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Conserved domains on  [gi|139394668|ref|NP_055945|]
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TBC1 domain family member 9 [Homo sapiens]

Protein Classification

PH-GRAM1_TCB1D9_TCB1D9B and TBC domain-containing protein( domain architecture ID 10193424)

protein containing domains PH-GRAM1_TCB1D9_TCB1D9B, PH-GRAM2_TCB1D9_TCB1D9B, TBC, and EFh

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-GRAM1_TCB1D9_TCB1D9B cd13351
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
 157-255 5.70e-68

TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 1; TBC1D9 and TCB1D9B may act as a GTPase-activating proteins for Rab family protein(s). TBC1D9 and TCB1D9B contain two N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the first repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


:

Pssm-ID: 275420  Cd Length: 99  Bit Score: 223.04  E-value: 5.70e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  157 EEKLVNYYSCSYWKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEKNATLLLPDVIKVSTRSSEHFFSVFL 236
Cdd:cd13351     1 EEKLVNYYSCSYWKGRVPRQGWLYLSVNHLCFYSFLLGKEAKLVIRWTDVTQLEKNNSLLLPDSIKVVTRDKEHYFSMFL 80

                          90
                  ....*....|....*....
gi 139394668  237 NINETFKLMEQLANIAMRQ 255
Cdd:cd13351    81 NISETFKLMEQLANLAMRQ 99
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 512-722 2.55e-56

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


:

Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 194.45  E-value: 2.55e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668    512 VLKGIPESMRGELWLLLSGAI-NEKATHPGYYEDLVEKSMGKYNLATEEIERDLHRSLPEHPAFQ--NEMGIAALRRVLT 588
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQpMDTSADKDLYSRLLKETAPDDKSIVHQIEKDLRRTFPEHSFFQdkEGPGQESLRRVLK 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668    589 AYAFRNPNIGYCQAMNIVTSVLLLY-AKEEEAFWLLVALCERMLPDYYNTRVVGALVDQGVFEELARDYVPQLYDCMQDL 667
Cdd:smart00164   81 AYALYNPEVGYCQGMNFLAAPLLLVmEDEEDAFWCLVKLMERYGPNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKDL 160

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 139394668    668 GVISTI-SLSWFLTLFLSVMPFESAVVVVDCFFYEGIKVIFQLALAVLDANVDKLL 722
Cdd:smart00164  161 GITPSLyALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PH-GRAM2_TCB1D9_TCB1D9B cd13354
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
 304-399 7.31e-47

TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 2; TBC1D9 and TCB1D9B may act as a GTPase-activating proteins for Rab family protein(s). TBC1D9 and TCB1D9B contain two N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the second repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


:

Pssm-ID: 270161  Cd Length: 97  Bit Score: 162.82  E-value: 7.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  304 DEKLDGHTDCTLWTPFNKMHILGQMFVSTNYICFTSKEENLCSLIIPLREVTIVEKADSSSVLPSPL-SISTRNRMTFLF 382
Cdd:cd13354     1 DEKLDGSTDCTLWTPYNKRHVWGTLYLSQNYICFTSKVRDLVSLVIPLREVTSVEKADSSSVSLPNGiLITTKSKMTFLF 80

                          90
                  ....*....|....*..
gi 139394668  383 ANLKDRDFLVQRISDFL 399
Cdd:cd13354    81 AQIKDRDFLVHKISDFL 97
EFh super family cl08302
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 893-923 8.09e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


The actual alignment was detected with superfamily member cd00213:

Pssm-ID: 415501 [Multi-domain]  Cd Length: 88  Bit Score: 36.70  E-value: 8.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 139394668  893 RLFQLLDENGDSLINFREFVS---GLSAACHGDL 923
Cdd:cd00213    55 KIMKDLDVNKDGKVDFQEFLVligKLAVACHEFF 88
 
Name Accession Description Interval E-value
PH-GRAM1_TCB1D9_TCB1D9B cd13351
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
 157-255 5.70e-68

TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 1; TBC1D9 and TCB1D9B may act as a GTPase-activating proteins for Rab family protein(s). TBC1D9 and TCB1D9B contain two N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the first repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275420  Cd Length: 99  Bit Score: 223.04  E-value: 5.70e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  157 EEKLVNYYSCSYWKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEKNATLLLPDVIKVSTRSSEHFFSVFL 236
Cdd:cd13351     1 EEKLVNYYSCSYWKGRVPRQGWLYLSVNHLCFYSFLLGKEAKLVIRWTDVTQLEKNNSLLLPDSIKVVTRDKEHYFSMFL 80

                          90
                  ....*....|....*....
gi 139394668  237 NINETFKLMEQLANIAMRQ 255
Cdd:cd13351    81 NISETFKLMEQLANLAMRQ 99
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 512-722 2.55e-56

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 194.45  E-value: 2.55e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668    512 VLKGIPESMRGELWLLLSGAI-NEKATHPGYYEDLVEKSMGKYNLATEEIERDLHRSLPEHPAFQ--NEMGIAALRRVLT 588
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQpMDTSADKDLYSRLLKETAPDDKSIVHQIEKDLRRTFPEHSFFQdkEGPGQESLRRVLK 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668    589 AYAFRNPNIGYCQAMNIVTSVLLLY-AKEEEAFWLLVALCERMLPDYYNTRVVGALVDQGVFEELARDYVPQLYDCMQDL 667
Cdd:smart00164   81 AYALYNPEVGYCQGMNFLAAPLLLVmEDEEDAFWCLVKLMERYGPNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKDL 160

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 139394668    668 GVISTI-SLSWFLTLFLSVMPFESAVVVVDCFFYEGIKVIFQLALAVLDANVDKLL 722
Cdd:smart00164  161 GITPSLyALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
COG5210 COG5210
GTPase-activating protein [General function prediction only];
504-799 3.61e-49

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 183.08  E-value: 3.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  504 RTEKTRELVLKGIPESMRGELWLLLSGAINEKATHPGYYEDLveksMGKYNLAT-------EEIERDLHRSLPEHPAFQN 576
Cdd:COG5210   201 QLSKLRELIRKGIPNELRGDVWEFLLGIGFDLDKNPGLYERL----LNLHREAKiptqeiiSQIEKDLSRTFPDNSLFQT 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  577 EMGIAA--LRRVLTAYAFRNPNIGYCQAMNIVTSVLLLY-AKEEEAFWLLVALCER-MLPDYYNTRVVGALVDQGVFEEL 652
Cdd:COG5210   277 EISIRAenLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVlESEEQAFWCLVKLLKNyGLPGYFLKNLSGLHRDLKVLDDL 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  653 ARDYVPQLYDCMQDLGV-ISTISLSWFLTLFLSVMPFESAVVVVDCFFYEGIKVIFQLALAVLDANVDKLLNCKDDGEAM 731
Cdd:COG5210   357 VEELDPELYEHLLREGVvLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLD 436

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 139394668  732 TVLGRYLDSVTNKDStlppiphLHSLLSDDVepyPEVDIFRLIRTSYEK-FGTIRADLIEQMRFKQRLK 799
Cdd:COG5210   437 LLLKQLFLHSGKEAW-------SSILKFRHG---TDRDILLFIEDLLKKdITPTRYRSELREIQRKRNE 495
PH-GRAM2_TCB1D9_TCB1D9B cd13354
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
 304-399 7.31e-47

TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 2; TBC1D9 and TCB1D9B may act as a GTPase-activating proteins for Rab family protein(s). TBC1D9 and TCB1D9B contain two N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the second repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 270161  Cd Length: 97  Bit Score: 162.82  E-value: 7.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  304 DEKLDGHTDCTLWTPFNKMHILGQMFVSTNYICFTSKEENLCSLIIPLREVTIVEKADSSSVLPSPL-SISTRNRMTFLF 382
Cdd:cd13354     1 DEKLDGSTDCTLWTPYNKRHVWGTLYLSQNYICFTSKVRDLVSLVIPLREVTSVEKADSSSVSLPNGiLITTKSKMTFLF 80

                          90
                  ....*....|....*..
gi 139394668  383 ANLKDRDFLVQRISDFL 399
Cdd:cd13354    81 AQIKDRDFLVHKISDFL 97
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 560-722 3.19e-44

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


Pssm-ID: 459855  Cd Length: 178  Bit Score: 158.19  E-value: 3.19e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668   560 IERDLHRSLPEHPAFQNEMGIAALRRVLTAYAFRNPNIGYCQAMNIVTSVLLL-YAKEEEAFWLLVALCER-MLPDYYNT 637
Cdd:pfam00566   12 IEKDVPRTFPHSFFFDNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENyLLRDFYTP 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668   638 RVVGALVDQGVFEELARDYVPQLYDCMQDLGVIST-ISLSWFLTLFLSVMPFESAVVVVDCFFYEGIKV-IFQLALAVLD 715
Cdd:pfam00566   92 DFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDlFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVALAILK 171


                   ....*..
gi 139394668   716 ANVDKLL 722
Cdd:pfam00566  172 RFREELL 178
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 147-256 9.73e-21

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 88.58  E-value: 9.73e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668   147 KFHRLFGMPEEEKLVNYYSCSYWKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEK--NATLLLPDVIKVS 224
Cdd:pfam02893    2 LFRKKFKLPPEERLIASYSCYLNRDGGPVQGRLYLTNYRLCFRSLPKGWSTKVVIPLVDIEEIEKlkGGANLFPNGIQVE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 139394668   225 TrSSEHFFSVFLNINETFKLMEQLANIAMRQL 256
Cdd:pfam02893   82 T-GSNDKFSFAGFVTRDEAIEFILALLKNAHP 112
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
153-211 1.81e-17

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 77.63  E-value: 1.81e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 139394668    153 GMPEEEKLVNYYSCSYWKgKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEK 211
Cdd:smart00568    1 KLPEEEKLIADYSCYLSR-TGPVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIEK 58
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 293-402 8.02e-13

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 66.24  E-value: 8.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668   293 ERYRALFRLPKDEKLDGHTDCTLWTPFnkMHILGQMFVSTNYICFTSKE-ENLCSLIIPLREVTIVEK-ADSSSVLPSPL 370
Cdd:pfam02893    1 ELFRKKFKLPPEERLIASYSCYLNRDG--GPVQGRLYLTNYRLCFRSLPkGWSTKVVIPLVDIEEIEKlKGGANLFPNGI 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 139394668   371 SISTRNRMTFLFANLKDRDFLVQRISDFLQQT 402
Cdd:pfam02893   79 QVETGSNDKFSFAGFVTRDEAIEFILALLKNA 110
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
300-359 3.26e-12

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 62.61  E-value: 3.26e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 139394668    300 RLPKDEKLDGHTDCTLWtpfNKMHILGQMFVSTNYICFTS-KEENLCSLIIPLREVTIVEK 359
Cdd:smart00568    1 KLPEEEKLIADYSCYLS---RTGPVQGRLYISNYRLCFRSnLPGKLTKVVIPLADITRIEK 58
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 893-923 8.09e-03

S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins.


Pssm-ID: 238131 [Multi-domain]  Cd Length: 88  Bit Score: 36.70  E-value: 8.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 139394668  893 RLFQLLDENGDSLINFREFVS---GLSAACHGDL 923
Cdd:cd00213    55 KIMKDLDVNKDGKVDFQEFLVligKLAVACHEFF 88
 
Name Accession Description Interval E-value
PH-GRAM1_TCB1D9_TCB1D9B cd13351
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
 157-255 5.70e-68

TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 1; TBC1D9 and TCB1D9B may act as a GTPase-activating proteins for Rab family protein(s). TBC1D9 and TCB1D9B contain two N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the first repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275420  Cd Length: 99  Bit Score: 223.04  E-value: 5.70e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  157 EEKLVNYYSCSYWKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEKNATLLLPDVIKVSTRSSEHFFSVFL 236
Cdd:cd13351     1 EEKLVNYYSCSYWKGRVPRQGWLYLSVNHLCFYSFLLGKEAKLVIRWTDVTQLEKNNSLLLPDSIKVVTRDKEHYFSMFL 80

                          90
                  ....*....|....*....
gi 139394668  237 NINETFKLMEQLANIAMRQ 255
Cdd:cd13351    81 NISETFKLMEQLANLAMRQ 99
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 512-722 2.55e-56

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 194.45  E-value: 2.55e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668    512 VLKGIPESMRGELWLLLSGAI-NEKATHPGYYEDLVEKSMGKYNLATEEIERDLHRSLPEHPAFQ--NEMGIAALRRVLT 588
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQpMDTSADKDLYSRLLKETAPDDKSIVHQIEKDLRRTFPEHSFFQdkEGPGQESLRRVLK 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668    589 AYAFRNPNIGYCQAMNIVTSVLLLY-AKEEEAFWLLVALCERMLPDYYNTRVVGALVDQGVFEELARDYVPQLYDCMQDL 667
Cdd:smart00164   81 AYALYNPEVGYCQGMNFLAAPLLLVmEDEEDAFWCLVKLMERYGPNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKDL 160

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 139394668    668 GVISTI-SLSWFLTLFLSVMPFESAVVVVDCFFYEGIKVIFQLALAVLDANVDKLL 722
Cdd:smart00164  161 GITPSLyALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PH-GRAM1_TCB1D8_TCB1D9_family cd13217
TCB1D8 and TCB1D9 family Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators ...
 157-255 1.30e-53

TCB1D8 and TCB1D9 family Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 1; TBC1D8, TBC1D8B, TBC1D9 and TBC1D9B may act as a GTPase-activating proteins for Rab family protein(s). They all contain an N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the first repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275404  Cd Length: 99  Bit Score: 181.87  E-value: 1.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  157 EEKLVNYYSCSYWKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEKNATLLLPDVIKVSTRSSEHFFSVFL 236
Cdd:cd13217     1 EEKLVTYYSCSYWKGRVPRQGWLYLSINHLCFYSFLLGSESKLIIRWTEVSDLERTSNTILTDTIKVNTRSKEHPFSMFL 80

                          90
                  ....*....|....*....
gi 139394668  237 NINETFKLMEQLANIAMRQ 255
Cdd:cd13217    81 NISETFKLMEQLAQIPDRP 99
COG5210 COG5210
GTPase-activating protein [General function prediction only];
504-799 3.61e-49

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 183.08  E-value: 3.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  504 RTEKTRELVLKGIPESMRGELWLLLSGAINEKATHPGYYEDLveksMGKYNLAT-------EEIERDLHRSLPEHPAFQN 576
Cdd:COG5210   201 QLSKLRELIRKGIPNELRGDVWEFLLGIGFDLDKNPGLYERL----LNLHREAKiptqeiiSQIEKDLSRTFPDNSLFQT 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  577 EMGIAA--LRRVLTAYAFRNPNIGYCQAMNIVTSVLLLY-AKEEEAFWLLVALCER-MLPDYYNTRVVGALVDQGVFEEL 652
Cdd:COG5210   277 EISIRAenLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVlESEEQAFWCLVKLLKNyGLPGYFLKNLSGLHRDLKVLDDL 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  653 ARDYVPQLYDCMQDLGV-ISTISLSWFLTLFLSVMPFESAVVVVDCFFYEGIKVIFQLALAVLDANVDKLLNCKDDGEAM 731
Cdd:COG5210   357 VEELDPELYEHLLREGVvLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLD 436

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 139394668  732 TVLGRYLDSVTNKDStlppiphLHSLLSDDVepyPEVDIFRLIRTSYEK-FGTIRADLIEQMRFKQRLK 799
Cdd:COG5210   437 LLLKQLFLHSGKEAW-------SSILKFRHG---TDRDILLFIEDLLKKdITPTRYRSELREIQRKRNE 495
PH-GRAM2_TCB1D9_TCB1D9B cd13354
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
 304-399 7.31e-47

TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 2; TBC1D9 and TCB1D9B may act as a GTPase-activating proteins for Rab family protein(s). TBC1D9 and TCB1D9B contain two N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the second repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 270161  Cd Length: 97  Bit Score: 162.82  E-value: 7.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  304 DEKLDGHTDCTLWTPFNKMHILGQMFVSTNYICFTSKEENLCSLIIPLREVTIVEKADSSSVLPSPL-SISTRNRMTFLF 382
Cdd:cd13354     1 DEKLDGSTDCTLWTPYNKRHVWGTLYLSQNYICFTSKVRDLVSLVIPLREVTSVEKADSSSVSLPNGiLITTKSKMTFLF 80

                          90
                  ....*....|....*..
gi 139394668  383 ANLKDRDFLVQRISDFL 399
Cdd:cd13354    81 AQIKDRDFLVHKISDFL 97
PH-GRAM2_TCB1D8_TCB1D9_family cd13218
TCB1D8 and TCB1D9 family Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators ...
 304-399 2.16e-45

TCB1D8 and TCB1D9 family Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 2; TBC1D8, TBC1D8B, TBC1D9 and TBC1D9B may act as a GTPase-activating proteins for Rab family protein(s). They all contain an N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the second repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275405  Cd Length: 96  Bit Score: 158.52  E-value: 2.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  304 DEKLDGHTDCTLWTPFNKMHILGQMFVSTNYICFTSKEENLCSLIIPLREVTIVEKADSSSVLPSPLSISTRNRMTFLFA 383
Cdd:cd13218     1 EEKLKEVHDCFLWTPFSHFHTHGKMFISENYICFASKEGNLCSVIIPLREVLAIEKTNDSSVLPKPVIISIKGKMAFRFS 80

                          90
                  ....*....|....*.
gi 139394668  384 NLKDRDFLVQRISDFL 399
Cdd:cd13218    81 ELKDRDELVAKLRLKL 96
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 560-722 3.19e-44

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


Pssm-ID: 459855  Cd Length: 178  Bit Score: 158.19  E-value: 3.19e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668   560 IERDLHRSLPEHPAFQNEMGIAALRRVLTAYAFRNPNIGYCQAMNIVTSVLLL-YAKEEEAFWLLVALCER-MLPDYYNT 637
Cdd:pfam00566   12 IEKDVPRTFPHSFFFDNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENyLLRDFYTP 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668   638 RVVGALVDQGVFEELARDYVPQLYDCMQDLGVIST-ISLSWFLTLFLSVMPFESAVVVVDCFFYEGIKV-IFQLALAVLD 715
Cdd:pfam00566   92 DFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDlFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVALAILK 171


                   ....*..
gi 139394668   716 ANVDKLL 722
Cdd:pfam00566  172 RFREELL 178
PH-GRAM1_TBC1D8 cd13349
TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) ...
 158-255 1.07e-42

TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 1; TBC1D8 may act as a GTPase-activating protein for Rab family protein(s). TBC1D8 contains an N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the first repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 270156  Cd Length: 99  Bit Score: 150.78  E-value: 1.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  158 EKLVNYYSCSYWKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEKNATLLLPDVIKVSTRSSEHFFSVFLN 237
Cdd:cd13349     2 EKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLLIPWVDVQKLERTSNVFMTDTIRVTTQNKERDFSMFLN 81

                          90
                  ....*....|....*...
gi 139394668  238 INETFKLMEQLANIAMRQ 255
Cdd:cd13349    82 IDEVFRIMEQLADVTLRR 99
PH-GRAM1_TBC1D8B cd13350
TBC1 domain family member 8B (TBC1D8B) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 157-255 9.22e-42

TBC1 domain family member 8B (TBC1D8B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 1; TBC1D8B may act as a GTPase-activating protein for Rab family protein(s). TBC1D8B contains an N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the first repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275419  Cd Length: 99  Bit Score: 148.15  E-value: 9.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  157 EEKLVNYYSCSYWKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEKNATLLLPDVIKVSTRSSEHFFSVFL 236
Cdd:cd13350     1 QEKLVTYYSCSYWRGRVPCQGWLYLSTNFLSFYSFLLGSEIKLIISWDEISKLEKTSNVILTESIHVCSRGEDHYFSMFL 80

                          90
                  ....*....|....*....
gi 139394668  237 NINETFKLMEQLANIAMRQ 255
Cdd:cd13350    81 HINETFLLMEQLANYAVRR 99
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 156-248 5.58e-25

GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; The GRAMDC proteins are membrane proteins. Nothing is known about its function. Members include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, GRAMDC4, and GRAMDC-like proteins. All of the members, except for GRAMDC4 are included in this hierarchy. Each contains a single PH-GRAM domain at their N-terminus. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275406  Cd Length: 94  Bit Score: 99.89  E-value: 5.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  156 EEEKLVNYYSCSyWKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEKNAT-LLLPDVIKVSTRSSEHFFSV 234
Cdd:cd13220     1 EDERLIDDFSCA-LQRDILLQGRLYISENHLCFYSNIFGWETKLVIPFKDITSIEKKKTaLIFPNAIEITTKGEKYFFTS 79

                          90
                  ....*....|....
gi 139394668  235 FLNINETFKLMEQL 248
Cdd:cd13220    80 FLSRDSAYKLLTRV 93
PH-GRAM2_TBC1D8 cd13353
TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) ...
 305-393 1.13e-23

TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 2; TBC1D8 may act as a GTPase-activating protein for Rab family protein(s). TBC1D8 contains two N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the second repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 270160  Cd Length: 96  Bit Score: 96.45  E-value: 1.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  305 EKLDGHTDCTLWTPFNKMHILGQMFVSTNYICFTSKEENLCSLIIPLREVTIVEKADSSSVLPSPLSISTRNRMTFLFAN 384
Cdd:cd13353     2 EKLHEVVDCSLWTPFSRCHTAGRMYTSDSYICFASKEDGSCNVILPLREVVSIEKMEDTSLLPNPIIVSIRSKMAFQFIE 81


                  ....*....
gi 139394668  385 LKDRDFLVQ 393
Cdd:cd13353    82 LKDRDSLVE 90
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 147-256 9.73e-21

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 88.58  E-value: 9.73e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668   147 KFHRLFGMPEEEKLVNYYSCSYWKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEK--NATLLLPDVIKVS 224
Cdd:pfam02893    2 LFRKKFKLPPEERLIASYSCYLNRDGGPVQGRLYLTNYRLCFRSLPKGWSTKVVIPLVDIEEIEKlkGGANLFPNGIQVE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 139394668   225 TrSSEHFFSVFLNINETFKLMEQLANIAMRQL 256
Cdd:pfam02893   82 T-GSNDKFSFAGFVTRDEAIEFILALLKNAHP 112
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 157-245 1.34e-18

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: 82.04  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  157 EEKLVNYYSCSYWKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEKNA-TLLLPDVIKVSTRSSEHFFSVF 235
Cdd:cd10570     1 IEKLGVRFCCALRPRKLPLEGTLYLSTYRLIFSSKADGDETKLVIPLVDITDVEKIAgASFLPSGLIITCKDFRTIKFSF 80

                          90
                  ....*....|
gi 139394668  236 LNINETFKLM 245
Cdd:cd10570    81 DSEDEAVKVI 90
PH-GRAM2_TBC1D8B cd13352
TBC1 domain family member 8B (TBC1D8B) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 304-395 1.05e-17

TBC1 domain family member 8B (TBC1D8B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 2; TBC1D8B may act as a GTPase-activating protein for Rab family protein(s). TBC1D8B contains an N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the second repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 270159  Cd Length: 93  Bit Score: 79.51  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  304 DEKLDGHTDCTLWTPFNKMHILGQMFVSTNYICFTSKEENLCSLIIPLREVTIVEKADsssVLPSPLSISTRNRMTFLFA 383
Cdd:cd13352     1 EETLKEVHECFLWVPFSHFNTHGKMCISENYICFASQDGSLCSVIIPLREVLSIDKTD---DSSRAVTISTKGKRAFRFT 77

                          90
                  ....*....|..
gi 139394668  384 NLKDRDFLVQRI 395
Cdd:cd13352    78 EVKDFEQLVAKL 89
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
153-211 1.81e-17

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 77.63  E-value: 1.81e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 139394668    153 GMPEEEKLVNYYSCSYWKgKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEK 211
Cdd:smart00568    1 KLPEEEKLIADYSCYLSR-TGPVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIEK 58
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 304-399 1.17e-14

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: 70.49  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  304 DEKLDGHTDCTLWTpfNKMHILGQMFVSTNYICFTSKE-ENLCSLIIPLREVTIVEKADSSSVLPSPLSISTRNRMTFLF 382
Cdd:cd10570     1 IEKLGVRFCCALRP--RKLPLEGTLYLSTYRLIFSSKAdGDETKLVIPLVDITDVEKIAGASFLPSGLIITCKDFRTIKF 78

                          90
                  ....*....|....*..
gi 139394668  383 ANLKDrDFLVQRISDFL 399
Cdd:cd10570    79 SFDSE-DEAVKVIARVL 94
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 293-402 8.02e-13

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 66.24  E-value: 8.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668   293 ERYRALFRLPKDEKLDGHTDCTLWTPFnkMHILGQMFVSTNYICFTSKE-ENLCSLIIPLREVTIVEK-ADSSSVLPSPL 370
Cdd:pfam02893    1 ELFRKKFKLPPEERLIASYSCYLNRDG--GPVQGRLYLTNYRLCFRSLPkGWSTKVVIPLVDIEEIEKlKGGANLFPNGI 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 139394668   371 SISTRNRMTFLFANLKDRDFLVQRISDFLQQT 402
Cdd:pfam02893   79 QVETGSNDKFSFAGFVTRDEAIEFILALLKNA 110
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
300-359 3.26e-12

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 62.61  E-value: 3.26e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 139394668    300 RLPKDEKLDGHTDCTLWtpfNKMHILGQMFVSTNYICFTS-KEENLCSLIIPLREVTIVEK 359
Cdd:smart00568    1 KLPEEEKLIADYSCYLS---RTGPVQGRLYISNYRLCFRSnLPGKLTKVVIPLADITRIEK 58
PH-GRAM_C2-GRAM cd13219
C2 and GRAM domain-containing protein Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 157-250 4.07e-09

C2 and GRAM domain-containing protein Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; C2GRAM contains two N-terminal C2 domains followed by a single PH-GRAM domain. Since it contains both of these domains it is assumed that this gene cross-links both calcium and phosphoinositide signaling pathways. In general he C2 domain is involved in binding phospholipids in a calcium dependent manner or calcium independent manner. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 270039 [Multi-domain]  Cd Length: 111  Bit Score: 55.55  E-value: 4.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 139394668  157 EEKLVNYYSCSYwKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEKNATLLLPDVIKVSTRSSE------- 229
Cdd:cd13219     1 EEFLINDFSCAL-KRKFLYQGRMFLSARHIGFHSNVFGKKTKFVFLWEDIEEIQESPHSLINPAIVITLRKGRgldagqg 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 139394668  230 ------------HFFSvFLNINETFKLMEQLAN 250
Cdd:cd13219    80 vppidpdgrlkyKFAS-FVNRNHAFRTLMRLWK 111
PH-GRAM2_AGT26 cd13216
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
 157-211 1.52e-05

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 2; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275403  Cd Length: 93  Bit Score: 44.88  E-value: 1.52e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 139394668  157 EEKLVNYYSCsYWKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEK 211
Cdd:cd13216     1 TEKLIASYYC-YLIRVLPVYGKLYVSNNYLCFRSLLPGVSTKMILPLRDIENVEK 54
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 893-923 8.09e-03

S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins.


Pssm-ID: 238131 [Multi-domain]  Cd Length: 88  Bit Score: 36.70  E-value: 8.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 139394668  893 RLFQLLDENGDSLINFREFVS---GLSAACHGDL 923
Cdd:cd00213    55 KIMKDLDVNKDGKVDFQEFLVligKLAVACHEFF 88
 
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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