  21 GTLYLSTYRLIFSSKADGDETKLVIPLVDITDVEKIAgASFLPSGLIITCKDFRTIKFSFDSEDEAV 87
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
310-428 3.76e-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: 43.12  E-value: 3.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956    310 LKHIRSIMEagifiSKAVADEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYRTIKgmmvliekdwvsfghkfshrcghld 389
Cdd:smart00012  23 LELLRAVKK-----NLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE------------------------- 72
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 94536956    390 geakevspvlDQFLECVWQLMDQFPCAFEYNEKFLISIH 428
Cdd:smart00012  73 ----------VDIFDTVKELRSQRPGMVQTEEQYLFLYR 101
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
310-428 3.76e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 43.12  E-value: 3.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94536956    310 LKHIRSIMEagifiSKAVADEGVSVLVHCSDGWDRTSQVCSVASVLLDPYYRTIKgmmvliekdwvsfghkfshrcghld 389
Cdd:smart00404  23 LELLRAVKK-----NLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE------------------------- 72
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 94536956    390 geakevspvlDQFLECVWQLMDQFPCAFEYNEKFLISIH 428
Cdd:smart00404  73 ----------VDIFDTVKELRSQRPGMVQTEEQYLFLYR 101
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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