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Conserved domains on  [gi|1057866282|ref|NP_001317277|]
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TBC1 domain family member 8 isoform 1 [Homo sapiens]

Protein Classification

TBC domain-containing protein( domain architecture ID 10193407)

TBC (Tre-2/Bub2/Cdc1) domain-containing protein may function as a GTPase activator protein of Rab-like small GTPases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-GRAM1_TBC1D8 cd13349
TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) ...
 171-269 5.40e-65

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: 214.33  E-value: 5.40e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  171 AEKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQKLERTSNVFLTDTIRITTQNKERDFSMFL 250
Cdd:cd13349      1 AEKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLLIPWVDVQKLERTSNVFMTDTIRVTTQNKERDFSMFL 80

                           90
                   ....*....|....*....
gi 1057866282  251 NLDEVFKVMEQLADVTLRR 269
Cdd:cd13349     81 NIDEVFRIMEQLADVTLRR 99
PH-GRAM2_TBC1D8 cd13353
TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) ...
 311-406 4.98e-59

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: 197.37  E-value: 4.98e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  311 KEKLHAVVDCSLWTPFSRCHTTGRMFASDSYICFASREDGCCKIILPLREVVSIEKMEDTSLLPHPIIVSIRSKVAFQFI 390
Cdd:cd13353      1 KEKLHEVVDCSLWTPFSRCHTAGRMYTSDSYICFASKEDGSCNVILPLREVVSIEKMEDTSLLPNPIIVSIRSKMAFQFI 80

                           90
                   ....*....|....*.
gi 1057866282  391 ELRDRDSLVEALLARL 406
Cdd:cd13353     81 ELKDRDSLVESLLARL 96
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 520-726 1.19e-51

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: 180.97  E-value: 1.19e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282   520 GIPESLRGRLWLLFSDA-VTDLASHPGYYGNLVEESLGKCCLVTEEIERDLHRSLPEHPAFQ--NETGIAALRRVLTAYA 596
Cdd:smart00164    4 GVPPSLRGVVWKLLLNAqPMDTSADKDLYSRLLKETAPDDKSIVHQIEKDLRRTFPEHSFFQdkEGPGQESLRRVLKAYA 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282   597 HRNPKIGYCQSMNILTSVLLLY-TKEEEAFWLLVAVCERMLPDYFNHRVIGAQVDQSVFEELIKGHLPELAEHMNDLSAL 675
Cdd:smart00164   84 LYNPEVGYCQGMNFLAAPLLLVmEDEEDAFWCLVKLMERYGPNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKDLGIT 163

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1057866282   676 ASV-SLSWFLTLFLSIMPLESAVNVVDCFFYDGIKAIFQLGLAVLEANAEDL 726
Cdd:smart00164  164 PSLyALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVL 215
 
Name Accession Description Interval E-value
PH-GRAM1_TBC1D8 cd13349
TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) ...
 171-269 5.40e-65

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: 214.33  E-value: 5.40e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  171 AEKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQKLERTSNVFLTDTIRITTQNKERDFSMFL 250
Cdd:cd13349      1 AEKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLLIPWVDVQKLERTSNVFMTDTIRVTTQNKERDFSMFL 80

                           90
                   ....*....|....*....
gi 1057866282  251 NLDEVFKVMEQLADVTLRR 269
Cdd:cd13349     81 NIDEVFRIMEQLADVTLRR 99
PH-GRAM2_TBC1D8 cd13353
TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) ...
 311-406 4.98e-59

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: 197.37  E-value: 4.98e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  311 KEKLHAVVDCSLWTPFSRCHTTGRMFASDSYICFASREDGCCKIILPLREVVSIEKMEDTSLLPHPIIVSIRSKVAFQFI 390
Cdd:cd13353      1 KEKLHEVVDCSLWTPFSRCHTAGRMYTSDSYICFASKEDGSCNVILPLREVVSIEKMEDTSLLPNPIIVSIRSKMAFQFI 80

                           90
                   ....*....|....*.
gi 1057866282  391 ELRDRDSLVEALLARL 406
Cdd:cd13353     81 ELKDRDSLVESLLARL 96
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 520-726 1.19e-51

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: 180.97  E-value: 1.19e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282   520 GIPESLRGRLWLLFSDA-VTDLASHPGYYGNLVEESLGKCCLVTEEIERDLHRSLPEHPAFQ--NETGIAALRRVLTAYA 596
Cdd:smart00164    4 GVPPSLRGVVWKLLLNAqPMDTSADKDLYSRLLKETAPDDKSIVHQIEKDLRRTFPEHSFFQdkEGPGQESLRRVLKAYA 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282   597 HRNPKIGYCQSMNILTSVLLLY-TKEEEAFWLLVAVCERMLPDYFNHRVIGAQVDQSVFEELIKGHLPELAEHMNDLSAL 675
Cdd:smart00164   84 LYNPEVGYCQGMNFLAAPLLLVmEDEEDAFWCLVKLMERYGPNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKDLGIT 163

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1057866282   676 ASV-SLSWFLTLFLSIMPLESAVNVVDCFFYDGIKAIFQLGLAVLEANAEDL 726
Cdd:smart00164  164 PSLyALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVL 215
COG5210 COG5210
GTPase-activating protein [General function prediction only];
493-751 2.20e-49

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 183.46  E-value: 2.20e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  493 LWNDHFVEYGRTVCMFRTEKIRKLVAMGIPESLRGRLWLLFSDAVTDLASHPGYYG---NLVEESLGKCCLVTEEIERDL 569
Cdd:COG5210    185 LWISYLDPNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFLLGIGFDLDKNPGLYErllNLHREAKIPTQEIISQIEKDL 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  570 HRSLPEHPAFQNETGIAA--LRRVLTAYAHRNPKIGYCQSMNILTSVLLLY-TKEEEAFWLLVAVCER-MLPDYFNHRVI 645
Cdd:COG5210    265 SRTFPDNSLFQTEISIRAenLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVlESEEQAFWCLVKLLKNyGLPGYFLKNLS 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  646 GAQVDQSVFEELIKGHLPELAEHMND-LSALASVSLSWFLTLFLSIMPLESAVNVVDCFFYDGIKAIFQLGLAVLEANAE 724
Cdd:COG5210    345 GLHRDLKVLDDLVEELDPELYEHLLReGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRD 424

                          250       260
                   ....*....|....*....|....*..
gi 1057866282  725 DLCSSKDDGQALMILSRFLDHIKNEDS 751
Cdd:COG5210    425 KLLKLDSDELLDLLLKQLFLHSGKEAW 451
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 565-726 8.20e-43

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: 153.95  E-value: 8.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  565 IERDLHRSLPEHPAFQNETGIAALRRVLTAYAHRNPKIGYCQSMNILTSVLLLYT-KEEEAFWLLVAVCER-MLPDYFNH 642
Cdd:pfam00566   12 IEKDVPRTFPHSFFFDNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVYlDEEDAFWCFVSLLENyLLRDFYTP 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  643 RVIGAQVDQSVFEELIKGHLPELAEHMNDLSALASV-SLSWFLTLFLSIMPLESAVNVVDCFFYDGIKA-IFQLGLAVLE 720
Cdd:pfam00566   92 DFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLfASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVALAILK 171


                   ....*.
gi 1057866282  721 ANAEDL 726
Cdd:pfam00566  172 RFREEL 177
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 300-411 5.66e-23

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: 94.74  E-value: 5.66e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  300 EFFRAFFRLPRKEKLHAVVDCSLWTPFsrCHTTGRMFASDSYICFASREDGC-CKIILPLREVVSIEKMEDTSLLPH-PI 377
Cdd:pfam02893    1 ELFRKKFKLPPEERLIASYSCYLNRDG--GPVQGRLYLTNYRLCFRSLPKGWsTKVVIPLVDIEEIEKLKGGANLFPnGI 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1057866282  378 IVSIRSKVAFQFIELRDRDSLVEALLARLKQVHA 411
Cdd:pfam02893   79 QVETGSNDKFSFAGFVTRDEAIEFILALLKNAHP 112
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 161-262 2.08e-16

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: 76.25  E-value: 2.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  161 KFEARFNFPEAEKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQKLERTSN--VFLTDTIRIT 238
Cdd:pfam02893    2 LFRKKFKLPPEERLIASYSCYLNRDGGPVQGRLYLTNYRLCFRSLPKGWSTKVVIPLVDIEEIEKLKGgaNLFPNGIQVE 81

                           90       100
                   ....*....|....*....|....*
gi 1057866282  239 TQNKERD-FSMFLNLDEVFKVMEQL 262
Cdd:pfam02893   82 TGSNDKFsFAGFVTRDEAIEFILAL 106
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
169-227 2.13e-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: 2.13e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1057866282   169 PEAEKLVTYYSCCCWKgRVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQKLERTS 227
Cdd:smart00568    3 PEEEKLIADYSCYLSR-TGPVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIEKST 60
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
307-367 3.05e-14

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 68.00  E-value: 3.05e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057866282   307 RLPRKEKLHAVVDCSLWTpfsRCHTTGRMFASDSYICFAS-REDGCCKIILPLREVVSIEKM 367
Cdd:smart00568    1 KLPEEEKLIADYSCYLSR---TGPVQGRLYISNYRLCFRSnLPGKLTKVVIPLADITRIEKS 59
 
Name Accession Description Interval E-value
PH-GRAM1_TBC1D8 cd13349
TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) ...
 171-269 5.40e-65

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: 214.33  E-value: 5.40e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  171 AEKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQKLERTSNVFLTDTIRITTQNKERDFSMFL 250
Cdd:cd13349      1 AEKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLLIPWVDVQKLERTSNVFMTDTIRVTTQNKERDFSMFL 80

                           90
                   ....*....|....*....
gi 1057866282  251 NLDEVFKVMEQLADVTLRR 269
Cdd:cd13349     81 NIDEVFRIMEQLADVTLRR 99
PH-GRAM2_TBC1D8 cd13353
TBC1 domain family member 8 (TBC1D8; also called Vascular Rab-GAP/TBC-containing protein) ...
 311-406 4.98e-59

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: 197.37  E-value: 4.98e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  311 KEKLHAVVDCSLWTPFSRCHTTGRMFASDSYICFASREDGCCKIILPLREVVSIEKMEDTSLLPHPIIVSIRSKVAFQFI 390
Cdd:cd13353      1 KEKLHEVVDCSLWTPFSRCHTAGRMYTSDSYICFASKEDGSCNVILPLREVVSIEKMEDTSLLPNPIIVSIRSKMAFQFI 80

                           90
                   ....*....|....*.
gi 1057866282  391 ELRDRDSLVEALLARL 406
Cdd:cd13353     81 ELKDRDSLVESLLARL 96
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 520-726 1.19e-51

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: 180.97  E-value: 1.19e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282   520 GIPESLRGRLWLLFSDA-VTDLASHPGYYGNLVEESLGKCCLVTEEIERDLHRSLPEHPAFQ--NETGIAALRRVLTAYA 596
Cdd:smart00164    4 GVPPSLRGVVWKLLLNAqPMDTSADKDLYSRLLKETAPDDKSIVHQIEKDLRRTFPEHSFFQdkEGPGQESLRRVLKAYA 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282   597 HRNPKIGYCQSMNILTSVLLLY-TKEEEAFWLLVAVCERMLPDYFNHRVIGAQVDQSVFEELIKGHLPELAEHMNDLSAL 675
Cdd:smart00164   84 LYNPEVGYCQGMNFLAAPLLLVmEDEEDAFWCLVKLMERYGPNFYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKDLGIT 163

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1057866282   676 ASV-SLSWFLTLFLSIMPLESAVNVVDCFFYDGIKAIFQLGLAVLEANAEDL 726
Cdd:smart00164  164 PSLyALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVL 215
PH-GRAM1_TCB1D8_TCB1D9_family cd13217
TCB1D8 and TCB1D9 family Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators ...
 171-269 3.54e-51

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: 174.93  E-value: 3.54e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  171 AEKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQKLERTSNVFLTDTIRITTQNKERDFSMFL 250
Cdd:cd13217      1 EEKLVTYYSCSYWKGRVPRQGWLYLSINHLCFYSFLLGSESKLIIRWTEVSDLERTSNTILTDTIKVNTRSKEHPFSMFL 80

                           90
                   ....*....|....*....
gi 1057866282  251 NLDEVFKVMEQLADVTLRR 269
Cdd:cd13217     81 NISETFKLMEQLAQIPDRP 99
COG5210 COG5210
GTPase-activating protein [General function prediction only];
493-751 2.20e-49

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 183.46  E-value: 2.20e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  493 LWNDHFVEYGRTVCMFRTEKIRKLVAMGIPESLRGRLWLLFSDAVTDLASHPGYYG---NLVEESLGKCCLVTEEIERDL 569
Cdd:COG5210    185 LWISYLDPNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFLLGIGFDLDKNPGLYErllNLHREAKIPTQEIISQIEKDL 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  570 HRSLPEHPAFQNETGIAA--LRRVLTAYAHRNPKIGYCQSMNILTSVLLLY-TKEEEAFWLLVAVCER-MLPDYFNHRVI 645
Cdd:COG5210    265 SRTFPDNSLFQTEISIRAenLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVlESEEQAFWCLVKLLKNyGLPGYFLKNLS 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  646 GAQVDQSVFEELIKGHLPELAEHMND-LSALASVSLSWFLTLFLSIMPLESAVNVVDCFFYDGIKAIFQLGLAVLEANAE 724
Cdd:COG5210    345 GLHRDLKVLDDLVEELDPELYEHLLReGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRD 424

                          250       260
                   ....*....|....*....|....*..
gi 1057866282  725 DLCSSKDDGQALMILSRFLDHIKNEDS 751
Cdd:COG5210    425 KLLKLDSDELLDLLLKQLFLHSGKEAW 451
PH-GRAM1_TCB1D9_TCB1D9B cd13351
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
 172-269 9.86e-49

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: 167.95  E-value: 9.86e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  172 EKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQKLERTSNVFLTDTIRITTQNKERDFSMFLN 251
Cdd:cd13351      2 EKLVNYYSCSYWKGRVPRQGWLYLSVNHLCFYSFLLGKEAKLVIRWTDVTQLEKNNSLLLPDSIKVVTRDKEHYFSMFLN 81

                           90
                   ....*....|....*...
gi 1057866282  252 LDEVFKVMEQLADVTLRR 269
Cdd:cd13351     82 ISETFKLMEQLANLAMRQ 99
PH-GRAM2_TCB1D8_TCB1D9_family cd13218
TCB1D8 and TCB1D9 family Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators ...
 311-406 7.53e-46

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: 159.68  E-value: 7.53e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  311 KEKLHAVVDCSLWTPFSRCHTTGRMFASDSYICFASREDGCCKIILPLREVVSIEKMEDTSLLPHPIIVSIRSKVAFQFI 390
Cdd:cd13218      1 EEKLKEVHDCFLWTPFSHFHTHGKMFISENYICFASKEGNLCSVIIPLREVLAIEKTNDSSVLPKPVIISIKGKMAFRFS 80

                           90
                   ....*....|....*.
gi 1057866282  391 ELRDRDSLVEALLARL 406
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 ...
 565-726 8.20e-43

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: 153.95  E-value: 8.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  565 IERDLHRSLPEHPAFQNETGIAALRRVLTAYAHRNPKIGYCQSMNILTSVLLLYT-KEEEAFWLLVAVCER-MLPDYFNH 642
Cdd:pfam00566   12 IEKDVPRTFPHSFFFDNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVYlDEEDAFWCFVSLLENyLLRDFYTP 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  643 RVIGAQVDQSVFEELIKGHLPELAEHMNDLSALASV-SLSWFLTLFLSIMPLESAVNVVDCFFYDGIKA-IFQLGLAVLE 720
Cdd:pfam00566   92 DFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLfASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVALAILK 171


                   ....*.
gi 1057866282  721 ANAEDL 726
Cdd:pfam00566  172 RFREEL 177
PH-GRAM1_TBC1D8B cd13350
TBC1 domain family member 8B (TBC1D8B) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 172-269 2.90e-41

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: 146.61  E-value: 2.90e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  172 EKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQKLERTSNVFLTDTIRITTQNKERDFSMFLN 251
Cdd:cd13350      2 EKLVTYYSCSYWRGRVPCQGWLYLSTNFLSFYSFLLGSEIKLIISWDEISKLEKTSNVILTESIHVCSRGEDHYFSMFLH 81

                           90
                   ....*....|....*...
gi 1057866282  252 LDEVFKVMEQLADVTLRR 269
Cdd:cd13350     82 INETFLLMEQLANYAVRR 99
PH-GRAM2_TCB1D9_TCB1D9B cd13354
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
 312-400 7.86e-26

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: 102.34  E-value: 7.86e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  312 EKLHAVVDCSLWTPFSRCHTTGRMFASDSYICFASREDGCCKIILPLREVVSIEKMEDTS-LLPHPIIVSIRSKVAFQFI 390
Cdd:cd13354      2 EKLDGSTDCTLWTPYNKRHVWGTLYLSQNYICFTSKVRDLVSLVIPLREVTSVEKADSSSvSLPNGILITTKSKMTFLFA 81

                           90
                   ....*....|
gi 1057866282  391 ELRDRDSLVE 400
Cdd:cd13354     82 QIKDRDFLVH 91
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 300-411 5.66e-23

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: 94.74  E-value: 5.66e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  300 EFFRAFFRLPRKEKLHAVVDCSLWTPFsrCHTTGRMFASDSYICFASREDGC-CKIILPLREVVSIEKMEDTSLLPH-PI 377
Cdd:pfam02893    1 ELFRKKFKLPPEERLIASYSCYLNRDG--GPVQGRLYLTNYRLCFRSLPKGWsTKVVIPLVDIEEIEKLKGGANLFPnGI 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1057866282  378 IVSIRSKVAFQFIELRDRDSLVEALLARLKQVHA 411
Cdd:pfam02893   79 QVETGSNDKFSFAGFVTRDEAIEFILALLKNAHP 112
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 170-262 1.61e-20

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: 87.18  E-value: 1.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  170 EAEKLVTYYSCCcWKGRVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQKLERTSNVFL-TDTIRITTQNKERDFSM 248
Cdd:cd13220      1 EDERLIDDFSCA-LQRDILLQGRLYISENHLCFYSNIFGWETKLVIPFKDITSIEKKKTALIfPNAIEITTKGEKYFFTS 79

                           90
                   ....*....|....
gi 1057866282  249 FLNLDEVFKVMEQL 262
Cdd:cd13220     80 FLSRDSAYKLLTRV 93
PH-GRAM2_TBC1D8B cd13352
TBC1 domain family member 8B (TBC1D8B) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 311-405 1.64e-20

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: 87.21  E-value: 1.64e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  311 KEKLHAVVDCSLWTPFSRCHTTGRMFASDSYICFASREDGCCKIILPLREVVSIEKMEDTSllpHPIIVSIRSKVAFQFI 390
Cdd:cd13352      1 EETLKEVHECFLWVPFSHFNTHGKMCISENYICFASQDGSLCSVIIPLREVLSIDKTDDSS---RAVTISTKGKRAFRFT 77

                           90
                   ....*....|....*
gi 1057866282  391 ELRDRDSLVEALLAR 405
Cdd:cd13352     78 EVKDFEQLVAKLRLK 92
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 161-262 2.08e-16

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: 76.25  E-value: 2.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  161 KFEARFNFPEAEKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQKLERTSN--VFLTDTIRIT 238
Cdd:pfam02893    2 LFRKKFKLPPEERLIASYSCYLNRDGGPVQGRLYLTNYRLCFRSLPKGWSTKVVIPLVDIEEIEKLKGgaNLFPNGIQVE 81

                           90       100
                   ....*....|....*....|....*
gi 1057866282  239 TQNKERD-FSMFLNLDEVFKVMEQL 262
Cdd:pfam02893   82 TGSNDKFsFAGFVTRDEAIEFILAL 106
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
169-227 2.13e-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: 2.13e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1057866282   169 PEAEKLVTYYSCCCWKgRVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQKLERTS 227
Cdd:smart00568    3 PEEEKLIADYSCYLSR-TGPVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIEKST 60
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
307-367 3.05e-14

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 68.00  E-value: 3.05e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057866282   307 RLPRKEKLHAVVDCSLWTpfsRCHTTGRMFASDSYICFAS-REDGCCKIILPLREVVSIEKM 367
Cdd:smart00568    1 KLPEEEKLIADYSCYLSR---TGPVQGRLYISNYRLCFRSnLPGKLTKVVIPLADITRIEKS 59
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 172-259 2.94e-11

Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275393  Cd Length: 94  Bit Score: 60.86  E-value: 2.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  172 EKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQKLE-RTSNVFLTDTIRITTQNKERDFSMFL 250
Cdd:cd10570      2 EKLGVRFCCALRPRKLPLEGTLYLSTYRLIFSSKADGDETKLVIPLVDITDVEkIAGASFLPSGLIITCKDFRTIKFSFD 81


                   ....*....
gi 1057866282  251 NLDEVFKVM 259
Cdd:cd10570     82 SEDEAVKVI 90
PH-GRAM_C2-GRAM cd13219
C2 and GRAM domain-containing protein Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 172-238 1.99e-08

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: 53.24  E-value: 1.99e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057866282  172 EKLVTYYSCCCwKGRVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQKLERTSNVFLTDTIRIT 238
Cdd:cd13219      2 EFLINDFSCAL-KRKFLYQGRMFLSARHIGFHSNVFGKKTKFVFLWEDIEEIQESPHSLINPAIVIT 67
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 312-406 9.79e-07

Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275393  Cd Length: 94  Bit Score: 48.15  E-value: 9.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866282  312 EKLHAVVDCSLWTpfSRCHTTGRMFASDSYICFASREDGC-CKIILPLREVVSIEKMEDTSLLPHPIIVSIR--SKVAFQ 388
Cdd:cd10570      2 EKLGVRFCCALRP--RKLPLEGTLYLSTYRLIFSSKADGDeTKLVIPLVDITDVEKIAGASFLPSGLIITCKdfRTIKFS 79

                           90
                   ....*....|....*...
gi 1057866282  389 FIElrdRDSLVEALLARL 406
Cdd:cd10570     80 FDS---EDEAVKVIARVL 94
PH-GRAM2_AGT26 cd13216
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
 172-221 1.89e-06

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: 47.19  E-value: 1.89e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1057866282  172 EKLVTYYSCCCWKGrVPRQGWLYLSINHLCFYSFFLGKELKLVVPWVDIQ 221
Cdd:cd13216      2 EKLIASYYCYLIRV-LPVYGKLYVSNNYLCFRSLLPGVSTKMILPLRDIE 50
PH-GRAM2_TCB1D9_TCB1D9B cd13354
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
 191-254 8.69e-04

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: 39.55  E-value: 8.69e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1057866282  191 GWLYLSINHLCFYSFFLGkELKLVVPWVDIQKLER--TSNVFLTDTIRITTQNKerDFSMFLNLDE 254
Cdd:cd13354     23 GTLYLSQNYICFTSKVRD-LVSLVIPLREVTSVEKadSSSVSLPNGILITTKSK--MTFLFAQIKD 85
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 333-397 1.60e-03

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: 39.03  E-value: 1.60e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057866282  333 GRMFASDSYICFAS----REDgccKIILPLREVVSIEKMEDTSLLPHPIIVSIRSKvAFQFIELRDRDS 397
Cdd:cd13220     21 GRLYISENHLCFYSnifgWET---KLVIPFKDITSIEKKKTALIFPNAIEITTKGE-KYFFTSFLSRDS 85
PH-GRAM2_AGT26 cd13216
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
 333-394 5.38e-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: 37.18  E-value: 5.38e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057866282  333 GRMFASDSYICFASREDGC-CKIILPLREVVSIEKMEDTSLLPHPIIVSIRS----KVAFQFIELRD 394
Cdd:cd13216     20 GKLYVSNNYLCFRSLLPGVsTKMILPLRDIENVEKEKGFRFGYSGLVIVIKGheelFFEFSSKSSRD 86
 
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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