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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  153 GEKLVNYYSCSFWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDVTRLEKNATLLFPESIRVDTRDQELFFSMFL 232
Cdd:cd13351      1 EEKLVNYYSCSYWKGRVPRQGWLYLSVNHLCFYSFLLGKEAKLVIRWTDVTQLEKNNSLLLPDSIKVVTRDKEHYFSMFL 80

                           90
                   ....*....|....*....
gi 2023175286  233 NIGETFKLMEQLANLAMRQ 251
Cdd:cd13351     81 NISETFKLMEQLANLAMRQ 99

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  299 DERLDGHTGCTLWTPFNKLHIPGQMFISYNYICFASKEEDACRLIIPLREVTIVEKADSSSVLPSPL-SISTKSKMTFLF 377
Cdd:cd13354      1 DEKLDGSTDCTLWTPYNKRHVWGTLYLSQNYICFTSKVRDLVSLVIPLREVTSVEKADSSSVSLPNGiLITTKSKMTFLF 80

                           90
                   ....*....|....*..
gi 2023175286  378 ANLKDRDFLVQRISDFL 394
Cdd:cd13354     81 AQIKDRDFLVHKISDFL 97

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2023175286  859 RIDASQFRELFASLTPwacgshTPVLAGRMFRLLDQNKDSLINFKEFVTGMSGMYHGD 916
Cdd:COG5126     85 KISADEFRRLLTALGV------SEEEADELFARLDTDGDGKISFEEFVAAVRDYYTPD 136

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  153 GEKLVNYYSCSFWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDVTRLEKNATLLFPESIRVDTRDQELFFSMFL 232
Cdd:cd13351      1 EEKLVNYYSCSYWKGRVPRQGWLYLSVNHLCFYSFLLGKEAKLVIRWTDVTQLEKNNSLLLPDSIKVVTRDKEHYFSMFL 80

                           90
                   ....*....|....*....
gi 2023175286  233 NIGETFKLMEQLANLAMRQ 251
Cdd:cd13351     81 NISETFKLMEQLANLAMRQ 99

GTPase-activating protein [General function prediction only];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  498 RTAKTRELVLKGIPESLRGELWLLFSGAWNEMVTHPGYYAEL---VEKSMGKYSLATEEIERDLHRSMPEHPAFQNELGI 574
Cdd:COG5210    201 QLSKLRELIRKGIPNELRGDVWEFLLGIGFDLDKNPGLYERLlnlHREAKIPTQEIISQIEKDLSRTFPDNSLFQTEISI 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  575 --AALRRVLTAYAFRNPTIGYCQAMNIVTSVLLLY-GSEEEAFWLLVALCER-MLPDYYNTRVVGALVDQGIFEELTRDV 650
Cdd:COG5210    281 raENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVlESEEQAFWCLVKLLKNyGLPGYFLKNLSGLHRDLKVLDDLVEEL 360

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023175286  651 LPRLSEKMQELGV-ISSISLSWFLTLFLSVMPFESAVVIVDCFFYEGIKVILQVALAVLDANMEQLLDCSDEGEAMTVL 728
Cdd:COG5210    361 DPELYEHLLREGVvLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDLLL 439

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  299 DERLDGHTGCTLWTPFNKLHIPGQMFISYNYICFASKEEDACRLIIPLREVTIVEKADSSSVLPSPL-SISTKSKMTFLF 377
Cdd:cd13354      1 DEKLDGSTDCTLWTPYNKRHVWGTLYLSQNYICFTSKVRDLVSLVIPLREVTSVEKADSSSVSLPNGiLITTKSKMTFLF 80

                           90
                   ....*....|....*..
gi 2023175286  378 ANLKDRDFLVQRISDFL 394
Cdd:cd13354     81 AQIKDRDFLVHKISDFL 97

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 2023175286   149 GMPEGEKLVNYYSCSFWKgRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDVTRLEK 207
Cdd:smart00568    1 KLPEEEKLIADYSCYLSR-TGPVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIEK 58

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

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023175286   295 RLPKDERLDGHTGCTLWtpfNKLHIPGQMFISYNYICFAS-KEEDACRLIIPLREVTIVEK 354
Cdd:smart00568    1 KLPEEEKLIADYSCYLS---RTGPVQGRLYISNYRLCFRSnLPGKLTKVVIPLADITRIEK 58

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2023175286  859 RIDASQFRELFASLTPwacgshTPVLAGRMFRLLDQNKDSLINFKEFVTGMSGMYHGD 916
Cdd:COG5126     85 KISADEFRRLLTALGV------SEEEADELFARLDTDGDGKISFEEFVAAVRDYYTPD 136

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  153 GEKLVNYYSCSFWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDVTRLEKNATLLFPESIRVDTRDQELFFSMFL 232
Cdd:cd13351      1 EEKLVNYYSCSYWKGRVPRQGWLYLSVNHLCFYSFLLGKEAKLVIRWTDVTQLEKNNSLLLPDSIKVVTRDKEHYFSMFL 80

                           90
                   ....*....|....*....
gi 2023175286  233 NIGETFKLMEQLANLAMRQ 251
Cdd:cd13351     81 NISETFKLMEQLANLAMRQ 99

GTPase-activating protein [General function prediction only];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  498 RTAKTRELVLKGIPESLRGELWLLFSGAWNEMVTHPGYYAEL---VEKSMGKYSLATEEIERDLHRSMPEHPAFQNELGI 574
Cdd:COG5210    201 QLSKLRELIRKGIPNELRGDVWEFLLGIGFDLDKNPGLYERLlnlHREAKIPTQEIISQIEKDLSRTFPDNSLFQTEISI 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  575 --AALRRVLTAYAFRNPTIGYCQAMNIVTSVLLLY-GSEEEAFWLLVALCER-MLPDYYNTRVVGALVDQGIFEELTRDV 650
Cdd:COG5210    281 raENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVlESEEQAFWCLVKLLKNyGLPGYFLKNLSGLHRDLKVLDDLVEEL 360

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023175286  651 LPRLSEKMQELGV-ISSISLSWFLTLFLSVMPFESAVVIVDCFFYEGIKVILQVALAVLDANMEQLLDCSDEGEAMTVL 728
Cdd:COG5210    361 DPELYEHLLREGVvLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLDLLL 439

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  154 EKLVNYYSCSFWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDVTRLEKNATLLFPESIRVDTRDQELFFSMFLN 233
Cdd:cd13217      2 EKLVTYYSCSYWKGRVPRQGWLYLSINHLCFYSFLLGSESKLIIRWTEVSDLERTSNTILTDTIKVNTRSKEHPFSMFLN 81

                           90
                   ....*....|....*...
gi 2023175286  234 IGETFKLMEQLANLAMRQ 251
Cdd:cd13217     82 ISETFKLMEQLAQIPDRP 99

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  154 EKLVNYYSCSFWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDVTRLEKNATLLFPESIRVDTRDQELFFSMFLN 233
Cdd:cd13349      2 EKLVTYYSCCCWKGRVPRQGWLYLSINHLCFYSFFLGKELKLLIPWVDVQKLERTSNVFMTDTIRVTTQNKERDFSMFLN 81

                           90
                   ....*....|....*...
gi 2023175286  234 IGETFKLMEQLANLAMRQ 251
Cdd:cd13349     82 IDEVFRIMEQLADVTLRR 99

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  299 DERLDGHTGCTLWTPFNKLHIPGQMFISYNYICFASKEEDACRLIIPLREVTIVEKADSSSVLPSPLSISTKSKMTFLFA 378
Cdd:cd13218      1 EEKLKEVHDCFLWTPFSHFHTHGKMFISENYICFASKEGNLCSVIIPLREVLAIEKTNDSSVLPKPVIISIKGKMAFRFS 80

                           90
                   ....*....|....*.
gi 2023175286  379 NLKDRDFLVQRISDFL 394
Cdd:cd13218     81 ELKDRDELVAKLRLKL 96

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  300 ERLDGHTGCTLWTPFNKLHIPGQMFISYNYICFASKEEDACRLIIPLREVTIVEKADSSSVLPSPLSISTKSKMTFLFAN 379
Cdd:cd13353      2 EKLHEVVDCSLWTPFSRCHTAGRMYTSDSYICFASKEDGSCNVILPLREVVSIEKMEDTSLLPNPIIVSIRSKMAFQFIE 81

                   ....*....
gi 2023175286  380 LKDRDFLVQ 388
Cdd:cd13353     82 LKDRDSLVE 90

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 2023175286   149 GMPEGEKLVNYYSCSFWKgRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDVTRLEK 207
Cdd:smart00568    1 KLPEEEKLIADYSCYLSR-TGPVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIEK 58

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023175286  154 EKLVNYYSCSFWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDVTRLEKNATLLFPES-IRVDTRDQELFFSMFL 232
Cdd:cd10570      2 EKLGVRFCCALRPRKLPLEGTLYLSTYRLIFSSKADGDETKLVIPLVDITDVEKIAGASFLPSgLIITCKDFRTIKFSFD 81

                   ....*....
gi 2023175286  233 NIGETFKLM 241
Cdd:cd10570     82 SEDEAVKVI 90

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

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023175286   295 RLPKDERLDGHTGCTLWtpfNKLHIPGQMFISYNYICFAS-KEEDACRLIIPLREVTIVEK 354
Cdd:smart00568    1 KLPEEEKLIADYSCYLS---RTGPVQGRLYISNYRLCFRSnLPGKLTKVVIPLADITRIEK 58

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2023175286  154 EKLVNYYSCSFwKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDVTRLEK 207
Cdd:cd13219      2 EFLINDFSCAL-KRKFLYQGRMFLSARHIGFHSNVFGKKTKFVFLWEDIEEIQE 54

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2023175286  153 GEKLVNYYSCSFWKGrVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDVTRLEK 207
Cdd:cd13216      1 TEKLIASYYCYLIRV-LPVYGKLYVSNNYLCFRSLLPGVSTKMILPLRDIENVEK 54

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.

                            10        20
                    ....*....|....*....|....*.
gi 2023175286   887 RMFRLLDQNKDSLINFKEFVTGMSGM 912
Cdd:smart00054    4 EAFRLFDKDGDGKIDFEEFKDLLKAL 29

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.

                           10        20
                   ....*....|....*....|....*.
gi 2023175286  887 RMFRLLDQNKDSLINFKEFVTGMSGM 912
Cdd:pfam00036    4 EIFRLFDKDGDGKIDFEEFKELLKKL 29