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Conserved domains on  [gi|45597177|ref|NP_055858|]
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TBC1 domain family member 9B isoform b [Homo sapiens]

Protein Classification

PH-GRAM1_TCB1D9_TCB1D9B and TBC domain-containing protein( domain architecture ID 10193429)

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 ...
153-251 2.85e-66

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: 218.03  E-value: 2.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  153 GEKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNATLLFPESIRVDTRDQELFFSMFL 232
Cdd:cd13351    1 EEKLVNYYSCSYWKGRVPRQGWLYLSVNHLCFYSFLLGKEAKLVIRWTDVTQLEKNNSLLLPDSIKVVTRDKEHYFSMFL 80
                         90
                 ....*....|....*....
gi 45597177  233 NIGETFKLMEQLANLAMRQ 251
Cdd:cd13351   81 NISETFKLMEQLANLAMRQ 99
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
505-715 3.85e-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: 194.06  E-value: 3.85e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177     505 VLKGIPESLRGELWLLFSGAW-NEMVTHPGYYAELVEKSTGKYSLATEEIERDLHRSMPEHPAFQ--NELGIAALRRVLT 581
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQpMDTSADKDLYSRLLKETAPDDKSIVHQIEKDLRRTFPEHSFFQdkEGPGQESLRRVLK 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177     582 AYAFRNPTIGYCQAMNIVTSVLLLY-GSEEEAFWLLVALCERMLPDYYNTRVVGALVDQGIFEELTRDFLPQLSEKMQDL 660
Cdd:smart00164   81 AYALYNPEVGYCQGMNFLAAPLLLVmEDEEDAFWCLVKLMERYGPNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKDL 160
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 45597177     661 GV-ISSISLSWFLTLFLSVMPFESAVVIVDCFFYEGIKVILQVALAVLDANMEQLL 715
Cdd:smart00164  161 GItPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PH-GRAM2_TCB1D9_TCB1D9B cd13354
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
299-394 9.15e-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: 162.43  E-value: 9.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  299 DERLDGHTSCTLWTPFNKLHIPGQMFISNNYICFASKEEDACHLIIPLREVTIVEKADSSSVLPSPL-SISTKSKMTFLF 377
Cdd:cd13354    1 DEKLDGSTDCTLWTPYNKRHVWGTLYLSQNYICFTSKVRDLVSLVIPLREVTSVEKADSSSVSLPNGiLITTKSKMTFLF 80
                         90
                 ....*....|....*..
gi 45597177  378 ANLKDRDFLVQRISDFL 394
Cdd:cd13354   81 AQIKDRDFLVHKISDFL 97
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
886-911 4.61e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


:

Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.82  E-value: 4.61e-03
                            10        20
                    ....*....|....*....|....*.
gi 45597177     886 RMFRLLDENKDSLINFKEFVTGMSGM 911
Cdd:smart00054    4 EAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
PH-GRAM1_TCB1D9_TCB1D9B cd13351
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
153-251 2.85e-66

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: 218.03  E-value: 2.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  153 GEKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNATLLFPESIRVDTRDQELFFSMFL 232
Cdd:cd13351    1 EEKLVNYYSCSYWKGRVPRQGWLYLSVNHLCFYSFLLGKEAKLVIRWTDVTQLEKNNSLLLPDSIKVVTRDKEHYFSMFL 80
                         90
                 ....*....|....*....
gi 45597177  233 NIGETFKLMEQLANLAMRQ 251
Cdd:cd13351   81 NISETFKLMEQLANLAMRQ 99
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
505-715 3.85e-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: 194.06  E-value: 3.85e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177     505 VLKGIPESLRGELWLLFSGAW-NEMVTHPGYYAELVEKSTGKYSLATEEIERDLHRSMPEHPAFQ--NELGIAALRRVLT 581
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQpMDTSADKDLYSRLLKETAPDDKSIVHQIEKDLRRTFPEHSFFQdkEGPGQESLRRVLK 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177     582 AYAFRNPTIGYCQAMNIVTSVLLLY-GSEEEAFWLLVALCERMLPDYYNTRVVGALVDQGIFEELTRDFLPQLSEKMQDL 660
Cdd:smart00164   81 AYALYNPEVGYCQGMNFLAAPLLLVmEDEEDAFWCLVKLMERYGPNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKDL 160
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 45597177     661 GV-ISSISLSWFLTLFLSVMPFESAVVIVDCFFYEGIKVILQVALAVLDANMEQLL 715
Cdd:smart00164  161 GItPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
COG5210 COG5210
GTPase-activating protein [General function prediction only];
407-715 4.43e-48

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 179.61  E-value: 4.43e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  407 SRKASVVDPSTESSPAPQE---GSEQPASPASPLSSRQSFCAQEAPTASQGLLKLFQKNSPMEDLGAKGAKEKMKEESWH 483
Cdd:COG5210  112 SLKSQSTSPELPKRLKDSLpthLPEASSTEKDFSSFKGSSSLNSNPELNKEINELSLKEEPQKLRYYELAADKLWISYLD 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  484 IHFFEYGRGvcmyRTAKTRALVLKGIPESLRGELWLLFSGAWNEMVTHPGYYAEL---VEKSTGKYSLATEEIERDLHRS 560
Cdd:COG5210  192 PNPLSFLPV----QLSKLRELIRKGIPNELRGDVWEFLLGIGFDLDKNPGLYERLlnlHREAKIPTQEIISQIEKDLSRT 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  561 MPEHPAFQNELGIAA--LRRVLTAYAFRNPTIGYCQAMNIVTSVLLLY-GSEEEAFWLLVALCER-MLPDYYNTRVVGAL 636
Cdd:COG5210  268 FPDNSLFQTEISIRAenLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVlESEEQAFWCLVKLLKNyGLPGYFLKNLSGLH 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  637 VDQGIFEELTRDFLPQLSEKMQDLGV-ISSISLSWFLTLFLSVMPFESAVVIVDCFFYEGIKVILQVALAVLDANMEQLL 715
Cdd:COG5210  348 RDLKVLDDLVEELDPELYEHLLREGVvLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLL 427
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
553-715 1.45e-47

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: 167.82  E-value: 1.45e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177    553 IERDLHRSMPEHPAFQNELGIAALRRVLTAYAFRNPTIGYCQAMNIVTSVLLL-YGSEEEAFWLLVALCER-MLPDYYNT 630
Cdd:pfam00566   12 IEKDVPRTFPHSFFFDNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENyLLRDFYTP 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177    631 RVVGALVDQGIFEELTRDFLPQLSEKMQDLGV-ISSISLSWFLTLFLSVMPFESAVVIVDCFFYEGIKV-ILQVALAVLD 708
Cdd:pfam00566   92 DFPGLKRDLYVFEELLKKKLPKLYKHLKELGLdPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVALAILK 171

                   ....*..
gi 45597177    709 ANMEQLL 715
Cdd:pfam00566  172 RFREELL 178
PH-GRAM2_TCB1D9_TCB1D9B cd13354
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
299-394 9.15e-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: 162.43  E-value: 9.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  299 DERLDGHTSCTLWTPFNKLHIPGQMFISNNYICFASKEEDACHLIIPLREVTIVEKADSSSVLPSPL-SISTKSKMTFLF 377
Cdd:cd13354    1 DEKLDGSTDCTLWTPYNKRHVWGTLYLSQNYICFTSKVRDLVSLVIPLREVTSVEKADSSSVSLPNGiLITTKSKMTFLF 80
                         90
                 ....*....|....*..
gi 45597177  378 ANLKDRDFLVQRISDFL 394
Cdd:cd13354   81 AQIKDRDFLVHKISDFL 97
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
143-252 2.87e-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: 90.12  E-value: 2.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177    143 KMRKQFGMPEGEKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEK--NATLLFPESIRVD 220
Cdd:pfam02893    2 LFRKKFKLPPEERLIASYSCYLNRDGGPVQGRLYLTNYRLCFRSLPKGWSTKVVIPLVDIEEIEKlkGGANLFPNGIQVE 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 45597177    221 TRDQElFFSMFLNIGETFKLMEQLANLAMRQL 252
Cdd:pfam02893   82 TGSND-KFSFAGFVTRDEAIEFILALLKNAHP 112
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
149-207 4.17e-18

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 79.17  E-value: 4.17e-18
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 45597177     149 GMPEGEKLVNYYSCSYWKgRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEK 207
Cdd:smart00568    1 KLPEEEKLIADYSCYLSR-TGPVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIEK 58
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
295-354 2.36e-14

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 68.77  E-value: 2.36e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45597177     295 RLPRDERLDGHTSCTLWtpfNKLHIPGQMFISNNYICFAS-KEEDACHLIIPLREVTIVEK 354
Cdd:smart00568    1 KLPEEEKLIADYSCYLS---RTGPVQGRLYISNYRLCFRSnLPGKLTKVVIPLADITRIEK 58
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
291-397 5.50e-14

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: 69.32  E-value: 5.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177    291 RATFRLPRDERLDGHTSCTLWTPFnkLHIPGQMFISNNYICFASKEEDA-CHLIIPLREVTIVEK-ADSSSVLPSPLSIS 368
Cdd:pfam02893    4 RKKFKLPPEERLIASYSCYLNRDG--GPVQGRLYLTNYRLCFRSLPKGWsTKVVIPLVDIEEIEKlKGGANLFPNGIQVE 81
                           90       100
                   ....*....|....*....|....*....
gi 45597177    369 TKSKMTFLFANLKDRDFLVQRISDFLQKT 397
Cdd:pfam02893   82 TGSNDKFSFAGFVTRDEAIEFILALLKNA 110
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
886-911 4.61e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.82  E-value: 4.61e-03
                            10        20
                    ....*....|....*....|....*.
gi 45597177     886 RMFRLLDENKDSLINFKEFVTGMSGM 911
Cdd:smart00054    4 EAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
PH-GRAM1_TCB1D9_TCB1D9B cd13351
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
153-251 2.85e-66

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: 218.03  E-value: 2.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  153 GEKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNATLLFPESIRVDTRDQELFFSMFL 232
Cdd:cd13351    1 EEKLVNYYSCSYWKGRVPRQGWLYLSVNHLCFYSFLLGKEAKLVIRWTDVTQLEKNNSLLLPDSIKVVTRDKEHYFSMFL 80
                         90
                 ....*....|....*....
gi 45597177  233 NIGETFKLMEQLANLAMRQ 251
Cdd:cd13351   81 NISETFKLMEQLANLAMRQ 99
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
505-715 3.85e-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: 194.06  E-value: 3.85e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177     505 VLKGIPESLRGELWLLFSGAW-NEMVTHPGYYAELVEKSTGKYSLATEEIERDLHRSMPEHPAFQ--NELGIAALRRVLT 581
Cdd:smart00164    1 VRKGVPPSLRGVVWKLLLNAQpMDTSADKDLYSRLLKETAPDDKSIVHQIEKDLRRTFPEHSFFQdkEGPGQESLRRVLK 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177     582 AYAFRNPTIGYCQAMNIVTSVLLLY-GSEEEAFWLLVALCERMLPDYYNTRVVGALVDQGIFEELTRDFLPQLSEKMQDL 660
Cdd:smart00164   81 AYALYNPEVGYCQGMNFLAAPLLLVmEDEEDAFWCLVKLMERYGPNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKDL 160
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 45597177     661 GV-ISSISLSWFLTLFLSVMPFESAVVIVDCFFYEGIKVILQVALAVLDANMEQLL 715
Cdd:smart00164  161 GItPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
COG5210 COG5210
GTPase-activating protein [General function prediction only];
407-715 4.43e-48

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 179.61  E-value: 4.43e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  407 SRKASVVDPSTESSPAPQE---GSEQPASPASPLSSRQSFCAQEAPTASQGLLKLFQKNSPMEDLGAKGAKEKMKEESWH 483
Cdd:COG5210  112 SLKSQSTSPELPKRLKDSLpthLPEASSTEKDFSSFKGSSSLNSNPELNKEINELSLKEEPQKLRYYELAADKLWISYLD 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  484 IHFFEYGRGvcmyRTAKTRALVLKGIPESLRGELWLLFSGAWNEMVTHPGYYAEL---VEKSTGKYSLATEEIERDLHRS 560
Cdd:COG5210  192 PNPLSFLPV----QLSKLRELIRKGIPNELRGDVWEFLLGIGFDLDKNPGLYERLlnlHREAKIPTQEIISQIEKDLSRT 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  561 MPEHPAFQNELGIAA--LRRVLTAYAFRNPTIGYCQAMNIVTSVLLLY-GSEEEAFWLLVALCER-MLPDYYNTRVVGAL 636
Cdd:COG5210  268 FPDNSLFQTEISIRAenLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVlESEEQAFWCLVKLLKNyGLPGYFLKNLSGLH 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  637 VDQGIFEELTRDFLPQLSEKMQDLGV-ISSISLSWFLTLFLSVMPFESAVVIVDCFFYEGIKVILQVALAVLDANMEQLL 715
Cdd:COG5210  348 RDLKVLDDLVEELDPELYEHLLREGVvLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLL 427
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
553-715 1.45e-47

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: 167.82  E-value: 1.45e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177    553 IERDLHRSMPEHPAFQNELGIAALRRVLTAYAFRNPTIGYCQAMNIVTSVLLL-YGSEEEAFWLLVALCER-MLPDYYNT 630
Cdd:pfam00566   12 IEKDVPRTFPHSFFFDNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLvYLDEEDAFWCFVSLLENyLLRDFYTP 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177    631 RVVGALVDQGIFEELTRDFLPQLSEKMQDLGV-ISSISLSWFLTLFLSVMPFESAVVIVDCFFYEGIKV-ILQVALAVLD 708
Cdd:pfam00566   92 DFPGLKRDLYVFEELLKKKLPKLYKHLKELGLdPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVALAILK 171

                   ....*..
gi 45597177    709 ANMEQLL 715
Cdd:pfam00566  172 RFREELL 178
PH-GRAM2_TCB1D9_TCB1D9B cd13354
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
299-394 9.15e-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: 162.43  E-value: 9.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  299 DERLDGHTSCTLWTPFNKLHIPGQMFISNNYICFASKEEDACHLIIPLREVTIVEKADSSSVLPSPL-SISTKSKMTFLF 377
Cdd:cd13354    1 DEKLDGSTDCTLWTPYNKRHVWGTLYLSQNYICFTSKVRDLVSLVIPLREVTSVEKADSSSVSLPNGiLITTKSKMTFLF 80
                         90
                 ....*....|....*..
gi 45597177  378 ANLKDRDFLVQRISDFL 394
Cdd:cd13354   81 AQIKDRDFLVHKISDFL 97
PH-GRAM1_TCB1D8_TCB1D9_family cd13217
TCB1D8 and TCB1D9 family Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators ...
154-251 1.30e-46

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: 161.84  E-value: 1.30e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  154 EKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNATLLFPESIRVDTRDQELFFSMFLN 233
Cdd:cd13217    2 EKLVTYYSCSYWKGRVPRQGWLYLSINHLCFYSFLLGSESKLIIRWTEVSDLERTSNTILTDTIKVNTRSKEHPFSMFLN 81
                         90
                 ....*....|....*...
gi 45597177  234 IGETFKLMEQLANLAMRQ 251
Cdd:cd13217   82 ISETFKLMEQLAQIPDRP 99
PH-GRAM1_TBC1D8B cd13350
TBC1 domain family member 8B (TBC1D8B) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
154-251 4.52e-43

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: 152.01  E-value: 4.52e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  154 EKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNATLLFPESIRVDTRDQELFFSMFLN 233
Cdd:cd13350    2 EKLVTYYSCSYWRGRVPCQGWLYLSTNFLSFYSFLLGSEIKLIISWDEISKLEKTSNVILTESIHVCSRGEDHYFSMFLH 81
                         90
                 ....*....|....*...
gi 45597177  234 IGETFKLMEQLANLAMRQ 251
Cdd:cd13350   82 INETFLLMEQLANYAVRR 99
PH-GRAM1_TBC1D8 cd13349
TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) ...
154-251 7.88e-43

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: 151.16  E-value: 7.88e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  154 EKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNATLLFPESIRVDTRDQELFFSMFLN 233
Cdd:cd13349    2 EKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLLIPWVDVQKLERTSNVFMTDTIRVTTQNKERDFSMFLN 81
                         90
                 ....*....|....*...
gi 45597177  234 IGETFKLMEQLANLAMRQ 251
Cdd:cd13349   82 IDEVFRIMEQLADVTLRR 99
PH-GRAM2_TCB1D8_TCB1D9_family cd13218
TCB1D8 and TCB1D9 family Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators ...
299-394 1.31e-41

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: 147.74  E-value: 1.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  299 DERLDGHTSCTLWTPFNKLHIPGQMFISNNYICFASKEEDACHLIIPLREVTIVEKADSSSVLPSPLSISTKSKMTFLFA 378
Cdd:cd13218    1 EEKLKEVHDCFLWTPFSHFHTHGKMFISENYICFASKEGNLCSVIIPLREVLAIEKTNDSSVLPKPVIISIKGKMAFRFS 80
                         90
                 ....*....|....*.
gi 45597177  379 NLKDRDFLVQRISDFL 394
Cdd:cd13218   81 ELKDRDELVAKLRLKL 96
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
154-244 1.12e-23

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: 96.42  E-value: 1.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  154 EKLVNYYSCSyWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNAT-LLFPESIRVDTRDQELFFSMFL 232
Cdd:cd13220    3 ERLIDDFSCA-LQRDILLQGRLYISENHLCFYSNIFGWETKLVIPFKDITSIEKKKTaLIFPNAIEITTKGEKYFFTSFL 81
                         90
                 ....*....|..
gi 45597177  233 NIGETFKLMEQL 244
Cdd:cd13220   82 SRDSAYKLLTRV 93
PH-GRAM2_TBC1D8 cd13353
TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) ...
300-388 6.28e-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: 94.14  E-value: 6.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  300 ERLDGHTSCTLWTPFNKLHIPGQMFISNNYICFASKEEDACHLIIPLREVTIVEKADSSSVLPSPLSISTKSKMTFLFAN 379
Cdd:cd13353    2 EKLHEVVDCSLWTPFSRCHTAGRMYTSDSYICFASKEDGSCNVILPLREVVSIEKMEDTSLLPNPIIVSIRSKMAFQFIE 81

                 ....*....
gi 45597177  380 LKDRDFLVQ 388
Cdd:cd13353   82 LKDRDSLVE 90
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
143-252 2.87e-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: 90.12  E-value: 2.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177    143 KMRKQFGMPEGEKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEK--NATLLFPESIRVD 220
Cdd:pfam02893    2 LFRKKFKLPPEERLIASYSCYLNRDGGPVQGRLYLTNYRLCFRSLPKGWSTKVVIPLVDIEEIEKlkGGANLFPNGIQVE 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 45597177    221 TRDQElFFSMFLNIGETFKLMEQLANLAMRQL 252
Cdd:pfam02893   82 TGSND-KFSFAGFVTRDEAIEFILALLKNAHP 112
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
149-207 4.17e-18

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 79.17  E-value: 4.17e-18
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 45597177     149 GMPEGEKLVNYYSCSYWKgRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEK 207
Cdd:smart00568    1 KLPEEEKLIADYSCYLSR-TGPVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIEK 58
PH-GRAM2_TBC1D8B cd13352
TBC1 domain family member 8B (TBC1D8B) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
308-390 2.10e-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: 78.35  E-value: 2.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  308 CTLWTPFNKLHIPGQMFISNNYICFASKEEDACHLIIPLREVTIVEKADsssVLPSPLSISTKSKMTFLFANLKDRDFLV 387
Cdd:cd13352   10 CFLWVPFSHFNTHGKMCISENYICFASQDGSLCSVIIPLREVLSIDKTD---DSSRAVTISTKGKRAFRFTEVKDFEQLV 86

                 ...
gi 45597177  388 QRI 390
Cdd:cd13352   87 AKL 89
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
154-241 2.69e-16

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: 75.50  E-value: 2.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  154 EKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNATLLFPES-IRVDTRDQELFFSMFL 232
Cdd:cd10570    2 EKLGVRFCCALRPRKLPLEGTLYLSTYRLIFSSKADGDETKLVIPLVDITDVEKIAGASFLPSgLIITCKDFRTIKFSFD 81

                 ....*....
gi 45597177  233 NIGETFKLM 241
Cdd:cd10570   82 SEDEAVKVI 90
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
295-354 2.36e-14

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 68.77  E-value: 2.36e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45597177     295 RLPRDERLDGHTSCTLWtpfNKLHIPGQMFISNNYICFAS-KEEDACHLIIPLREVTIVEK 354
Cdd:smart00568    1 KLPEEEKLIADYSCYLS---RTGPVQGRLYISNYRLCFRSnLPGKLTKVVIPLADITRIEK 58
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
291-397 5.50e-14

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: 69.32  E-value: 5.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177    291 RATFRLPRDERLDGHTSCTLWTPFnkLHIPGQMFISNNYICFASKEEDA-CHLIIPLREVTIVEK-ADSSSVLPSPLSIS 368
Cdd:pfam02893    4 RKKFKLPPEERLIASYSCYLNRDG--GPVQGRLYLTNYRLCFRSLPKGWsTKVVIPLVDIEEIEKlKGGANLFPNGIQVE 81
                           90       100
                   ....*....|....*....|....*....
gi 45597177    369 TKSKMTFLFANLKDRDFLVQRISDFLQKT 397
Cdd:pfam02893   82 TGSNDKFSFAGFVTRDEAIEFILALLKNA 110
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
299-394 1.81e-12

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: 64.32  E-value: 1.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  299 DERLDGHTSCTLWTpfNKLHIPGQMFISNNYICFASKEEDA-CHLIIPLREVTIVEKADSSSVLPSPLSISTKSKMTFLF 377
Cdd:cd10570    1 IEKLGVRFCCALRP--RKLPLEGTLYLSTYRLIFSSKADGDeTKLVIPLVDITDVEKIAGASFLPSGLIITCKDFRTIKF 78
                         90
                 ....*....|....*..
gi 45597177  378 ANLKDrDFLVQRISDFL 394
Cdd:cd10570   79 SFDSE-DEAVKVIARVL 94
PH-GRAM_C2-GRAM cd13219
C2 and GRAM domain-containing protein Pleckstrin Homology-Glucosyltransferases, Rab-like ...
154-207 2.23e-05

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: 44.76  E-value: 2.23e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45597177  154 EKLVNYYSCSYwKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEK 207
Cdd:cd13219    2 EFLINDFSCAL-KRKFLYQGRMFLSARHIGFHSNVFGKKTKFVFLWEDIEEIQE 54
PH-GRAM_GRAMDC4 cd13221
GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
171-228 5.36e-05

GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; GRAMDC4 is a membrane protein. Nothing is known about its function. Paralogs include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, and GRAMDC-like proteins. It contains a single PH-GRAM domain at its 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: 270041  Cd Length: 104  Bit Score: 43.48  E-value: 5.36e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45597177  171 RQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNATLLF-PES-----IRVDTRDQELFF 228
Cdd:cd13221   24 RNGRLYLTENYLCFESSSSSSKKNVVIPLTDITRIEKAKPYSFlPGSgmsieVSVSSADKPLFF 87
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
299-384 2.49e-04

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: 41.34  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597177  299 DERLDGHTSCTLwtpFNKLHIPGQMFISNNYICFASK----EEdacHLIIPLREVTIVEKADSSSVLPSPLSISTKSKmT 374
Cdd:cd13220    2 DERLIDDFSCAL---QRDILLQGRLYISENHLCFYSNifgwET---KLVIPFKDITSIEKKKTALIFPNAIEITTKGE-K 74
                         90
                 ....*....|
gi 45597177  375 FLFANLKDRD 384
Cdd:cd13220   75 YFFTSFLSRD 84
PH-GRAM2_AGT26 cd13216
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
153-207 9.19e-04

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: 39.49  E-value: 9.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 45597177  153 GEKLVNYYSCsYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEK 207
Cdd:cd13216    1 TEKLIASYYC-YLIRVLPVYGKLYVSNNYLCFRSLLPGVSTKMILPLRDIENVEK 54
PH-GRAM2_AGT26 cd13216
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
299-355 2.61e-03

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: 38.33  E-value: 2.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45597177  299 DERLDGHTSCTLwtpFNKLHIPGQMFISNNYICFAS-------KeedachLIIPLREVTIVEKA 355
Cdd:cd13216    1 TEKLIASYYCYL---IRVLPVYGKLYVSNNYLCFRSllpgvstK------MILPLRDIENVEKE 55
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
886-911 4.61e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.82  E-value: 4.61e-03
                            10        20
                    ....*....|....*....|....*.
gi 45597177     886 RMFRLLDENKDSLINFKEFVTGMSGM 911
Cdd:smart00054    4 EAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
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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