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Conserved domains on  [gi|17532681|ref|NP_495987|]
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GRAM domain-containing protein [Caenorhabditis elegans]

Protein Classification

GRAM domain-containing protein( domain architecture ID 10192315)

GRAM domain-containing protein is a membrane-associated protein; similar to Homo sapiens WW domain-binding protein 2, which acts as a transcriptional coactivator of estrogen and progesterone receptors (ESR1 and PGR) upon hormone activation

CATH:  2.30.29.30
Gene Ontology:  GO:0003713|GO:0031490
PubMed:  11050430|18201690
SCOP:  4000903

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-GRAM_WBP2 cd13214
WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 29-130 7.94e-43

WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; WBP2 plays a number of roles including: acting as a tyrosine kinase substrate, activation of estrogen receptor alpha (ERalpha)/progesterone receptor (PR) transcription, and playing a role in breast cancer. WBP2 contain a N-terminal PH-GRAM domain and a C-terminal WWbp domain. 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. The WWbp domain is characterized by several short PY and PT-like motifs of the PPPPY form and binds to WW domains. WW domains contain two highly conserved tryptophans that are spaced 20-23 residues apart. They bind proline-rich peptide motifs [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs.


:

Pssm-ID: 275401  Cd Length: 103  Bit Score: 140.39  E-value: 7.94e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532681  29 VVMTLGTSENENLEGRRTGTIYLTSHRIIFMPD-PGDWLKSFEIPFNSMQDVNLNQPIFGANYLCGIASAVQGGQMRGEV 107
Cdd:cd13214   1 VESVKGKGAPPFFKGSKKGTIYLTNQRLIFVSSkPTDNFQSFSMPLLNIRDVKFEQPVFGANYLKGKVKPVPGGGWPGEA 80

                        90       100
                ....*....|....*....|...
gi 17532681 108 KWRMTFNRGGCIEFGQSLLQAVE 130
Cdd:cd13214  81 EFKLTFKDGGAIEFGQAFLRLAE 103
 
Name Accession Description Interval E-value
PH-GRAM_WBP2 cd13214
WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 29-130 7.94e-43

WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; WBP2 plays a number of roles including: acting as a tyrosine kinase substrate, activation of estrogen receptor alpha (ERalpha)/progesterone receptor (PR) transcription, and playing a role in breast cancer. WBP2 contain a N-terminal PH-GRAM domain and a C-terminal WWbp domain. 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. The WWbp domain is characterized by several short PY and PT-like motifs of the PPPPY form and binds to WW domains. WW domains contain two highly conserved tryptophans that are spaced 20-23 residues apart. They bind proline-rich peptide motifs [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs.


Pssm-ID: 275401  Cd Length: 103  Bit Score: 140.39  E-value: 7.94e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532681  29 VVMTLGTSENENLEGRRTGTIYLTSHRIIFMPD-PGDWLKSFEIPFNSMQDVNLNQPIFGANYLCGIASAVQGGQMRGEV 107
Cdd:cd13214   1 VESVKGKGAPPFFKGSKKGTIYLTNQRLIFVSSkPTDNFQSFSMPLLNIRDVKFEQPVFGANYLKGKVKPVPGGGWPGEA 80

                        90       100
                ....*....|....*....|...
gi 17532681 108 KWRMTFNRGGCIEFGQSLLQAVE 130
Cdd:cd13214  81 EFKLTFKDGGAIEFGQAFLRLAE 103
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 43-129 1.75e-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: 80.49  E-value: 1.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532681    43 GRRTGTIYLTSHRIIFMPDPGDWLKSFEIPFNSMqdVNLNQPIFGANYLCGIASAVQGGQMrgEVKWRMTFNRGGCIEFG 122
Cdd:pfam02893  28 GPVQGRLYLTNYRLCFRSLPKGWSTKVVIPLVDI--EEIEKLKGGANLFPNGIQVETGSND--KFSFAGFVTRDEAIEFI 103


                  ....*..
gi 17532681   123 QSLLQAV 129
Cdd:pfam02893 104 LALLKNA 110
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
34-80 5.72e-04

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 37.19  E-value: 5.72e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 17532681     34 GTSENENL----------EGRRTGTIYLTSHRIIFMPDPGDWLKSFEIPFNSMQDVN 80
Cdd:smart00568   1 KLPEEEKLiadyscylsrTGPVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIE 57
 
Name Accession Description Interval E-value
PH-GRAM_WBP2 cd13214
WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 29-130 7.94e-43

WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; WBP2 plays a number of roles including: acting as a tyrosine kinase substrate, activation of estrogen receptor alpha (ERalpha)/progesterone receptor (PR) transcription, and playing a role in breast cancer. WBP2 contain a N-terminal PH-GRAM domain and a C-terminal WWbp domain. 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. The WWbp domain is characterized by several short PY and PT-like motifs of the PPPPY form and binds to WW domains. WW domains contain two highly conserved tryptophans that are spaced 20-23 residues apart. They bind proline-rich peptide motifs [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs.


Pssm-ID: 275401  Cd Length: 103  Bit Score: 140.39  E-value: 7.94e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532681  29 VVMTLGTSENENLEGRRTGTIYLTSHRIIFMPD-PGDWLKSFEIPFNSMQDVNLNQPIFGANYLCGIASAVQGGQMRGEV 107
Cdd:cd13214   1 VESVKGKGAPPFFKGSKKGTIYLTNQRLIFVSSkPTDNFQSFSMPLLNIRDVKFEQPVFGANYLKGKVKPVPGGGWPGEA 80

                        90       100
                ....*....|....*....|...
gi 17532681 108 KWRMTFNRGGCIEFGQSLLQAVE 130
Cdd:cd13214  81 EFKLTFKDGGAIEFGQAFLRLAE 103
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 43-129 1.75e-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: 80.49  E-value: 1.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532681    43 GRRTGTIYLTSHRIIFMPDPGDWLKSFEIPFNSMqdVNLNQPIFGANYLCGIASAVQGGQMrgEVKWRMTFNRGGCIEFG 122
Cdd:pfam02893  28 GPVQGRLYLTNYRLCFRSLPKGWSTKVVIPLVDI--EEIEKLKGGANLFPNGIQVETGSND--KFSFAGFVTRDEAIEFI 103


                  ....*..
gi 17532681   123 QSLLQAV 129
Cdd:pfam02893 104 LALLKNA 110
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
34-80 5.72e-04

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 37.19  E-value: 5.72e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 17532681     34 GTSENENL----------EGRRTGTIYLTSHRIIFMPDPGDWLKSFEIPFNSMQDVN 80
Cdd:smart00568   1 KLPEEEKLiadyscylsrTGPVQGRLYISNYRLCFRSNLPGKLTKVVIPLADITRIE 57
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 43-91 3.01e-03

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: 35.82  E-value: 3.01e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 17532681  43 GRRTGTIYLTSHRIIFMPDPGDWLKSFEIPFNSMQDVNLNQP-IFGANYL 91
Cdd:cd10570  17 LPLEGTLYLSTYRLIFSSKADGDETKLVIPLVDITDVEKIAGaSFLPSGL 66
Vps36_ESCRT-II pfam11605
Vacuolar protein sorting protein 36 Vps36; Vps36 is a subunit of ESCRT-II, a protein involved ...
 2-61 3.53e-03

Vacuolar protein sorting protein 36 Vps36; Vps36 is a subunit of ESCRT-II, a protein involved in driving protein sorting from endosomes to lysosomes. The GLUE domain of Vps36 allows for a tight interaction to occur between the protein and Vps28, a subunit of ESCRT-I. This interaction is critical for ubiquitinated cargo progression from early to late endosomes.


Pssm-ID: 402964  Cd Length: 92  Bit Score: 35.75  E-value: 3.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532681     2 SINTANTPdglgvLLYNGETIVIFAQGVVMTLGTSENENlegRRTGTIYLTSHRIIFMPD 61
Cdd:pfam11605   1 ERNTSGRP-----VLRENEVDIYVQDNVGLYQGDQKILN---RQNGRLYLTTHRIIYVDS 52
 
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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