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Conserved domains on  [gi|18399985|ref|NP_565538|]
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GRAM domain family protein [Arabidopsis thaliana]

Protein Classification

GEM family protein( domain architecture ID 10192383)

GEM (GLABRA2 expression modulator) family GRAM domain-containing protein similar to Arabidopsis thaliana GEM-like protein 5

CATH:  2.30.29.30
PubMed:  11050430
SCOP:  4000903

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-GRAM_GEM cd13222
GLABRA 2 expression modulator (GEM) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 186-292 3.52e-64

GLABRA 2 expression modulator (GEM) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; GEM interacts with CDT1, a pre-replication complex component that is involved in DNA replication, and with TTG1 (Transparent Testa GLABRA 1), a transcriptional regulator of epidermal cell fate. GEM controls the level of histone H3K9 methylation at the promoters of the GLABRA 2 and CAPRICE (CPC) genes, which are essential for epidermis patterning. GEM also regulates cell division in different root cell types. GEM regulates proliferation-differentiation decisions by integrating DNA replication, cell division and transcriptional controls. 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: 270042  Cd Length: 109  Bit Score: 197.18  E-value: 3.52e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399985 186 EEQLLNSFACYLSTSAGPVMGVLYISSAKLAYCSDNPLSYKN-GDQTEWSYYKVVIPLHQLKAVNPSASIVNPAEKYIQV 264
Cdd:cd13222   1 EEKLLKTFACYLSTSTGPVAGVLYISTKKIAFCSDRPLSFTSpSGQTSWSYYKVVIPLEQLKSVNPSTNVEKPAEKYIQI 80

                        90       100
                ....*....|....*....|....*...
gi 18399985 265 ISVDNHEFWFMGFLNYDGAVTSLQDSLQ 292
Cdd:cd13222  81 VTVDGHEFWFMGFVNYDKAFKNLQEALR 108
 
Name Accession Description Interval E-value
PH-GRAM_GEM cd13222
GLABRA 2 expression modulator (GEM) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 186-292 3.52e-64

GLABRA 2 expression modulator (GEM) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; GEM interacts with CDT1, a pre-replication complex component that is involved in DNA replication, and with TTG1 (Transparent Testa GLABRA 1), a transcriptional regulator of epidermal cell fate. GEM controls the level of histone H3K9 methylation at the promoters of the GLABRA 2 and CAPRICE (CPC) genes, which are essential for epidermis patterning. GEM also regulates cell division in different root cell types. GEM regulates proliferation-differentiation decisions by integrating DNA replication, cell division and transcriptional controls. 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: 270042  Cd Length: 109  Bit Score: 197.18  E-value: 3.52e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399985 186 EEQLLNSFACYLSTSAGPVMGVLYISSAKLAYCSDNPLSYKN-GDQTEWSYYKVVIPLHQLKAVNPSASIVNPAEKYIQV 264
Cdd:cd13222   1 EEKLLKTFACYLSTSTGPVAGVLYISTKKIAFCSDRPLSFTSpSGQTSWSYYKVVIPLEQLKSVNPSTNVEKPAEKYIQI 80

                        90       100
                ....*....|....*....|....*...
gi 18399985 265 ISVDNHEFWFMGFLNYDGAVTSLQDSLQ 292
Cdd:cd13222  81 VTVDGHEFWFMGFVNYDKAFKNLQEALR 108
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 175-292 7.59e-19

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: 80.10  E-value: 7.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399985   175 KIFRQTFETDPEEQLLNSFACYLSTSAGPVMGVLYISSAKLAYCSDNPlsykngdqtEWSyYKVVIPLHQLKAVNPSASI 254
Cdd:pfam02893   1 ELFRKKFKLPPEERLIASYSCYLNRDGGPVQGRLYLTNYRLCFRSLPK---------GWS-TKVVIPLVDIEEIEKLKGG 70

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 18399985   255 VNPAEKYIQVISVDNHEFWFMGFLNYDGAVTSLQDSLQ 292
Cdd:pfam02893  71 ANLFPNGIQVETGSNDKFSFAGFVTRDEAIEFILALLK 108
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
185-251 5.57e-12

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 59.91  E-value: 5.57e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18399985    185 PEEQLLNSFACYLSTsAGPVMGVLYISSAKLAYCSDNPLSYKngdqtewsyyKVVIPLHQLKAVNPS 251
Cdd:smart00568   4 EEEKLIADYSCYLSR-TGPVQGRLYISNYRLCFRSNLPGKLT----------KVVIPLADITRIEKS 59
 
Name Accession Description Interval E-value
PH-GRAM_GEM cd13222
GLABRA 2 expression modulator (GEM) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 186-292 3.52e-64

GLABRA 2 expression modulator (GEM) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; GEM interacts with CDT1, a pre-replication complex component that is involved in DNA replication, and with TTG1 (Transparent Testa GLABRA 1), a transcriptional regulator of epidermal cell fate. GEM controls the level of histone H3K9 methylation at the promoters of the GLABRA 2 and CAPRICE (CPC) genes, which are essential for epidermis patterning. GEM also regulates cell division in different root cell types. GEM regulates proliferation-differentiation decisions by integrating DNA replication, cell division and transcriptional controls. 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: 270042  Cd Length: 109  Bit Score: 197.18  E-value: 3.52e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399985 186 EEQLLNSFACYLSTSAGPVMGVLYISSAKLAYCSDNPLSYKN-GDQTEWSYYKVVIPLHQLKAVNPSASIVNPAEKYIQV 264
Cdd:cd13222   1 EEKLLKTFACYLSTSTGPVAGVLYISTKKIAFCSDRPLSFTSpSGQTSWSYYKVVIPLEQLKSVNPSTNVEKPAEKYIQI 80

                        90       100
                ....*....|....*....|....*...
gi 18399985 265 ISVDNHEFWFMGFLNYDGAVTSLQDSLQ 292
Cdd:cd13222  81 VTVDGHEFWFMGFVNYDKAFKNLQEALR 108
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 175-292 7.59e-19

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: 80.10  E-value: 7.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399985   175 KIFRQTFETDPEEQLLNSFACYLSTSAGPVMGVLYISSAKLAYCSDNPlsykngdqtEWSyYKVVIPLHQLKAVNPSASI 254
Cdd:pfam02893   1 ELFRKKFKLPPEERLIASYSCYLNRDGGPVQGRLYLTNYRLCFRSLPK---------GWS-TKVVIPLVDIEEIEKLKGG 70

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 18399985   255 VNPAEKYIQVISVDNHEFWFMGFLNYDGAVTSLQDSLQ 292
Cdd:pfam02893  71 ANLFPNGIQVETGSNDKFSFAGFVTRDEAIEFILALLK 108
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 186-291 2.84e-15

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


Pssm-ID: 275393  Cd Length: 94  Bit Score: 70.10  E-value: 2.84e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399985 186 EEQLLNSFACYLSTSAGPVMGVLYISSAKLAYCSDNPlsykngdqteWSYYKVVIPLHQLKAVNPSASIVNPAeKYIQVI 265
Cdd:cd10570   1 IEKLGVRFCCALRPRKLPLEGTLYLSTYRLIFSSKAD----------GDETKLVIPLVDITDVEKIAGASFLP-SGLIIT 69

                        90       100
                ....*....|....*....|....*.
gi 18399985 266 SVDnHEFWFMGFLNYDGAVTSLQDSL 291
Cdd:cd10570  70 CKD-FRTIKFSFDSEDEAVKVIARVL 94
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
185-251 5.57e-12

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 59.91  E-value: 5.57e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18399985    185 PEEQLLNSFACYLSTsAGPVMGVLYISSAKLAYCSDNPLSYKngdqtewsyyKVVIPLHQLKAVNPS 251
Cdd:smart00568   4 EEEKLIADYSCYLSR-TGPVQGRLYISNYRLCFRSNLPGKLT----------KVVIPLADITRIEKS 59
 
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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