NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2065857414|gb|KAG7623534|]
View 

GRAM domain [Arabidopsis suecica]

Protein Classification

PH domain-containing protein( domain architecture ID 106840)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  22728242|17233582|15493994

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 192-246 1.02e-27

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13222:

Pssm-ID: 473070  Cd Length: 109  Bit Score: 102.42  E-value: 1.02e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2065857414 192 EEQLQNSFACYLSTSAGPVMGVLYVSTAKLAYCSDNPLSYKNS-GQTEWSYYKVIL 246
Cdd:cd13222     1 EEKLLKTFACYLSTSTGPVAGVLYISTKKIAFCSDRPLSFTSPsGQTSWSYYKVVI 56
 
Name Accession Description Interval E-value
PH-GRAM_GEM cd13222
GLABRA 2 expression modulator (GEM) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 192-246 1.02e-27

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: 102.42  E-value: 1.02e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2065857414 192 EEQLQNSFACYLSTSAGPVMGVLYVSTAKLAYCSDNPLSYKNS-GQTEWSYYKVIL 246
Cdd:cd13222     1 EEKLLKTFACYLSTSTGPVAGVLYISTKKIAFCSDRPLSFTSPsGQTSWSYYKVVI 56
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
191-233 3.97e-08

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 48.74  E-value: 3.97e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2065857414  191 PEEQLQNSFACYLSTsAGPVMGVLYVSTAKLAYCSDNPLSYKN 233
Cdd:smart00568   4 EEEKLIADYSCYLSR-TGPVQGRLYISNYRLCFRSNLPGKLTK 45
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 181-247 1.51e-07

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: 48.52  E-value: 1.51e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065857414 181 KIFRQTFETVPEEQLQNSFACYLSTSAGPVMGVLYVSTAKLAYCSDNPlsyknsgqtEWSYYKVILF 247
Cdd:pfam02893   1 ELFRKKFKLPPEERLIASYSCYLNRDGGPVQGRLYLTNYRLCFRSLPK---------GWSTKVVIPL 58
 
Name Accession Description Interval E-value
PH-GRAM_GEM cd13222
GLABRA 2 expression modulator (GEM) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 192-246 1.02e-27

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: 102.42  E-value: 1.02e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2065857414 192 EEQLQNSFACYLSTSAGPVMGVLYVSTAKLAYCSDNPLSYKNS-GQTEWSYYKVIL 246
Cdd:cd13222     1 EEKLLKTFACYLSTSTGPVAGVLYISTKKIAFCSDRPLSFTSPsGQTSWSYYKVVI 56
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
191-233 3.97e-08

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 48.74  E-value: 3.97e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2065857414  191 PEEQLQNSFACYLSTsAGPVMGVLYVSTAKLAYCSDNPLSYKN 233
Cdd:smart00568   4 EEEKLIADYSCYLSR-TGPVQGRLYISNYRLCFRSNLPGKLTK 45
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 181-247 1.51e-07

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: 48.52  E-value: 1.51e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065857414 181 KIFRQTFETVPEEQLQNSFACYLSTSAGPVMGVLYVSTAKLAYCSDNPlsyknsgqtEWSYYKVILF 247
Cdd:pfam02893   1 ELFRKKFKLPPEERLIASYSCYLNRDGGPVQGRLYLTNYRLCFRSLPK---------GWSTKVVIPL 58
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 192-233 2.91e-06

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: 44.68  E-value: 2.91e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2065857414 192 EEQLQNSFACYLSTSAGPVMGVLYVSTAKLAYCSDNPLSYKN 233
Cdd:cd10570     1 IEKLGVRFCCALRPRKLPLEGTLYLSTYRLIFSSKADGDETK 42
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH