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Conserved domains on  [gi|1046898371|ref|XP_017450771|]
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GRAM domain-containing protein 4 isoform X1 [Rattus norvegicus]

Protein Classification

GRAM domain-containing protein 4( domain architecture ID 10192382)

GRAM domain-containing protein 4 (GRAMD4) plays a role as a mediator of E2F1-induced apoptosis in the absence of p53/TP53

CATH:  2.30.29.30
Gene Ontology:  GO:0006915
PubMed:  11050430|18201690
SCOP:  4000903

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-GRAM_GRAMDC4 cd13221
GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 464-569 4.33e-55

GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; GRAMDC4 is a membrane protein. Nothing is known about its function. Paralogs include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, and GRAMDC-like proteins. It contains a single PH-GRAM domain at its 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: 270041  Cd Length: 104  Bit Score: 181.38  E-value: 4.33e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046898371 464 LAVCENGWRCCLINRDrKMPTDYIRNGVLYVTENYLCFESSKSgSSKRNKVIKLMDITDIQKYKVLSVLPGSGMGIAVST 543
Cdd:cd13221     1 LPVWENGWRCCLINRD-KMPTDYIRNGRLYLTENYLCFESSSS-SSKKNVVIPLTDITRIEKAKPYSFLPGSGMSIEVSV 78

                          90       100
                  ....*....|....*....|....*.
gi 1046898371 544 PSTQKPLVFGAMVHRDEAFETIFSQY 569
Cdd:cd13221    79 SSADKPLFFGAMFRRDEFFDIIALGA 104
tolA super family cl35847
cell envelope integrity inner membrane protein TolA; Provisional
 96-153 2.76e-03

cell envelope integrity inner membrane protein TolA; Provisional


The actual alignment was detected with superfamily member PRK09510:

Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 2.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046898371  96 EELRKLREETNSEMLRQELDRERQRRIELEQKMQEVLKARsEEQPAQPQQPAKGQSQA 153
Cdd:PRK09510   78 EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQK-KQAEEAAKQAALKQKQA 134
 
Name Accession Description Interval E-value
PH-GRAM_GRAMDC4 cd13221
GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 464-569 4.33e-55

GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; GRAMDC4 is a membrane protein. Nothing is known about its function. Paralogs include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, and GRAMDC-like proteins. It contains a single PH-GRAM domain at its 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: 270041  Cd Length: 104  Bit Score: 181.38  E-value: 4.33e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046898371 464 LAVCENGWRCCLINRDrKMPTDYIRNGVLYVTENYLCFESSKSgSSKRNKVIKLMDITDIQKYKVLSVLPGSGMGIAVST 543
Cdd:cd13221     1 LPVWENGWRCCLINRD-KMPTDYIRNGRLYLTENYLCFESSSS-SSKKNVVIPLTDITRIEKAKPYSFLPGSGMSIEVSV 78

                          90       100
                  ....*....|....*....|....*.
gi 1046898371 544 PSTQKPLVFGAMVHRDEAFETIFSQY 569
Cdd:cd13221    79 SSADKPLFFGAMFRRDEFFDIIALGA 104
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 450-569 8.07e-20

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: 85.11  E-value: 8.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046898371 450 NFHEIFNLTENERPLAVCengwrCCLINRDRkmptdYIRNGVLYVTENYLCFESSKSGSSKRnKVIKLMDITDIQKYKVL 529
Cdd:pfam02893   2 LFRKKFKLPPEERLIASY-----SCYLNRDG-----GPVQGRLYLTNYRLCFRSLPKGWSTK-VVIPLVDIEEIEKLKGG 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1046898371 530 SVLPGSGMGIAVSTPStqkPLVFGAMVHRDEAFETIFSQY 569
Cdd:pfam02893  71 ANLFPNGIQVETGSND---KFSFAGFVTRDEAIEFILALL 107
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
456-527 6.21e-09

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 52.21  E-value: 6.21e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046898371  456 NLTENERPLAVcengWRCCLINrdrkmptDYIRNGVLYVTENYLCFESSKSGSSKrNKVIKLMDITDIQKYK 527
Cdd:smart00568   1 KLPEEEKLIAD----YSCYLSR-------TGPVQGRLYISNYRLCFRSNLPGKLT-KVVIPLADITRIEKST 60
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 96-153 2.76e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 2.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046898371  96 EELRKLREETNSEMLRQELDRERQRRIELEQKMQEVLKARsEEQPAQPQQPAKGQSQA 153
Cdd:PRK09510   78 EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQK-KQAEEAAKQAALKQKQA 134
cwf21_SRRM3 cd21376
cwf21 domain found in serine/arginine repetitive matrix protein 3 and similar proteins; Serine ...
 95-139 3.94e-03

cwf21 domain found in serine/arginine repetitive matrix protein 3 and similar proteins; Serine/arginine repetitive matrix protein 3 (SRRM3) may play a role in regulating breast cancer cell invasiveness. It may also be involved in RYBP-mediated breast cancer progression. SRRM3 contains a cwf21 domain at the N-terminus. The cwf21 domain is involved in mRNA splicing; it binds directly to the spliceosomal protein Prp8.


Pssm-ID: 410602 [Multi-domain]  Cd Length: 68  Bit Score: 36.26  E-value: 3.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1046898371  95 QEELRKLREETNSEMLRQELDRERQRRIELE-QKMQEVLkarsEEQ 139
Cdd:cd21376     3 EEEIKKLDAALVKKPNREILDHERKRKVELKcMEMQELM----EEQ 44
 
Name Accession Description Interval E-value
PH-GRAM_GRAMDC4 cd13221
GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 464-569 4.33e-55

GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; GRAMDC4 is a membrane protein. Nothing is known about its function. Paralogs include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, and GRAMDC-like proteins. It contains a single PH-GRAM domain at its 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: 270041  Cd Length: 104  Bit Score: 181.38  E-value: 4.33e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046898371 464 LAVCENGWRCCLINRDrKMPTDYIRNGVLYVTENYLCFESSKSgSSKRNKVIKLMDITDIQKYKVLSVLPGSGMGIAVST 543
Cdd:cd13221     1 LPVWENGWRCCLINRD-KMPTDYIRNGRLYLTENYLCFESSSS-SSKKNVVIPLTDITRIEKAKPYSFLPGSGMSIEVSV 78

                          90       100
                  ....*....|....*....|....*.
gi 1046898371 544 PSTQKPLVFGAMVHRDEAFETIFSQY 569
Cdd:cd13221    79 SSADKPLFFGAMFRRDEFFDIIALGA 104
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 450-569 8.07e-20

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: 85.11  E-value: 8.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046898371 450 NFHEIFNLTENERPLAVCengwrCCLINRDRkmptdYIRNGVLYVTENYLCFESSKSGSSKRnKVIKLMDITDIQKYKVL 529
Cdd:pfam02893   2 LFRKKFKLPPEERLIASY-----SCYLNRDG-----GPVQGRLYLTNYRLCFRSLPKGWSTK-VVIPLVDIEEIEKLKGG 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1046898371 530 SVLPGSGMGIAVSTPStqkPLVFGAMVHRDEAFETIFSQY 569
Cdd:pfam02893  71 ANLFPNGIQVETGSND---KFSFAGFVTRDEAIEFILALL 107
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 467-569 7.97e-13

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: 64.32  E-value: 7.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046898371 467 CENGWRCCLINRDRKMPtdyiRNGVLYVTENYLCFESSKSGsSKRNKVIKLMDITDIQKYKVLSVLPgSGMGIAVSTPST 546
Cdd:cd10570     2 EKLGVRFCCALRPRKLP----LEGTLYLSTYRLIFSSKADG-DETKLVIPLVDITDVEKIAGASFLP-SGLIITCKDFRT 75

                          90       100
                  ....*....|....*....|...
gi 1046898371 547 QKPLVFGAMvhrdEAFETIFSQY 569
Cdd:cd10570    76 IKFSFDSED----EAVKVIARVL 94
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 490-568 9.04e-11

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: 58.67  E-value: 9.04e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046898371 490 GVLYVTENYLCFESSKSGsSKRNKVIKLMDITDIQKYKVLSVLPGSgmgIAVSTPSTQkpLVFGAMVHRDEAFETIFSQ 568
Cdd:cd13220    21 GRLYISENHLCFYSNIFG-WETKLVIPFKDITSIEKKKTALIFPNA---IEITTKGEK--YFFTSFLSRDSAYKLLTRV 93
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
456-527 6.21e-09

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


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 52.21  E-value: 6.21e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046898371  456 NLTENERPLAVcengWRCCLINrdrkmptDYIRNGVLYVTENYLCFESSKSGSSKrNKVIKLMDITDIQKYK 527
Cdd:smart00568   1 KLPEEEKLIAD----YSCYLSR-------TGPVQGRLYISNYRLCFRSNLPGKLT-KVVIPLADITRIEKST 60
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 96-153 2.76e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 2.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046898371  96 EELRKLREETNSEMLRQELDRERQRRIELEQKMQEVLKARsEEQPAQPQQPAKGQSQA 153
Cdd:PRK09510   78 EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQK-KQAEEAAKQAALKQKQA 134
PH-GRAM1_TCB1D9_TCB1D9B cd13351
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
 469-563 3.32e-03

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: 37.37  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046898371 469 NGWRCCLINRdrKMPtdyiRNGVLYVTENYLCFESSKSGSSKRnKVIKLMDITDIQKYKVLsVLPGSgmgIAVSTPStqK 548
Cdd:cd13351     6 NYYSCSYWKG--RVP----RQGWLYLSVNHLCFYSFLLGKEAK-LVIRWTDVTQLEKNNSL-LLPDS---IKVVTRD--K 72

                          90
                  ....*....|....*
gi 1046898371 549 PLVFGAMVHRDEAFE 563
Cdd:cd13351    73 EHYFSMFLNISETFK 87
cwf21_SRRM3 cd21376
cwf21 domain found in serine/arginine repetitive matrix protein 3 and similar proteins; Serine ...
 95-139 3.94e-03

cwf21 domain found in serine/arginine repetitive matrix protein 3 and similar proteins; Serine/arginine repetitive matrix protein 3 (SRRM3) may play a role in regulating breast cancer cell invasiveness. It may also be involved in RYBP-mediated breast cancer progression. SRRM3 contains a cwf21 domain at the N-terminus. The cwf21 domain is involved in mRNA splicing; it binds directly to the spliceosomal protein Prp8.


Pssm-ID: 410602 [Multi-domain]  Cd Length: 68  Bit Score: 36.26  E-value: 3.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1046898371  95 QEELRKLREETNSEMLRQELDRERQRRIELE-QKMQEVLkarsEEQ 139
Cdd:cd21376     3 EEEIKKLDAALVKKPNREILDHERKRKVELKcMEMQELM----EEQ 44
 
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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