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Conserved domains on  [gi|2209674677|ref|NP_001389517|]
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myotubularin-related protein 4 isoform 1 [Mus musculus]

Protein Classification

PH-GRAM_MTMR4 and PTP-MTMR4 domain-containing protein( domain architecture ID 12988771)

protein containing domains PH-GRAM_MTMR4, PTP-MTMR4, and FYVE_MTMR4

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
172-479 0e+00

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: 711.42  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  172 NVWRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYL 251
Cdd:cd14587      1 NVWRVSEINSNYKLCSSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAVIARCSQPEISWWGWRNADDEYL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  252 VTSIAKACALDPGTRASGGSLSTGTNDASEACDTDFDSSLTACSGVESTAAPQKLLILDARSYTAAVANRAKGGGCECEE 331
Cdd:cd14587     81 VTSIAKACALDPGTRAPGGSPSKGNSDGSDASDTDFDSSLTACSAVESGAAPQKLLILDARSYTAAVANRAKGGGCECEE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  332 YYPNCEVLFMGMANIHAIRNSFQYLRAVCSQMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGW 411
Cdd:cd14587    161 YYPNCEVMFMGMANIHSIRNSFQYLRAVCSQMPDPGNWLSALESTKWLQHLSVMLKAAVLVASAVDREGRPVLVHCSDGW 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2209674677  412 DRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENAEDQNEQCPVFLQWLDSVHQ 479
Cdd:cd14587    241 DRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHQENVEDQNEQCPVFLQWLDCVHQ 308
PH-GRAM_MTMR4 cd13342
Myotubularian (MTM) related 4 protein (MTMR4) Pleckstrin Homology-Glucosyltransferases, ...
23-136 3.63e-78

Myotubularian (MTM) related 4 protein (MTMR4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR4 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR4 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The protein form heteromers with MTMR3. Both MTMR3 and MTMR4 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal lipid-binding FYVE domain which binds phosphotidylinositol-3-phosphate. 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: 270150  Cd Length: 114  Bit Score: 252.21  E-value: 3.63e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677   23 LVKEEENLQVPFTVLQGEGVEFLGRATDALIAISNYRLHIKFKDSVINVPLRMIDSVESRDMFQLHIACKDSKVVRCHFS 102
Cdd:cd13342      1 LVKEEESLQVPFPVLQGEGVEYLGHANDAVIAISNYRLHIKFKDSVINVPLRMMESVESRDMFQLHIICKDSKVVRCHFS 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2209674677  103 TFKQCQEWLSRLSRATARPAKPEDLFAFAYHAWC 136
Cdd:cd13342     81 TFKQCQEWLKRLNRATARPAKPEDLFAFAYHAWC 114
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
1106-1165 1.10e-38

FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.


:

Pssm-ID: 277272 [Multi-domain]  Cd Length: 60  Bit Score: 137.95  E-value: 1.10e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd15733      1 WVPDHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQLYDPVRVCNSCY 60
 
Name Accession Description Interval E-value
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
172-479 0e+00

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: 711.42  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  172 NVWRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYL 251
Cdd:cd14587      1 NVWRVSEINSNYKLCSSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAVIARCSQPEISWWGWRNADDEYL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  252 VTSIAKACALDPGTRASGGSLSTGTNDASEACDTDFDSSLTACSGVESTAAPQKLLILDARSYTAAVANRAKGGGCECEE 331
Cdd:cd14587     81 VTSIAKACALDPGTRAPGGSPSKGNSDGSDASDTDFDSSLTACSAVESGAAPQKLLILDARSYTAAVANRAKGGGCECEE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  332 YYPNCEVLFMGMANIHAIRNSFQYLRAVCSQMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGW 411
Cdd:cd14587    161 YYPNCEVMFMGMANIHSIRNSFQYLRAVCSQMPDPGNWLSALESTKWLQHLSVMLKAAVLVASAVDREGRPVLVHCSDGW 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2209674677  412 DRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENAEDQNEQCPVFLQWLDSVHQ 479
Cdd:cd14587    241 DRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHQENVEDQNEQCPVFLQWLDCVHQ 308
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
160-518 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: 538.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  160 EAELARMGFDLQNVWRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPEIS 239
Cdd:pfam06602   11 EAEFARQGLPSKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVITRSSQPLVG 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  240 WWGWRNADDEYLVTSIAKACaldpgtrasggslstgtndaseacdtdfdssltacsgveSTAAPQKLLILDARSYTAAVA 319
Cdd:pfam06602   91 LNGKRSIEDEKLLQAIFKSS---------------------------------------NPYSAKKLYIVDARPKLNAMA 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  320 NRAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVCS-QMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDR 398
Cdd:pfam06602  132 NRAKGGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACNdRSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDL 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  399 EGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENAEDQNEQCPVFLQWLDSVH 478
Cdd:pfam06602  212 EGSSVLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGFTDSKERSPVFLQFLDCVW 291
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2209674677  479 QLLKQFPCLFEFNEAFLVKLVQHTYSCLYGTFLANNPCER 518
Cdd:pfam06602  292 QLLRQFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKER 331
PH-GRAM_MTMR4 cd13342
Myotubularian (MTM) related 4 protein (MTMR4) Pleckstrin Homology-Glucosyltransferases, ...
23-136 3.63e-78

Myotubularian (MTM) related 4 protein (MTMR4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR4 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR4 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The protein form heteromers with MTMR3. Both MTMR3 and MTMR4 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal lipid-binding FYVE domain which binds phosphotidylinositol-3-phosphate. 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: 270150  Cd Length: 114  Bit Score: 252.21  E-value: 3.63e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677   23 LVKEEENLQVPFTVLQGEGVEFLGRATDALIAISNYRLHIKFKDSVINVPLRMIDSVESRDMFQLHIACKDSKVVRCHFS 102
Cdd:cd13342      1 LVKEEESLQVPFPVLQGEGVEYLGHANDAVIAISNYRLHIKFKDSVINVPLRMMESVESRDMFQLHIICKDSKVVRCHFS 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2209674677  103 TFKQCQEWLSRLSRATARPAKPEDLFAFAYHAWC 136
Cdd:cd13342     81 TFKQCQEWLKRLNRATARPAKPEDLFAFAYHAWC 114
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
1106-1165 1.10e-38

FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.


Pssm-ID: 277272 [Multi-domain]  Cd Length: 60  Bit Score: 137.95  E-value: 1.10e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd15733      1 WVPDHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQLYDPVRVCNSCY 60
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
1104-1169 3.73e-28

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 108.29  E-value: 3.73e-28
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2209674677  1104 TRWVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCYEHIQ 1169
Cdd:smart00064    2 PHWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDCYENLN 67
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
1104-1169 2.93e-23

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 93.99  E-value: 2.93e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2209674677 1104 TRWVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYD-PVLVCNSCYEHIQ 1169
Cdd:pfam01363    1 PVWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLPELGSNkPVRVCDACYDTLQ 67
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
402-433 1.11e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 45.43  E-value: 1.11e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2209674677   402 PVLVHCSDGWDRTPQIVALAKILLDPYYRTLE 433
Cdd:smart00404   41 PVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE 72
 
Name Accession Description Interval E-value
PTP-MTMR4 cd14587
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
172-479 0e+00

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: 711.42  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  172 NVWRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYL 251
Cdd:cd14587      1 NVWRVSEINSNYKLCSSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAVIARCSQPEISWWGWRNADDEYL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  252 VTSIAKACALDPGTRASGGSLSTGTNDASEACDTDFDSSLTACSGVESTAAPQKLLILDARSYTAAVANRAKGGGCECEE 331
Cdd:cd14587     81 VTSIAKACALDPGTRAPGGSPSKGNSDGSDASDTDFDSSLTACSAVESGAAPQKLLILDARSYTAAVANRAKGGGCECEE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  332 YYPNCEVLFMGMANIHAIRNSFQYLRAVCSQMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGW 411
Cdd:cd14587    161 YYPNCEVMFMGMANIHSIRNSFQYLRAVCSQMPDPGNWLSALESTKWLQHLSVMLKAAVLVASAVDREGRPVLVHCSDGW 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2209674677  412 DRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENAEDQNEQCPVFLQWLDSVHQ 479
Cdd:cd14587    241 DRTPQIVALAKILLDPYYRTIEGFQVLVETDWLDFGHKFGDRCGHQENVEDQNEQCPVFLQWLDCVHQ 308
PTP-MTMR3 cd14586
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
167-479 0e+00

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: 577.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  167 GFDLQNVWRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPEISWWGWRNA 246
Cdd:cd14586      1 GFDMQNAWRISNINEKYKLCGSYPQELIVPAWITDKELESVASFRSWKRIPAVVYRHQSNGAVIARCGQPEVSWWGWRNA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  247 DDEYLVTSIAKACALDpgTRASGGSLSTGT-----NDASEACDTDFDSSLTACSGVESTA-APQKLLILDARSYTAAVAN 320
Cdd:cd14586     81 DDEHLVQSVAKACASD--SSSCKSVLMTGNcsrdfPNGGDLSDVEFDSSMSNASGVESLAiQPQKLLILDARSYAAAVAN 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  321 RAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVCSQMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDREG 400
Cdd:cd14586    159 RAKGGGCECPEYYPNCEVVFMGMANIHSIRKSFQSLRLLCTQMPDPANWLSALESTKWLQHLSMLLKSALLVVHAVDRDQ 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2209674677  401 RPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENAEDQNEQCPVFLQWLDSVHQ 479
Cdd:cd14586    239 RPVLVHCSDGWDRTPQIVALSKLLLDPYYRTIEGFQVLVETEWLDFGHKFADRCGHGENSDDLNERCPVFLQWLDCVHQ 317
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
160-518 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: 538.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  160 EAELARMGFDLQNVWRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPEIS 239
Cdd:pfam06602   11 EAEFARQGLPSKDEWRISDINKDYKVCPTYPALLVVPKSISDETLKKAAKFRSKGRIPVLSYRHKENGAVITRSSQPLVG 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  240 WWGWRNADDEYLVTSIAKACaldpgtrasggslstgtndaseacdtdfdssltacsgveSTAAPQKLLILDARSYTAAVA 319
Cdd:pfam06602   91 LNGKRSIEDEKLLQAIFKSS---------------------------------------NPYSAKKLYIVDARPKLNAMA 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  320 NRAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVCS-QMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDR 398
Cdd:pfam06602  132 NRAKGGGYENEDNYPNCKKIFLGIENIHVMRDSLNKLVEACNdRSPSMDKWLSRLESSGWLKHIKAILDGACLIAQAVDL 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  399 EGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENAEDQNEQCPVFLQWLDSVH 478
Cdd:pfam06602  212 EGSSVLVHCSDGWDRTAQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFADRCGHLAGFTDSKERSPVFLQFLDCVW 291
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2209674677  479 QLLKQFPCLFEFNEAFLVKLVQHTYSCLYGTFLANNPCER 518
Cdd:pfam06602  292 QLLRQFPCAFEFNERFLIRLLYHLYSCQFGTFLCNSEKER 331
PTP-MTMR3-like cd14533
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
213-479 5.21e-151

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: 451.47  E-value: 5.21e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  213 WKRIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYLVTSIAKACAldpgtrasggslstgtndaseacdtdfdsslt 292
Cdd:cd14533      1 SKRIPSVVWRHQRNGAVIARCSQPEVGWLGWRNAEDENLLQAIAEACA-------------------------------- 48
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  293 acsgveSTAAPQKLLILDARSYTAAVANRAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVCSQMPDPSNWLSA 372
Cdd:cd14533     49 ------SNASPKKLLIVDARSYAAAVANRAKGGGCECPEYYPNCEVVFMNLANIHAIRKSFHSLRALCSSAPDQPNWLSN 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  373 LESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGD 452
Cdd:cd14533    123 LESTKWLHHLSGLLKAALLVVNAVDEEGRPVLVHCSDGWDRTPQIVALAELMLDPYYRTIEGFQVLVEREWLDFGHKFAD 202
                          250       260
                   ....*....|....*....|....*..
gi 2209674677  453 RCGHQENAEDQNEQCPVFLQWLDSVHQ 479
Cdd:cd14533    203 RCGHGVNSEDINERCPVFLQWLDCVHQ 229
PTP-MTM-like cd14507
protein tyrosine phosphatase-like domain of myotubularins; Myotubularins are a unique subgroup ...
214-479 4.16e-118

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: 364.95  E-value: 4.16e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  214 KRIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYLVTSIAKACAldpgtrasggslstgtndaseacdtdfdsslta 293
Cdd:cd14507      1 GRIPVLSWRHPRNGAVICRSSQPLVGLTGSRSKEDEKLLNAIRKASP--------------------------------- 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  294 csgvestaAPQKLLILDARSYTAAVANRAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVCSQMPDP-SNWLSA 372
Cdd:cd14507     48 --------SSKKLYIVDARPKLNAVANRAKGGGYENTEYYPNCELEFLNIENIHAMRDSLNKLRDACLSPNDEeSNWLSA 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  373 LESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGD 452
Cdd:cd14507    120 LESSGWLEHIRLILKGAVRVADLLEKEGTSVLVHCSDGWDRTSQLTSLAQLLLDPYYRTIEGFQVLIEKEWLSFGHKFAD 199
                          250       260
                   ....*....|....*....|....*..
gi 2209674677  453 RCGHQENAEDQNEQCPVFLQWLDSVHQ 479
Cdd:cd14507    200 RCGHGDKNSSDEERSPIFLQFLDCVWQ 226
PTP-MTMR6-like cd14532
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases ...
160-504 1.32e-107

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: 339.70  E-value: 1.32e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  160 EAELARMGFDLQNvWRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPeIS 239
Cdd:cd14532      2 ESEYTRMGVPNDN-WTLSDINKDYELCDTYPRELFVPTSASTPVLVGSSKFRSKGRLPVLSYLHKDNQAAICRCSQP-LS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  240 WWGWRNADDEYLVTSIAKAcalDPGTRAsggslstgtndaseacdtdfdssltacsgvestaapqkLLILDARSYTAAVA 319
Cdd:cd14532     80 GFSARCVEDEQLLQAIRKA---NPNSKF--------------------------------------MYVVDTRPKINAMA 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  320 NRAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVCSQM-PDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDr 398
Cdd:cd14532    119 NKAAGKGYENEDNYSNIKFQFFGIENIHVMRSSLQKLLEVCELKnPSMSAFLSGLESSGWLKHIKAVMDTSVFIAKAVS- 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  399 EGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENaeDQNEQCPVFLQWLDSVH 478
Cdd:cd14532    198 EGASVLVHCSDGWDRTAQTCSLASLLLDPYYRTIKGFQVLIEKEWLSFGHKFTDRCGHLQG--DAKEVSPVFTQFLDCVW 275
                          330       340
                   ....*....|....*....|....*.
gi 2209674677  479 QLLKQFPCLFEFNEAFLVKLVQHTYS 504
Cdd:cd14532    276 QLMQQFPRAFEFNERFLLTLHDHVYS 301
PTP-MTM1-like cd14535
protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related ...
215-503 4.13e-86

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: 279.33  E-value: 4.13e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  215 RIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYLVTSIakacaldpgtrasggslstgtndaseacdtdfdssltac 294
Cdd:cd14535      2 RIPVLSWIHPESQATITRCSQPLVGVSGKRSKDDEKYLQLI--------------------------------------- 42
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  295 sgVESTAAPQKLLILDARSYTAAVANRAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVCSQMPDPSNWLSALE 374
Cdd:cd14535     43 --MDANAQSHKLFIMDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKDICFPNIDDSHWLSNLE 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  375 STKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRC 454
Cdd:cd14535    121 STHWLEHIKLILAGAVRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDPYYRTIRGFEVLIEKEWLSFGHKFAQRI 200
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2209674677  455 GHQENAEDQNEQCPVFLQWLDSVHQLLKQFPCLFEFNEAFLVKLVQHTY 503
Cdd:cd14535    201 GHGDKNHSDADRSPVFLQFIDCVWQMTRQFPNAFEFNEHFLITILDHLY 249
PTP-MTMR8 cd14584
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
160-504 2.30e-85

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: 279.84  E-value: 2.30e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  160 EAELARMGFDLQNvWRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPeIS 239
Cdd:cd14584      8 KVDFQRMGIPNDY-WEITDANKNYEICSTYPPELVVPKSASKATVVGSSKFRSRGRFPVLSYLYKENNAAICRCSQP-LS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  240 WWGWRNADDEYLVTSIAKAcalDPGTrasggslstgtndaseacdtdfdssltacsgvestaapQKLLILDARSYTAAVA 319
Cdd:cd14584     86 GFSARCVEDEQMLQAISKA---NPGS--------------------------------------PFMYVVDTRPKLNAMA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  320 NRAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVCS-QMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDR 398
Cdd:cd14584    125 NRAAGKGYENEDNYSNIRFQFIGIENIHVMRSSLQKLLEVCEmKSPSMSDFLTGLENSGWLRHIKAVMDAGVFLAKAVKE 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  399 EGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENaeDQNEQCPVFLQWLDSVH 478
Cdd:cd14584    205 EKASVLVHCSDGWDRTAQVCSLASLLLDPFYRTIKGLMVLIEKEWISMGHKFSQRCGHLDG--DPKEVSPVFTQFLECVW 282
                          330       340
                   ....*....|....*....|....*.
gi 2209674677  479 QLLKQFPCLFEFNEAFLVKLVQHTYS 504
Cdd:cd14584    283 QLMEQFPCAFEFNEHFLLEIHDHVFS 308
PTP-MTMR7 cd14583
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
160-504 6.17e-84

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: 275.69  E-value: 6.17e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  160 EAELARMGFdLQNVWRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPeIS 239
Cdd:cd14583      2 KAEYNRMGL-PNSLWQVSDVNRDYRVCDTYPTELYVPKSATAPIIVGSSKFRSRGRFPVLSYYCKDNNASICRSSQP-LS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  240 WWGWRNADDEYLVTSIAKAcalDPGTrasggslstgtndaseacdtDFdssltacsgvestaapqkLLILDARSYTAAVA 319
Cdd:cd14583     80 GFSARCLEDEQMLQAIRKA---NPGS--------------------DF------------------MYVVDTRPKLNAMA 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  320 NRAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVCS-QMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDR 398
Cdd:cd14583    119 NRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCElRSPSMGDFLWGLENSGWLKHIKAIMDAGIFIAKAVAE 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  399 EGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENaeDQNEQCPVFLQWLDSVH 478
Cdd:cd14583    199 EGASVLVHCSDGWDRTAQVCSVASLLLDPYYRTIKGFMVLIEKDWVSFGHKFNHRYGHLDG--DPKEVSPVIDQFIECVW 276
                          330       340
                   ....*....|....*....|....*.
gi 2209674677  479 QLLKQFPCLFEFNEAFLVKLVQHTYS 504
Cdd:cd14583    277 QLMEQFPCAFEFNERFLIHIHHHIYS 302
PTP-MTMR6 cd14585
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
161-504 4.83e-83

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: 272.96  E-value: 4.83e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  161 AELARMGFDlQNVWRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPeISW 240
Cdd:cd14585      3 EEYKRMGVP-NDYWQLSDVNRDYKICDTYPRDLYVPITASKPIIVGSSKFRSKGRFPVLSYYHQEKKAAICRCSQP-LSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  241 WGWRNADDEYLVTSIAKAcalDPGTRasggslstgtndaseacdtdfdssltacsgvestaapqKLLILDARSYTAAVAN 320
Cdd:cd14585     81 FSARCLEDEHMLQAISKA---NPNNR--------------------------------------YMYVMDTRPKLNAMAN 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  321 RAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVC-SQMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDRE 399
Cdd:cd14585    120 RAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVCgTKALSVNDFLSGLESSGWLRHIKAVLDAAVFLAKAVAVE 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  400 GRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENaeDQNEQCPVFLQWLDSVHQ 479
Cdd:cd14585    200 GASVLVHCSDGWDRTAQVCSLGSLLLDPYYRTIKGFMVLIEKDWISFGHKFSDRCGQLDG--DPKEISPVFTQFLECVWQ 277
                          330       340
                   ....*....|....*....|....*
gi 2209674677  480 LLKQFPCLFEFNEAFLVKLVQHTYS 504
Cdd:cd14585    278 LTEQFPRAFEFSEAFLLQIHEHIHS 302
PTP-MTMR2 cd14590
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
201-503 7.38e-83

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: 271.14  E-value: 7.38e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  201 DKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYLVTSIakacaldpgtrasggslstgtndas 280
Cdd:cd14590      1 DEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAI------------------------- 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  281 eacdtdfdssltacsgVESTAAPQKLLILDARSYTAAVANRAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVC 360
Cdd:cd14590     56 ----------------MDSNAQSHKIFIFDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIV 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  361 SQMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVE 440
Cdd:cd14590    120 YPNIEESHWLSNLESTHWLEHIKLILAGALRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVE 199
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2209674677  441 SDWLDFGHKFGDRCGHQENAEDQNEQCPVFLQWLDSVHQLLKQFPCLFEFNEAFLVKLVQHTY 503
Cdd:cd14590    200 KEWLSFGHRFQLRVGHGDKNHADADRSPVFLQFIDCVWQMTRQFPTAFEFNEYFLITILDHLY 262
PTP-MTM1 cd14591
protein tyrosine phosphatase-like domain of myotubularin phosphoinositide phosphatase 1; ...
215-503 9.84e-79

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: 259.19  E-value: 9.84e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  215 RIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYLVTSIAkacaldpgtrasggslstgtndaseacdtdfdssltac 294
Cdd:cd14591      2 RIPVLSWIHPENQAVIMRCSQPLVGMSGKRNKDDEKYLDIIR-------------------------------------- 43
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  295 sgvESTAAPQKLLILDARSYTAAVANRAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVCSQMPDPSNWLSALE 374
Cdd:cd14591     44 ---EANGQTSKLTIYDARPSVNAVANKATGGGYEGDDAYQNAELVFLDIHNIHVMRESLKKLKDIVYPNVEESHWLSSLE 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  375 STKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRC 454
Cdd:cd14591    121 STHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSYYRTIEGFEVLVQKEWISFGHKFASRI 200
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2209674677  455 GHQENAEDQNEQCPVFLQWLDSVHQLLKQFPCLFEFNEAFLVKLVQHTY 503
Cdd:cd14591    201 GHGDKNHADADRSPIFLQFIDCVWQMSKQFPTAFEFNEQFLITILDHLY 249
PH-GRAM_MTMR4 cd13342
Myotubularian (MTM) related 4 protein (MTMR4) Pleckstrin Homology-Glucosyltransferases, ...
23-136 3.63e-78

Myotubularian (MTM) related 4 protein (MTMR4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR4 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR4 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The protein form heteromers with MTMR3. Both MTMR3 and MTMR4 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal lipid-binding FYVE domain which binds phosphotidylinositol-3-phosphate. 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: 270150  Cd Length: 114  Bit Score: 252.21  E-value: 3.63e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677   23 LVKEEENLQVPFTVLQGEGVEFLGRATDALIAISNYRLHIKFKDSVINVPLRMIDSVESRDMFQLHIACKDSKVVRCHFS 102
Cdd:cd13342      1 LVKEEESLQVPFPVLQGEGVEYLGHANDAVIAISNYRLHIKFKDSVINVPLRMMESVESRDMFQLHIICKDSKVVRCHFS 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2209674677  103 TFKQCQEWLSRLSRATARPAKPEDLFAFAYHAWC 136
Cdd:cd13342     81 TFKQCQEWLKRLNRATARPAKPEDLFAFAYHAWC 114
PTP-MTMR1 cd14592
protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase ...
215-503 2.80e-70

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: 235.26  E-value: 2.80e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  215 RIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYLVTSIakacaldpgtrasggslstgtndaseacdtdfdssltac 294
Cdd:cd14592      2 RVPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYLQTI--------------------------------------- 42
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  295 sgVESTAAPQKLLILDARSYTAAVANRAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVCSQMPDPSNWLSALE 374
Cdd:cd14592     43 --MDANAQSHKLIIFDARQNSVADTNKTKGGGYESESAYPNAELVFLEIHNIHVMRESLRKLKEIVYPSIDEARWLSNVD 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  375 STKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRC 454
Cdd:cd14592    121 GTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGWDRTAQLTSLAMLMLDSYYRTIKGFEVLIEKEWISFGHRFALRV 200
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2209674677  455 GHQENAEDQNEQCPVFLQWLDSVHQLLKQFPCLFEFNEAFLVKLVQHTY 503
Cdd:cd14592    201 GHGDDNHADADRSPIFLQFIDCVWQMTRQFPSAFEFNELFLITILDHLY 249
PTP-MTM-like_fungal cd17666
protein tyrosine phosphatase-like domain of fungal myotubularins; Myotubularins are a unique ...
214-479 8.13e-68

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: 227.71  E-value: 8.13e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  214 KRIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYLVTSIakacaldpgtrasggslstgtndaseacdtdFDSSLTA 293
Cdd:cd17666      1 QRIPVLTYLHKANGCSITRSSQPLVGLKQNRSIQDEKLVSEI-------------------------------FNTSINE 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  294 CSGvestaAPQKLLILDARSYTAAVANRAKGGGCECEE--YYPNCEVLFMGMANIHAIRNSFQYLRAVC-----SQMPDP 366
Cdd:cd17666     50 IYI-----SPQKNLIVDARPTTNAMAQVALGAGTENMDnyKYKTAKKIYLGIDNIHVMRDSLNKVTEALkdgddSNPSYP 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  367 SNwLSALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDF 446
Cdd:cd17666    125 PL-INALKKSNWLKYLAIILQGADLIAKSIHFNHSHVLIHCSDGWDRTSQLSALAQLCLDPYYRTLEGFMVLVEKDWLSF 203
                          250       260       270
                   ....*....|....*....|....*....|...
gi 2209674677  447 GHKFGDRCGHQENAedqneqcPVFLQWLDSVHQ 479
Cdd:cd17666    204 GHRFAERSGHKETS-------PVFHQFLDCVYQ 229
PH-GRAM_MTMR3_MTMR4 cd13209
Myotubularian (MTM) related 3 and 4 proteins (MTMR3 and MTMR4) Pleckstrin ...
23-116 1.71e-59

Myotubularian (MTM) related 3 and 4 proteins (MTMR3 and MTMR4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR3 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR3 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The protein can self-associate and also form heteromers with MTMR4. MTMR4, a member of the myotubularin dual specificity protein phosphatase gene family. MTMR4 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The protein form heteromers with MTMR3. Both MTMR3 and MTMR4 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal lipid-binding FYVE domain which binds phosphotidylinositol-3-phosphate. 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: 275397  Cd Length: 94  Bit Score: 198.52  E-value: 1.71e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677   23 LVKEEENLQVPFTVLQGEGVEFLGRATDALIAISNYRLHIKFKDSVINVPLRMIDSVESRDMFQLHIACKDSKVVRCHFS 102
Cdd:cd13209      1 LVKEDENLQVPFPELHGEGTEYVGRAEDAVIAISNYRLHIKFKESVINVPLQLIESVECRDMFQLHITCKDCKVIRCQFS 80
                           90
                   ....*....|....
gi 2209674677  103 TFKQCQEWLSRLSR 116
Cdd:cd13209     81 TFEQCQEWLKRLNR 94
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
174-483 7.14e-54

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: 189.50  E-value: 7.14e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  174 WRVSHINSNYKLCPSYPQKLLVPVWITDKELENVA-SFRSwKRIPVVVYRHLRNGAAIARCSQPEiswwgwrnaddeylV 252
Cdd:cd14534      1 FRISTANRDYSICRSYPALVVVPQSVSDESLRKVArCYRQ-GRFPVVTWRHPRTKALLLRSGGFH--------------G 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  253 TSIAkacaldpGTRASGGSLSTGTNDASeacdTDFDSSLTAcsgvESTAAPQKLLILDARSYTAAVANrakgggceceEY 332
Cdd:cd14534     66 KGVM-------GMLKSANTSTSSPTVSS----SETSSSLEQ----EKYLSALVLYVLGEKSQMKGVKA----------ES 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  333 YPNCEVLFMGMANIHAIRNSFQYLRAVC----SQMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCS 408
Cdd:cd14534    121 DPKCEFIPVEYPEVRQVKASFKKLLRACvpssAPTEPEQSFLKAVEDSEWLQQLQCLMQLSGAVVDLLDVQGSSVLLCLE 200
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2209674677  409 DGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENAEDQNeQCPVFLQWLDSVHQLLKQ 483
Cdd:cd14534    201 DGWDVTTQVSSLSQLLLDPYYRTLEGFRVLVEKEWLAFGHRFSHRSNLTAASQSSG-FAPVFLQFLDAVHQIHRQ 274
PTP-MTMR9 cd14536
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
215-479 6.41e-49

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: 173.29  E-value: 6.41e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  215 RIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYLVTSiakacALDPGTRAsggslstgtndaseacdtdfdssltac 294
Cdd:cd14536      2 RFPVLSYYHKKNGMVLMRSSQPLTGPNGKRCKEDEKLLNA-----VLGGGKRG--------------------------- 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  295 sgvestaapqklLILDARSYTAAVANRAKGGGCECEEYYPNCEVLFMGMANIHAIRNSFQYLRAVCSqmpDPS----NWL 370
Cdd:cd14536     50 ------------YIIDTRSKNVAQQARAKGGGFEPEAHYPQWRRIHKPIERYNVLQESLIKLVEACN---DQGhsmdKWL 114
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  371 SALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKF 450
Cdd:cd14536    115 SKLESSNWLSHVKEILTTACLVAQCIDREGASVLVHGSEGMDSTLQVTSLAQIILDPDCRTIRGFEALIEREWLQAGHPF 194
                          250       260       270
                   ....*....|....*....|....*....|
gi 2209674677  451 GDRCGHQENAEDQN-EQCPVFLQWLDSVHQ 479
Cdd:cd14536    195 QSRCAKSAYSNSKQkFESPVFLLFLDCVWQ 224
PH-GRAM_MTMR3 cd13341
Myotubularian (MTM) related 3 protein (MTMR3) Pleckstrin Homology-Glucosyltransferases, ...
23-115 1.21e-46

Myotubularian (MTM) related 3 protein (MTMR3) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR3 is a member of the myotubularin dual specificity protein phosphatase gene family. MTMR3 binds to phosphoinositide lipids through its PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The protein can self-associate and also form heteromers with MTMR4. Both MTMR3 and MTMR4 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain, a coiled-coil region, and a C-terminal lipid-binding FYVE domain which binds phosphotidylinositol-3-phosphate. 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: 270149  Cd Length: 94  Bit Score: 161.71  E-value: 1.21e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677   23 LVKEEENLQVPFTVLQGEGVEFLGRATDALIAISNYRLHIKFKDSVINVPLRMIDSVESRDMFQLHIACKDSKVVRCHFS 102
Cdd:cd13341      1 LIREDENLQVPFQELHGESTEFVGRAEDAIIALSNYRLHIKFKESVVNVPLQLIESVECRDIFQLHLTCKDCKVIRCQFS 80
                           90
                   ....*....|...
gi 2209674677  103 TFKQCQEWLSRLS 115
Cdd:cd13341     81 TFEQCQEWLKRLN 93
PTP-MTMR13 cd14589
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
174-483 5.38e-40

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: 150.46  E-value: 5.38e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  174 WRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSqpeiswwGWRNADdeylVT 253
Cdd:cd14589      1 FRITAVNRMYSLCRSYPGLLVVPQSVQDSSLQKVARCYRHNRLPVVCWKNSKTKAVLLRSG-------GFHGKG----VV 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  254 SIAKAcaLDPGTRASGGSLSTGTNDASEACDTDFDSSLTACS-GVESTAAPQKLLILDARSYTAAVANRAKGGGCEceeY 332
Cdd:cd14589     70 GLFKS--QNPHSAAPASSESSSSIEQEKYLQALLNAISVHQKmNGNSTLLQSQLLKRQAALYIFGEKSQLRGFKLD---F 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  333 YPNCEVLFMGMANIHAIRNSFQYLRAVC--SQMP-DP-SNWLSALESTKWLQHLSVMLKAAVLVANTVDrEGRPVLVHCS 408
Cdd:cd14589    145 ALNCEFVPVEFHDIRQVKASFKKLMRACvpSTIPtDSeVTFLKALGESEWFLQLHRIMQLAVVISELLE-SGSSVMVCLE 223
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2209674677  409 DGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENAEDQNeQCPVFLQWLDSVHQLLKQ 483
Cdd:cd14589    224 DGWDITTQVVSLVQLLSDPFYRTLEGFQMLVEKEWLSFGHKFSQRSNLTPNSQGSG-FAPIFLQFLDCVHQIHNQ 297
PTP-MTMR5 cd14588
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
174-483 7.26e-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: 149.73  E-value: 7.26e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  174 WRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSqpeiswwGWRNADdeylVT 253
Cdd:cd14588      1 FRISTVNRMYAVCRSYPGLLIVPQSIQDNTIQRISRCYRQNRFPVVCWRNSRTKAVLLRSG-------GLHGKG----VV 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  254 SIAKAcaldPGTRASGGSLSTGTNDASEACDTDFDSSLTACSgveSTAAPQKLLILDARSYTAAVANRAKGGGCECEEYY 333
Cdd:cd14588     70 GLFKS----QNAPAAGQSQTDSTSLEQEKYLQAVINSMPRYA---DASGRNTLSGFRAALYIIGDKSQLKGVKQDPLQQW 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  334 pncEVLFMGMANIHAIRNSFQYLRAVC----SQMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDrEGRPVLVHCSD 409
Cdd:cd14588    143 ---EVVPIEVFDVRQVKASFKKLMKACvpscPSTDPSQTYLRTLEESEWLSQLHKLLQVSVLVVELLD-SGSSVLVSLED 218
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2209674677  410 GWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRcGHQENAEDQNEQCPVFLQWLDSVHQLLKQ 483
Cdd:cd14588    219 GWDITTQVVSLVQLLSDPYYRTIEGFRLLVEKEWLSFGHRFSHR-GAQTLASQSSGFTPVFLQFLDCVHQIHLQ 291
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
1106-1165 1.10e-38

FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.


Pssm-ID: 277272 [Multi-domain]  Cd Length: 60  Bit Score: 137.95  E-value: 1.10e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd15733      1 WVPDHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQLYDPVRVCNSCY 60
PTP-MTMR10-like cd14537
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
344-479 1.19e-31

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: 122.84  E-value: 1.19e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  344 ANIHAirnSFQYLRAVCsqMPDP--------SNWLSALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTP 415
Cdd:cd14537     62 QDVQA---AYLKLRELC--TPDSseqfwvqdSKWYSLLENTKWLHYVSACLKKASEAAEALESRGRSVVLQESDGRDLSC 136
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2209674677  416 QIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENAEDQNEQCPVFLQWLDSVHQ 479
Cdd:cd14537    137 VVSSLVQLLLDPHFRTITGFQSLIQKEWVALGHPFCDRLGHVKPNKTESEESPVFLLFLDCVWQ 200
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
1104-1169 3.73e-28

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 108.29  E-value: 3.73e-28
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2209674677  1104 TRWVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCYEHIQ 1169
Cdd:smart00064    2 PHWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDCYENLN 67
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
1105-1165 1.56e-26

FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides.


Pssm-ID: 277271 [Multi-domain]  Cd Length: 61  Bit Score: 103.44  E-value: 1.56e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2209674677 1105 RWVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd15732      1 RWVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQLFEPSRVCKSCF 61
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
1104-1169 2.93e-23

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 93.99  E-value: 2.93e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2209674677 1104 TRWVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYD-PVLVCNSCYEHIQ 1169
Cdd:pfam01363    1 PVWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLPELGSNkPVRVCDACYDTLQ 67
PTP-MTMR10 cd14593
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
343-479 4.18e-23

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: 98.04  E-value: 4.18e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  343 MANIHAIRNSFQYLRAVCSQMP---DPSNWLSALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVA 419
Cdd:cd14593     58 LPNIQEIQAAFVKLKQLCVNEPfeeTEEKWLSSLESTRWLEYVRAFLKHSAELVYMLESKHVSVILQEEEGRDLSCVVAS 137
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  420 LAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENAEDQneQCPVFLQWLDSVHQ 479
Cdd:cd14593    138 LVQVMLDPYFRTITGFQSLIQKEWVMAGYRFLDRCNHLKKSSKK--ESPLFLLFLDCVWQ 195
PTP-MTMR12 cd14594
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
369-480 7.96e-21

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: 91.83  E-value: 7.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  369 WLSALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGH 448
Cdd:cd14594     94 WFSSLESSNWLEIIRQCLKKAVEVVECLEKQNTNVLLTEEEATDLCCVISSLVQIMMDPYCRTKSGFQSLIQKEWVMGGH 173
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2209674677  449 KFGDRCGHQEnaEDQNEQCPVFLQWLDSVHQL 480
Cdd:cd14594    174 CFLDRCNHLR--QNDKEEVPVFLLFLDCVWQL 203
PTP-MTMR11 cd14595
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
349-480 2.15e-20

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: 90.28  E-value: 2.15e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677  349 IRNSFQYLRAVCsqMPDPS------NWLSALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAK 422
Cdd:cd14595     62 IQLAYLKLRTLC--LPDISvsvsdeKWLSNLEGTRWLDHVRACLRKASEVSCLLAERHRSVILQESEDRDLNCLLSSLVQ 139
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2209674677  423 ILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCG-HQENAEdqnEQCPVFLQWLDSVHQL 480
Cdd:cd14595    140 LLSDPHARTISGFQSLVQKEWVVAGHPFLQRLNlTRESDK---EESPVFLLFLDCVWQL 195
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
1105-1165 2.26e-20

FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; Lst2, also termed zinc finger FYVE domain-containing protein 28, is a monoubiquitinylated phosphoprotein that functions as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Unlike other FYVE domain-containing proteins, Lst2 displays primarily non-endosomal localization. Its endosomal localization is regulated by monoubiquitinylation. Lst2 physically binds Trim3, also known as BERP or RNF22, which is a coordinator of endosomal trafficking and interacts with Hrs and a complex that biases cargo recycling.


Pssm-ID: 277270 [Multi-domain]  Cd Length: 65  Bit Score: 85.86  E-value: 2.26e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2209674677 1105 RWVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd15731      4 LWVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGQMKPVRVCNHCF 64
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
1106-1166 1.84e-19

FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ZF21 is phosphoinositide-binding protein that functions as a regulator of focal adhesions and cell movement through interaction with focal adhesion kinase. It can also bind to the cytoplasmic tail of membrane type 1 matrix metalloproteinase, a potent invasion-promoting protease, and play a key role in regulating multiple aspects of cancer cell migration and invasion. ZF21 contains a FYVE domain, which corresponds to this model.


Pssm-ID: 277266 [Multi-domain]  Cd Length: 64  Bit Score: 83.20  E-value: 1.84e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCYE 1166
Cdd:cd15727      4 WVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPRMCFVDPVRVCNECAL 64
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
1106-1168 2.67e-17

FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes.


Pssm-ID: 277268 [Multi-domain]  Cd Length: 68  Bit Score: 77.39  E-value: 2.67e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLK--LPIPDQQlydPVLVCNSCYEHI 1168
Cdd:cd15729      7 WVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCSLKarLEYLDNK---EARVCVPCYQTL 68
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
1106-1165 2.92e-16

FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins; WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain.


Pssm-ID: 277259 [Multi-domain]  Cd Length: 65  Bit Score: 74.34  E-value: 2.92e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd15719      3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRLRISRPVRVCQACY 62
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
1106-1165 3.41e-16

FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277261 [Multi-domain]  Cd Length: 58  Bit Score: 73.57  E-value: 3.41e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQlyDPVLVCNSCY 1165
Cdd:cd15721      1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSA--KPVRVCDTCY 58
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
1114-1165 4.96e-15

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.


Pssm-ID: 277249 [Multi-domain]  Cd Length: 52  Bit Score: 70.25  E-value: 4.96e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2209674677 1114 HCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd00065      1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGSGKPVRVCDSCY 52
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
1105-1165 2.46e-14

FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed endosome-associated protein p162, or zinc finger FYVE domain-containing protein 2, is an essential component of the endosomal fusion machinery and required for the fusion and maturation of early endosomes in endocytosis. It forms a parallel coiled-coil homodimer in cells. EEA1 serves as the p97 ATPase substrate and the p97 ATPase may regulate the size of early endosomes by governing the oligomeric state of EEA1. It can interact with the GTP-bound form of Rab22a and be involved in endosomal membrane trafficking. EEA1 also functions as an obligate scaffold for angiotensin II-induced Akt activation in early endosomes. It can be phosphorylated by p38 mitogen-activated protein kinase (MAPK) and further regulate mu opioid receptor endocytosis. EEA1 consists of an N-terminal C2H2 Zn2+ finger, four long heptad repeats, and a C-terminal region containing a calmodulin binding (IQ) motif, a Rab5 interaction site, and a FYVE domain. This model corresponds to the FYVE domain that is responsible for binding phosphatidyl inositol-3-phosphate (PtdIns3P or PI3P) on the membrane.


Pssm-ID: 277269 [Multi-domain]  Cd Length: 63  Bit Score: 68.58  E-value: 2.46e-14
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gi 2209674677 1105 RWVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQlyDPVLVCNSCY 1165
Cdd:cd15730      2 KWADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSK--KPVRVCDACF 60
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
1105-1165 8.67e-14

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and similar proteins; scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif.


Pssm-ID: 277299 [Multi-domain]  Cd Length: 59  Bit Score: 66.94  E-value: 8.67e-14
                           10        20        30        40        50        60
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gi 2209674677 1105 RWVPDhmaSHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQ-QLYDPVLVCNSCY 1165
Cdd:cd15760      1 HWKPD---SRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPLPHLgPLGVPQRVCDRCF 59
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
1106-1165 2.14e-13

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), and similar proteins; This family includes protein containing both PH and FYVE domains 1 (phafin-1) and 2 (phafin-2). Phafin-1 is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway. Phafin-2 is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277257 [Multi-domain]  Cd Length: 61  Bit Score: 65.85  E-value: 2.14e-13
                           10        20        30        40        50        60
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gi 2209674677 1106 WVPDHMASHCFNC-DCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQlYDPVLVCNSCY 1165
Cdd:cd15717      2 WVPDSEAPVCMHCkKTKFTAINRRHHCRKCGAVVCGACSSKKFLLPHQS-SKPLRVCDTCY 61
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
1106-1165 2.84e-13

FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277297 [Multi-domain]  Cd Length: 71  Bit Score: 65.86  E-value: 2.84e-13
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gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQlyDPVLVCNSCY 1165
Cdd:cd15758      6 WLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYP--KPVRVCDSCH 63
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
1106-1166 1.19e-12

FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate Epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human ether-a-go-go (hERG) channels. This family also includes the yeast and plant orthologs of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal lipid kinase domain related to PtdInsP kinases.


Pssm-ID: 277264 [Multi-domain]  Cd Length: 62  Bit Score: 63.88  E-value: 1.19e-12
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gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCYE 1166
Cdd:cd15725      2 WMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGDLRVCTYCCK 62
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
1106-1165 2.07e-12

FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins; ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop.


Pssm-ID: 277273 [Multi-domain]  Cd Length: 61  Bit Score: 63.12  E-value: 2.07e-12
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gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd15734      2 WVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRGWDHPVRVCDPCA 61
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
1106-1165 5.26e-12

FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions.


Pssm-ID: 277298 [Multi-domain]  Cd Length: 71  Bit Score: 62.35  E-value: 5.26e-12
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gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQlyDPVLVCNSCY 1165
Cdd:cd15759      4 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSP--KPVRVCDSCH 61
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
1115-1165 6.66e-12

FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins; spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs.


Pssm-ID: 277274 [Multi-domain]  Cd Length: 59  Bit Score: 61.78  E-value: 6.66e-12
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gi 2209674677 1115 CFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd15735      9 CMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQPVRVCDGCY 59
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
1115-1168 7.83e-12

FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.


Pssm-ID: 277260 [Multi-domain]  Cd Length: 61  Bit Score: 61.63  E-value: 7.83e-12
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gi 2209674677 1115 CFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCYEHI 1168
Cdd:cd15720      8 CHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKFGIEKEVRVCDPCYEKL 61
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
1106-1166 4.55e-11

FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins; Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277294 [Multi-domain]  Cd Length: 64  Bit Score: 59.28  E-value: 4.55e-11
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gi 2209674677 1106 WVPDHMASHCFNCD-CEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQlYDPVLVCNSCYE 1166
Cdd:cd15755      2 WVPDSEATVCMRCQkAKFTPVNRRHHCRKCGFVVCGPCSEKKFLLPSQS-SKPVRVCDFCYD 62
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
1106-1165 1.57e-10

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins; FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site.


Pssm-ID: 277282 [Multi-domain]  Cd Length: 61  Bit Score: 57.83  E-value: 1.57e-10
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gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIpDQQLYDPVLVCNSCY 1165
Cdd:cd15743      3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKAPL-EYLKNKSARVCDECF 61
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
1113-1166 1.77e-10

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.


Pssm-ID: 277267 [Multi-domain]  Cd Length: 63  Bit Score: 57.82  E-value: 1.77e-10
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gi 2209674677 1113 SHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCYE 1166
Cdd:cd15728      8 DYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFD 61
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
1106-1168 3.32e-09

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins; Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway.


Pssm-ID: 277293 [Multi-domain]  Cd Length: 64  Bit Score: 54.19  E-value: 3.32e-09
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gi 2209674677 1106 WVPDHMASHCFNC-DCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQlYDPVLVCNSCYEHI 1168
Cdd:cd15754      2 WIPDKATDICMRCtQTNFSLLTRRHHCRKCGFVVCHECSRQRFLIPRLS-PKPVRVCSLCYRKL 64
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
1106-1166 5.64e-09

FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody.


Pssm-ID: 277263 [Multi-domain]  Cd Length: 61  Bit Score: 53.29  E-value: 5.64e-09
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gi 2209674677 1106 WVPDHMASHCFNCDCE-FWLAKRRHHCRNCGNVFCAGCCHLKLPIpDQQLYDPVLVCNSCYE 1166
Cdd:cd15724      1 WVPDEAVSVCMVCQVErFSMFNRRHHCRRCGRVVCSSCSTKKMLV-EGYRENPVRVCDQCYE 61
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
1107-1169 6.50e-09

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar proteins; FGD5, also termed zinc finger FYVE domain-containing protein 23, is an endothelial cell (EC)-specific guanine nucleotide exchange factor (GEF) that regulates endothelial adhesion, survival, and angiogenesis by modulating phosphatidylinositol 3-kinase signaling. It functions as a novel genetic regulator of vascular pruning by activation of endothelial cell-targeted apoptosis. FGD5 is a homologue of FGD1 and contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. The FYVE domain of FGD5 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277281 [Multi-domain]  Cd Length: 67  Bit Score: 53.40  E-value: 6.50e-09
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gi 2209674677 1107 VPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIpdQQLYD-PVLVCNSCYEHIQ 1169
Cdd:cd15742      4 VPVSHVMMCMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYPL--KYLKDrPAKVCDGCFAELR 65
FYVE_protrudin cd15723
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ...
1115-1168 1.39e-08

FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc finger FYVE domain-containing protein 27 (ZFY27 or ZFYVE27), is a FYVE domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia (HSP). It is involved in neurite outgrowth through binding to spastin. Moreover, it functions as a key regulator of the Rab11-dependent membrane trafficking during neurite extension. It serves as an adaptor molecule that links its associated proteins, such as Rab11-GDP, VAP-A and -B, Surf4, and RTN3, to KIF5, a motor protein that mediates anterograde vesicular transport in neurons, and thus plays a key role in the maintenance of neuronal function. The FYVE domain of protrudin resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. In addition, unlike canonical FYVE domains that is located to early endosomes and specifically binds to phosphatidylinositol 3-phosphate (PtdIns3P or PI3P), the FYVE domain of protrudin is located to plasma membrane and preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). In addition to FYVE-related domain, protrudin also contains a Rab11-binding domain (RBD11), two hydrophobic domains, HP-1 and HP-2, an FFAT motif, and a coiled-coil domain.


Pssm-ID: 277262 [Multi-domain]  Cd Length: 62  Bit Score: 52.12  E-value: 1.39e-08
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gi 2209674677 1115 CFNCDCEF-WLAKRRHHCRNCGNVFCAGCCHLKLP-------IPDQQlYDPVLVCNSCYEHI 1168
Cdd:cd15723      2 CTGCGASFsVLLKKRRSCNNCGNAFCSRCCSKKVPrsvmgatAPAAQ-RETVFVCSGCNDKL 62
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
1106-1165 1.88e-08

FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.


Pssm-ID: 277265 [Multi-domain]  Cd Length: 58  Bit Score: 51.79  E-value: 1.88e-08
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gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPvlVCNSCY 1165
Cdd:cd15726      1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKER--CCKACF 58
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
1102-1165 2.29e-08

FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site.


Pssm-ID: 277278 [Multi-domain]  Cd Length: 73  Bit Score: 51.96  E-value: 2.29e-08
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                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2209674677 1102 EVtRWVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCchLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd15739      1 EV-RWQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDC--LTKTVPSGPNRRPARVCDVCH 61
FYVE_RBNS5 cd15716
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ...
1106-1142 4.33e-08

FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and similar proteins; Rbsn-5, also termed zinc finger FYVE domain-containing protein 20, is a novel Rab5 effector that is complexed to the Sec1-like protein VPS45 and recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. It also binds to Rab4 and EHD1/RME-1, two regulators of the recycling route, and is involved in cargo recycling to the plasma membrane. Moreover, Rbsn-5 regulates endocytosis at the apical side of the wing epithelium and plays a role of the apical endocytic trafficking of Fmi in the establishment of planar cell polarity (PCP).


Pssm-ID: 277256 [Multi-domain]  Cd Length: 61  Bit Score: 50.81  E-value: 4.33e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2209674677 1106 WVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGC 1142
Cdd:cd15716      4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKC 40
FYVE_FGD1_2_4 cd15741
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ...
1105-1165 1.33e-07

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia FGD1, FGD2, FGD4; This family represents a group of Rho GTPase cell division cycle 42 (Cdc42)-specific guanine nucleotide exchange factors (GEFs), including FYVE, RhoGEF and PH domain-containing protein FGD1, FGD2 and FGD4. FGD1, also termed faciogenital dysplasia 1 protein, or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF), or zinc finger FYVE domain-containing protein 3, is a central regulator of extracellular matrix remodeling and belongs to the DBL family of GEFs that regulate the activation of the Rho GTPases. FGD1 is encoded by gene FGD1. Disabling mutations in the FGD1 gene cause the human X-linked developmental disorder faciogenital dysplasia (FGDY, also known as Aarskog-Scott syndrome). FGD2, also termed zinc finger FYVE domain-containing protein 4, is expressed in antigen-presenting cells, including B lymphocytes, macrophages, and dendritic cells. It localizes to early endosomes and active membrane ruffles. It plays a role in leukocyte signaling and vesicle trafficking in cells specialized to present antigen in the immune system. FGD4, also termed actin filament-binding protein frabin, or FGD1-related F-actin-binding protein, or zinc finger FYVE domain-containing protein 6, functions as an F-actin-binding (FAB) protein showing significant homology to FGD1. It induces the formation of filopodia through the activation of Cdc42 in fibroblasts. Those FGD proteins possess a similar domain organization that contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus. However, each FGD has a unique N-terminal region that may directly or indirectly interact with F-actin. FGD1 and FGD4 have an N-terminal proline-rich domain (PRD) and an N-terminal F-actin binding (FAB) domain, respectively. This model corresponds to the FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site. FGD1 possesses a FYVE-like domain that lack the N-terminal WxxD motif. Moreover, FGD2 is the only known RhoGEF family member shown to have a functional FYVE domain and endosomal binding activity.


Pssm-ID: 277280 [Multi-domain]  Cd Length: 65  Bit Score: 49.79  E-value: 1.33e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2209674677 1105 RWVPDHMASHCFNCDCEF-WLAKRRHHCRNCGNVFCAGCCHLKLPIPdqqlYD---PVLVCNSCY 1165
Cdd:cd15741      2 RWVRDNEVTMCMRCKEPFnALTRRRHHCRACGYVVCWKCSDYKATLE----YDgnkLNRVCKHCY 62
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
27-114 1.45e-07

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: 50.46  E-value: 1.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2209674677   27 EENLQVPFTV------LQGEGVEFLGraTDALIAISNYRLHikfkDSVINVPLRMIDSVESRDMFQ-----LHIACKDSK 95
Cdd:cd10570      1 IEKLGVRFCCalrprkLPLEGTLYLS--TYRLIFSSKADGD----ETKLVIPLVDITDVEKIAGASflpsgLIITCKDFR 74
                           90
                   ....*....|....*....
gi 2209674677   96 VVRCHFSTFKQCQEWLSRL 114
Cdd:cd10570     75 TIKFSFDSEDEAVKVIARV 93
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
1117-1165 2.04e-07

FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from eumetazoa; This family includes a group of uncharacterized myotubularin-related proteins mainly found in eumetazoa. Although their biological functions remain unclear, they share similar domain architecture that consists of an N-terminal pleckstrin homology (PH) domain, a highly conserved region related to myotubularin proteins, a C-terminal FYVE domain. The model corresponds to the FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277277 [Multi-domain]  Cd Length: 61  Bit Score: 48.86  E-value: 2.04e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2209674677 1117 NCDCE--FWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd15738     11 ECSCStpFDHFSKKHHCWRCGNVFCTRCIDKQRALPGHLSQRPVPVCRACY 61
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
1124-1165 3.50e-07

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 48.18  E-value: 3.50e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2209674677 1124 LAKRRHHCRNCGNVFCAGCCHLKLPIPdQQLYDPVLVCNSCY 1165
Cdd:cd15744     12 LALPKHNCYNCGGTFCDACSSNELPLP-SSIYEPARVCDVCY 52
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
1115-1165 3.94e-07

FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear.


Pssm-ID: 277288 [Multi-domain]  Cd Length: 51  Bit Score: 47.89  E-value: 3.94e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2209674677 1115 CFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPdQQLYDPVLVCNSCY 1165
Cdd:cd15749      2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVP-RKGNQKQKVCKQCH 51
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
1114-1165 5.94e-07

FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.


Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 47.50  E-value: 5.94e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2209674677 1114 HCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd15745      1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVPDTCIYLRVCKTCY 52
FYVE2_Vac1p_like cd15737
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ...
1105-1152 8.91e-07

FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the second FYVE domain that is responsible for the ability of Pep7p to efficiently interact with Vac1p and Vps45p.


Pssm-ID: 277276 [Multi-domain]  Cd Length: 83  Bit Score: 47.89  E-value: 8.91e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2209674677 1105 RWVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGC---CHLKLPIPDQ 1152
Cdd:cd15737      1 PWEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVCDDRrtkCSTEVPLDLL 51
FYVE_scVPS27p_Vac1p_like cd15736
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
1115-1165 3.46e-06

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.


Pssm-ID: 277275 [Multi-domain]  Cd Length: 56  Bit Score: 45.25  E-value: 3.46e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2209674677 1115 CFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQ----QLYDPVLVCNSCY 1165
Cdd:cd15736      2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIPLNLSaydpRNGKWYRCCHSCF 56
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
402-433 1.11e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 45.43  E-value: 1.11e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2209674677   402 PVLVHCSDGWDRTPQIVALAKILLDPYYRTLE 433
Cdd:smart00404   41 PVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE 72
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
402-433 1.11e-05

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 45.43  E-value: 1.11e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2209674677   402 PVLVHCSDGWDRTPQIVALAKILLDPYYRTLE 433
Cdd:smart00012   41 PVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE 72
FYVE1_Vac1p_like cd15761
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ...
1104-1167 1.48e-05

FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277300  Cd Length: 76  Bit Score: 44.18  E-value: 1.48e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2209674677 1104 TRWVPDHMASHCFNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPV-----LVCNSCYEH 1167
Cdd:cd15761      2 SHWKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRNRIKLNNSAEYDPKngkwcRCCEKCFTS 70
FYVE_WDFY1_like cd15718
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ...
1124-1165 3.97e-05

FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and similar proteins; This family includes WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2. WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. Both WDFY1 and WDFY2 contain a FYVE domain and multiple WD-40 repeats.


Pssm-ID: 277258 [Multi-domain]  Cd Length: 70  Bit Score: 42.69  E-value: 3.97e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2209674677 1124 LAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd15718     29 LGVRQHHCRKCGKAVCDKCSSNRSTIPVMGFEFPVRVCNECY 70
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
366-425 4.23e-05

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: 43.88  E-value: 4.23e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2209674677  366 PSNWLSALESTKWLQHLSV-------MLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAKILL 425
Cdd:cd14494     15 PLSPLEADSRFLKQLGVTTivdltlaMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLL 81
FYVE_WDFY1 cd15756
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ...
1124-1169 6.46e-05

FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar proteins; WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. In addition to FYVE domain, WDFY1 harbors multiple WD-40 repeats.


Pssm-ID: 277295 [Multi-domain]  Cd Length: 76  Bit Score: 42.36  E-value: 6.46e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2209674677 1124 LAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCYEHIQ 1169
Cdd:cd15756     29 LGLRQHHCRKCGQAVCGKCSSKRSSYPIMGFEFQVRVCDSCFETIK 74
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
1115-1165 2.24e-03

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277279 [Multi-domain]  Cd Length: 54  Bit Score: 37.29  E-value: 2.24e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2209674677 1115 CFNCDCEF-WLAKRRHHCRNCGNVFCAGCCHLKLPIPDQqlydpVLVCNSCY 1165
Cdd:cd15740      8 CKGCNESFnSITKRRHHCKQCGAVICGKCSEFKDLASRH-----NRVCRDCF 54
PH-GRAM_MTM-like cd13223
Myotubularian 1 and related proteins Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase; ...
53-106 2.58e-03

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


Pssm-ID: 275407  Cd Length: 100  Bit Score: 38.37  E-value: 2.58e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2209674677   53 IAISNYRLHIKFKDS----VINVPLRMIDSVE--------SRDMFQLHIACKDSKVVRchFsTFKQ 106
Cdd:cd13223     20 LYITNYRLYFKSRDRepnfVLDVPLGVISRVEkvggatsrGENSYGLEIHCKDMRNLR--F-AHKQ 82
FYVE_WDFY2 cd15757
FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also ...
1127-1165 6.19e-03

FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. WDFY2 contains WD40 motifs and a FYVE domain.


Pssm-ID: 277296 [Multi-domain]  Cd Length: 70  Bit Score: 36.58  E-value: 6.19e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2209674677 1127 RRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCY 1165
Cdd:cd15757     32 RQHHCRKCGKAVCGKCSSKRSTIPLMGFEFEVRVCDSCH 70
 
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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