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Conserved domains on  [gi|30039698|ref|NP_835463|]
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ras association domain-containing protein 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RA_RASSF3 cd17219
Ras-associating (RA) domain found in Ras-association domain-containing protein 3 (RASSF3); ...
51-185 1.41e-89

Ras-associating (RA) domain found in Ras-association domain-containing protein 3 (RASSF3); RASSF3 is a member of a family of six related classical RASSF1-6 proteins (the classical RASSF proteins). RASSF3 has three transcripts (A-C) due to alternative splicing of the exons. The RASSF3B and 3C isoforms are shorter than RASSF3A, and unlike RASSF3A do not contain the RA or SARAH domains. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases, and the SARAH domain mediates protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF3A regulates apoptosis and cell cycle via p53 stabilization and possibly is involved in DNA repair.


:

Pssm-ID: 340739  Cd Length: 141  Bit Score: 260.58  E-value: 1.41e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039698  51 KEEIKEKVHKYNLAVTDKLKMTLNSNGIYTGFIKVQMELCKPPQTSP------NSGKLSPSSNGCMNTLHISSTNTVGEV 124
Cdd:cd17219   1 KEEIKQKIQLYNLAVTDKLKMTLNSSGIYTGFIKVQMDLRRPITVRGgaagnnNNETAFYLPKGSVNTLHISSTNTVREV 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30039698 125 IEALLKKFLVTESPAKFALYKRCHREDQVYACKLSDREHPLYLRLVAGPRTDTLSFVLREH 185
Cdd:cd17219  81 IEALLKKFLVADNPAKFALYKRCHKEDQVYACKLSDREHPLYLRLVAGPNTDTLSFVLREH 141
SARAH_RASSF3 cd21891
C-terminal SARAH domain found in Ras-association domain-containing protein 3 (RASSF3); RASSF3 ...
189-234 1.03e-23

C-terminal SARAH domain found in Ras-association domain-containing protein 3 (RASSF3); RASSF3 is one of six related proteins, the classical RASSF proteins (RASSF1-6), that contain a conserved RalGDS/AF6 Ras association (RA) domain located towards the C-terminus. RASSF3 has three transcripts (A-C) due to alternative splicing of the exons. The RASSF3B and 3C isoforms are shorter than RASSF3A, and unlike RASSF3A do not contain the RA or SARAH (Salvador-RassF-Hippo) domains. RASSF3A regulates apoptosis and the cell cycle via p53 stabilization and is possibly involved in DNA repair. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases, and the SARAH domain mediates protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. This model corresponds to the SARAH domain of RASSF3.


:

Pssm-ID: 439185  Cd Length: 46  Bit Score: 89.81  E-value: 1.03e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 30039698 189 EWEAFSLPELQNFLRILDKEEDEQLQNLKRRYTAYRQKLEEALREV 234
Cdd:cd21891   1 MWEAFSLPELQNFLRILDKEEDEQLRSIKRRYNAYREKLEEALRGV 46
 
Name Accession Description Interval E-value
RA_RASSF3 cd17219
Ras-associating (RA) domain found in Ras-association domain-containing protein 3 (RASSF3); ...
51-185 1.41e-89

Ras-associating (RA) domain found in Ras-association domain-containing protein 3 (RASSF3); RASSF3 is a member of a family of six related classical RASSF1-6 proteins (the classical RASSF proteins). RASSF3 has three transcripts (A-C) due to alternative splicing of the exons. The RASSF3B and 3C isoforms are shorter than RASSF3A, and unlike RASSF3A do not contain the RA or SARAH domains. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases, and the SARAH domain mediates protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF3A regulates apoptosis and cell cycle via p53 stabilization and possibly is involved in DNA repair.


Pssm-ID: 340739  Cd Length: 141  Bit Score: 260.58  E-value: 1.41e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039698  51 KEEIKEKVHKYNLAVTDKLKMTLNSNGIYTGFIKVQMELCKPPQTSP------NSGKLSPSSNGCMNTLHISSTNTVGEV 124
Cdd:cd17219   1 KEEIKQKIQLYNLAVTDKLKMTLNSSGIYTGFIKVQMDLRRPITVRGgaagnnNNETAFYLPKGSVNTLHISSTNTVREV 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30039698 125 IEALLKKFLVTESPAKFALYKRCHREDQVYACKLSDREHPLYLRLVAGPRTDTLSFVLREH 185
Cdd:cd17219  81 IEALLKKFLVADNPAKFALYKRCHKEDQVYACKLSDREHPLYLRLVAGPNTDTLSFVLREH 141
SARAH_RASSF3 cd21891
C-terminal SARAH domain found in Ras-association domain-containing protein 3 (RASSF3); RASSF3 ...
189-234 1.03e-23

C-terminal SARAH domain found in Ras-association domain-containing protein 3 (RASSF3); RASSF3 is one of six related proteins, the classical RASSF proteins (RASSF1-6), that contain a conserved RalGDS/AF6 Ras association (RA) domain located towards the C-terminus. RASSF3 has three transcripts (A-C) due to alternative splicing of the exons. The RASSF3B and 3C isoforms are shorter than RASSF3A, and unlike RASSF3A do not contain the RA or SARAH (Salvador-RassF-Hippo) domains. RASSF3A regulates apoptosis and the cell cycle via p53 stabilization and is possibly involved in DNA repair. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases, and the SARAH domain mediates protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. This model corresponds to the SARAH domain of RASSF3.


Pssm-ID: 439185  Cd Length: 46  Bit Score: 89.81  E-value: 1.03e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 30039698 189 EWEAFSLPELQNFLRILDKEEDEQLQNLKRRYTAYRQKLEEALREV 234
Cdd:cd21891   1 MWEAFSLPELQNFLRILDKEEDEQLRSIKRRYNAYREKLEEALRGV 46
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
79-186 2.06e-17

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 74.68  E-value: 2.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039698    79 YTGFIKVQMELCKPPQTSpnsgklspssngcmNTLHISSTNTVGEVIEALLKKFLVTESPAKFALYKRCHREDQVYacKL 158
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTY--------------KTILVSSSTTAEEVIEALLEKFGLEDDPRDYVLVEVLERGGGER--RL 64
                          90       100
                  ....*....|....*....|....*...
gi 30039698   159 SDREHPLYLRLVAGPRTDTLSFVLREHE 186
Cdd:pfam00788  65 PDDECPLQIQLQWPRDASDSRFLLRKRD 92
Nore1-SARAH pfam16517
Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain; The Nore1-SARAH, C-terminal, ...
192-231 4.74e-14

Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain; The Nore1-SARAH, C-terminal, domain of Nore1, the tumour-suppressor, a novel Ras effector, has a characteriztic coiled-coil structure. It is a small helical module that is important in signal-transduction networks. The recombinant SARAH domain of Nore1 crystallizes as an anti-parallel homodimer with representative characteriztics of coiled coils. The central function of the SARAH domain seems to be the mediation of homo- and hetero-oligomerization between SARAH domain-containing proteins. Nore1 forms homo- and hetero complexes through its C-terminal SARAH (Sav/Rassf/Hpo) domain.


Pssm-ID: 435392  Cd Length: 40  Bit Score: 64.06  E-value: 4.74e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 30039698   192 AFSLPELQNFLRILDKEEDEQLQNLKRRYTAYRQKLEEAL 231
Cdd:pfam16517   1 AFSLPELENFLRILDEEEEREIQQIRRKYTALRQKLQQAL 40
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
112-186 4.34e-11

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 57.69  E-value: 4.34e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30039698    112 TLHISSTNTVGEVIEALLKKFLVTESPAKFALYKR-CHREDQVyackLSDREHPLYLRLVAGPRTDTLSFVLREHE 186
Cdd:smart00314  19 TLRVSSRTTARDVIQQLLEKFHLTDDPEEYVLVEVlPDGKERV----LPDDENPLQLQKLWPRRGPNLRFVLRKRD 90
 
Name Accession Description Interval E-value
RA_RASSF3 cd17219
Ras-associating (RA) domain found in Ras-association domain-containing protein 3 (RASSF3); ...
51-185 1.41e-89

Ras-associating (RA) domain found in Ras-association domain-containing protein 3 (RASSF3); RASSF3 is a member of a family of six related classical RASSF1-6 proteins (the classical RASSF proteins). RASSF3 has three transcripts (A-C) due to alternative splicing of the exons. The RASSF3B and 3C isoforms are shorter than RASSF3A, and unlike RASSF3A do not contain the RA or SARAH domains. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases, and the SARAH domain mediates protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF3A regulates apoptosis and cell cycle via p53 stabilization and possibly is involved in DNA repair.


Pssm-ID: 340739  Cd Length: 141  Bit Score: 260.58  E-value: 1.41e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039698  51 KEEIKEKVHKYNLAVTDKLKMTLNSNGIYTGFIKVQMELCKPPQTSP------NSGKLSPSSNGCMNTLHISSTNTVGEV 124
Cdd:cd17219   1 KEEIKQKIQLYNLAVTDKLKMTLNSSGIYTGFIKVQMDLRRPITVRGgaagnnNNETAFYLPKGSVNTLHISSTNTVREV 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30039698 125 IEALLKKFLVTESPAKFALYKRCHREDQVYACKLSDREHPLYLRLVAGPRTDTLSFVLREH 185
Cdd:cd17219  81 IEALLKKFLVADNPAKFALYKRCHKEDQVYACKLSDREHPLYLRLVAGPNTDTLSFVLREH 141
RA_RASSF1_like cd01778
Ras-associating (RA) domain found in Ras-association domain family members, RASSF1, RASSF3, ...
77-185 4.18e-46

Ras-associating (RA) domain found in Ras-association domain family members, RASSF1, RASSF3, and RASSF5; The RASSF family of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain which is located either at the C-terminus (RASSF1-6, the classical group) or at the N-terminus (RASSF7-10). RASSF1-6 contains a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that functions in scaffolding and regulatory interactions. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. Classical RASSF members interact either directly or indirectly with activated Ras. Ras proteins are small GTPases that are involved in cellular signal transduction. The classical RASSF proteins seem to modulate some of the growth inhibitory responses mediated by Ras and may serve as tumor suppressor genes. This family contains RASSF1, RASSF3, and RASSF5.


Pssm-ID: 340476  Cd Length: 130  Bit Score: 149.75  E-value: 4.18e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039698  77 GIYTGFIKVQMELCKPPQTSPNSGKLS--------------------PSSNGCMNTLHISSTNTVGEVIEALLKKFLVTE 136
Cdd:cd01778   1 GSFQGFIRVHMNLTRPISVSAGTRPPSiydvlkledsgdsrktrtsfYLPKDTVKALHITSDTTAREVIEALLKKFKITD 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 30039698 137 SPAKFALYKRCHRED-QVYACKLSDREHPLYLRLVAGPRTDTLSFVLREH 185
Cdd:cd01778  81 NPRKFALYERTHEEEgKVKLRKLSDDERPLYLCLLWGSQGDSKSFVLQEN 130
RA_RASSF1 cd17218
Ras-associating (RA) domain found in Ras-association domain-containing protein 1 (RASSF1); ...
49-185 2.15e-44

Ras-associating (RA) domain found in Ras-association domain-containing protein 1 (RASSF1); RASSF1 is a member of a family of six related RASSF1-6 proteins (the classical RASSF proteins). RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. With the exception of some minor splice variants (RASSF1F and RASSF1G), RASSF1 contains an RA domain and a C-terminal SARAH protein-protein interaction motif. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases, and the SARAH domain mediates protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF1A and 1C are the most extensively studied RASSF1 with both localized to microtubules and involved in regulation of growth and migration.


Pssm-ID: 340738  Cd Length: 157  Bit Score: 146.53  E-value: 2.15e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039698  49 LSKEEIKEKVHKYNLAVTDKLKMTLNSNGIYTGFIKVQMELCKP--------PQTSPNSGKLSPSSNGC----------- 109
Cdd:cd17218   1 LSQAEIEQKIKEYNAQINSNLFMSLNKDGSYTGFIKVQLKLVRPvsvpankkPSSIQDSRKGSGRSQPVkrrtsfylpkd 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30039698 110 -MNTLHISSTNTVGEVIEALLKKFLVTESPAKFALYKRCHREDQVYACKLSDREHPLYLRLVAGPRTDTLSFVLREH 185
Cdd:cd17218  81 tVKHLHISSKTRASEVIEALLKKFTVVDNPRKFALFERTEKDDQVYLRKLSDDEQPLYLRLLAGPNEKTLSFVLKEN 157
RA_RASSF5 cd17220
Ras-associating (RA) domain of Ras-association domain family 5 (RASSF5); RASSF5, also called ...
52-184 1.09e-41

Ras-associating (RA) domain of Ras-association domain family 5 (RASSF5); RASSF5, also called New ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is a member of a family of six related RASSF1-6 proteins (the classical RASSF proteins) and is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. All transcripts variants of RASSF5 contain the RA or SARAH domains. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases, and the SARAH domain mediates protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion.


Pssm-ID: 340740  Cd Length: 152  Bit Score: 139.23  E-value: 1.09e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039698  52 EEIKEKVHKYNLAVTDKLKMTLNSNGIYTGFIKVQMELCKP----PQTSPNSGKLSPSSNG------------CMNTLHI 115
Cdd:cd17220   3 EEIKQKIESYNTKVKNCLGMKLSPDGTYTGFIKVHLKLRRPvtvpAGIRPQSIYEVNPADTtdkrtsfylpldAIKQLHI 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30039698 116 SSTNTVGEVIEALLKKFLVTESPAKFALYKRCHREDQVYACKLSDREHPLYLRLVAGPRTDTLSFVLRE 184
Cdd:cd17220  83 SSTTTVSEVIQGLLKKFMVVDNPQKFALFKRMRKDGQVLFQKLPLTEYPLYLRLLAGPDTDVLSFVLKE 151
SARAH_RASSF3 cd21891
C-terminal SARAH domain found in Ras-association domain-containing protein 3 (RASSF3); RASSF3 ...
189-234 1.03e-23

C-terminal SARAH domain found in Ras-association domain-containing protein 3 (RASSF3); RASSF3 is one of six related proteins, the classical RASSF proteins (RASSF1-6), that contain a conserved RalGDS/AF6 Ras association (RA) domain located towards the C-terminus. RASSF3 has three transcripts (A-C) due to alternative splicing of the exons. The RASSF3B and 3C isoforms are shorter than RASSF3A, and unlike RASSF3A do not contain the RA or SARAH (Salvador-RassF-Hippo) domains. RASSF3A regulates apoptosis and the cell cycle via p53 stabilization and is possibly involved in DNA repair. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases, and the SARAH domain mediates protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. This model corresponds to the SARAH domain of RASSF3.


Pssm-ID: 439185  Cd Length: 46  Bit Score: 89.81  E-value: 1.03e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 30039698 189 EWEAFSLPELQNFLRILDKEEDEQLQNLKRRYTAYRQKLEEALREV 234
Cdd:cd21891   1 MWEAFSLPELQNFLRILDKEEDEQLRSIKRRYNAYREKLEEALRGV 46
SARAH_RASSF5 cd21892
C-terminal SARAH domain found in Ras-association domain-containing protein 5 (RASSF5); RASSF5, ...
189-233 1.11e-19

C-terminal SARAH domain found in Ras-association domain-containing protein 5 (RASSF5); RASSF5, also called New ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is one of six related proteins, the classical RASSF proteins (RASSF1-6), that contain a conserved RalGDS/AF6 Ras association (RA) domain located towards the C-terminus. It acts as a potential tumor suppressor that may be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. RASSF5 is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. All transcript variants of RASSF5 contain the RA and SARAH (Salvador-RassF-Hippo) domains. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases, and the SARAH domain mediates protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. This model corresponds to the SARAH domain of RASSF5, that mediates homo- and heterodimerization.


Pssm-ID: 439186  Cd Length: 48  Bit Score: 79.01  E-value: 1.11e-19
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 30039698 189 EWEAFSLPELQNFLRILDKEEDEQLQNLKRRYTAYRQKLEEALRE 233
Cdd:cd21892   4 EWDAFSVPELQNFLRILEKEEQDKIQQVQKKYAKFRQKLQDALKE 48
SARAH_RASSF1-like cd21885
C-terminal SARAH domain found in Ras-association domain proteins, RASSF1, RASSF3, and RASSF5; ...
189-233 2.25e-18

C-terminal SARAH domain found in Ras-association domain proteins, RASSF1, RASSF3, and RASSF5; The RASSF subfamily of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain which is located either at the C-terminus (RASSF1-6, the classical group) or at the N-terminus (RASSF7-10). Classical RASSF proteins interact either directly or indirectly with activated Ras. Ras proteins are small GTPases that are involved in cellular signal transduction. They seem to modulate some of the growth inhibitory responses mediated by Ras and may serve as tumor suppressor genes. RASSF1-6 contains a conserved SARAH (Salvador-RassF-Hippo) motif adjacent to the RA domain that functions in scaffolding and regulatory interactions. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. This model corresponds to the SARAH domain of RASSF1, RASSF3, and RASSF5. It is a characteristic coiled-coil structure that is important in signal-transduction networks. The central function of the SARAH domain is the mediation of homo- and heterodimerization between SARAH domain-containing proteins.


Pssm-ID: 439179  Cd Length: 45  Bit Score: 75.62  E-value: 2.25e-18
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 30039698 189 EWEAFSLPELQNFLRILDKEEDEQLQNLKRRYTAYRQKLEEALRE 233
Cdd:cd21885   1 LWEAFSLPELENFLKILDREEKEYIEQIREKYRIYRKKLQRRLDE 45
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
79-186 2.06e-17

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 74.68  E-value: 2.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039698    79 YTGFIKVQMELCKPPQTSpnsgklspssngcmNTLHISSTNTVGEVIEALLKKFLVTESPAKFALYKRCHREDQVYacKL 158
Cdd:pfam00788   1 DDGVLKVYTEDGKPGTTY--------------KTILVSSSTTAEEVIEALLEKFGLEDDPRDYVLVEVLERGGGER--RL 64
                          90       100
                  ....*....|....*....|....*...
gi 30039698   159 SDREHPLYLRLVAGPRTDTLSFVLREHE 186
Cdd:pfam00788  65 PDDECPLQIQLQWPRDASDSRFLLRKRD 92
Nore1-SARAH pfam16517
Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain; The Nore1-SARAH, C-terminal, ...
192-231 4.74e-14

Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain; The Nore1-SARAH, C-terminal, domain of Nore1, the tumour-suppressor, a novel Ras effector, has a characteriztic coiled-coil structure. It is a small helical module that is important in signal-transduction networks. The recombinant SARAH domain of Nore1 crystallizes as an anti-parallel homodimer with representative characteriztics of coiled coils. The central function of the SARAH domain seems to be the mediation of homo- and hetero-oligomerization between SARAH domain-containing proteins. Nore1 forms homo- and hetero complexes through its C-terminal SARAH (Sav/Rassf/Hpo) domain.


Pssm-ID: 435392  Cd Length: 40  Bit Score: 64.06  E-value: 4.74e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 30039698   192 AFSLPELQNFLRILDKEEDEQLQNLKRRYTAYRQKLEEAL 231
Cdd:pfam16517   1 AFSLPELENFLRILDEEEEREIQQIRRKYTALRQKLQQAL 40
SARAH_RASSF1 cd21890
C-terminal SARAH domain found in Ras-association domain-containing protein 1 (RASSF1); RASSF1 ...
190-231 6.79e-13

C-terminal SARAH domain found in Ras-association domain-containing protein 1 (RASSF1); RASSF1 is one of six related proteins, the classical RASSF proteins (RASSF1-6), that contain a conserved RalGDS/AF6 Ras association (RA) domain located towards the C-terminus. It acts as a potential tumor suppressor that is required for death receptor-dependent apoptosis. It mediates activation of STK3/MST2 and STK4/MST1 during Fas-induced apoptosis by preventing their dephosphorylation. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1, with both localized to microtubules and involved in regulation of growth and migration. With the exception of some minor splice variants (RASSF1F and RASSF1G), RASSF1 contains an RA domain and a C-terminal SARAH (Salvador-RassF-Hippo) protein-protein interaction motif. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. The RA domain mediates interactions with Ras and other small GTPases, and the SARAH domain mediates protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. This model corresponds to the SARAH domain of RASSF1.


Pssm-ID: 439184  Cd Length: 46  Bit Score: 61.37  E-value: 6.79e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 30039698 190 WEAFSLPELQNFLRILDKEEDEQLQNLKRRYTAYRQKLEEAL 231
Cdd:cd21890   2 WDAFSMPELQNFLRILQREEEEHVRQILQRYTRCREKMQEAL 43
SARAH_SF cd21883
C-terminal SARAH domain found in scaffold protein salvador (Sav), Ras-association domain ...
189-233 2.08e-12

C-terminal SARAH domain found in scaffold protein salvador (Sav), Ras-association domain proteins, and mammalian STE20-like protein kinases (MST); The SARAH (Salvador-RassF-Hippo) domain family includes scaffold protein salvador (Sav), Ras-association domain proteins (RASSF1-6), and mammalian STE20-like protein kinase (MST) subfamily members (MST1-2 and Hippo). Sav is a scaffold protein mainly found in metazoans. Drosophila melanogaster Sav, also called Shar-pei (SHRP), promotes both cell cycle exit and apoptosis in Drosophila. It plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. Human protein salvador homolog 1, also called 45 kDa WW domain protein (WW45), acts as a mammalian sterile 20-like kinase 1 (MST1)-binding protein required to enhance MST1-mediated apoptosis. It is a regulator of STK3/MST2 and STK4/MST1 in the Hippo signaling pathway. Classical RASSF proteins interact either directly or indirectly with activated Ras. Ras proteins are small GTPases that are involved in cellular signal transduction. They seem to modulate some of the growth inhibitory responses mediated by Ras and may serve as tumor suppressor genes. RASSF1-6 contains a conserved SARAH motif adjacent to the RA domain that functions in scaffolding and regulatory interactions. MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 and MST2 are STE20 family stress-activated, pro-apoptotic serine/threonine-protein kinases which, following caspase-cleavage, enter the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. They are key components of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. Hippo (Hpo), also called STE20-like kinase MST (dMST), is the Drosophila homolog of STE20-like protein kinases, MST1 and MST2. It is a STE20 family serine/threonine-protein kinase that functions as a tumor suppressor by restricting cell proliferation and promotes apoptosis in conjunction with salvador and warts. Hpo also plays a key role in the Hippo/SWH signaling pathway. This model corresponds to the C-terminal SARAH domain, a characteristic coiled-coil structure. It is a small helical module that is important in signal-transduction networks. The central function of the SARAH domain seems to be the mediation of homo- and heterodimerization between SARAH domain-containing proteins.


Pssm-ID: 439177  Cd Length: 45  Bit Score: 59.72  E-value: 2.08e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 30039698 189 EWEAFSLPELQNFLRILDKEEDEQLQNLKRRYTAYRQKLEEALRE 233
Cdd:cd21883   1 QLKNFSLPELQMFLKMLDPEEEREIEQLVKKYTAYRQAILDALEE 45
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
112-186 4.34e-11

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 57.69  E-value: 4.34e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30039698    112 TLHISSTNTVGEVIEALLKKFLVTESPAKFALYKR-CHREDQVyackLSDREHPLYLRLVAGPRTDTLSFVLREHE 186
Cdd:smart00314  19 TLRVSSRTTARDVIQQLLEKFHLTDDPEEYVLVEVlPDGKERV----LPDDENPLQLQKLWPRRGPNLRFVLRKRD 90
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
112-184 2.92e-10

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 55.40  E-value: 2.92e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30039698 112 TLHISSTNTVGEVIEALLKKFLVTESPAKFALYKRCHREDQVYacKLSDREHPLYLRLVAGPRTDTLSFVLRE 184
Cdd:cd17043  17 SILVSSTTTAREVVQLLLEKYGLEEDPEDYSLYEVSEKQETER--VLHDDECPLLIQLEWGPQGTEFRFVLKR 87
RA_RASSF2_like cd01784
Ras-associating (RA) domain found in Ras-association domain family members, RASSF2, RASSF4, ...
108-173 7.58e-08

Ras-associating (RA) domain found in Ras-association domain family members, RASSF2, RASSF4, and RASSF6; The RASSF family of proteins shares a conserved RalGDS/AF6 RA domain either in the C-terminus (RASSF1-6) or N-terminus (RASSF7-10). The classical family members (RASSF1-6) contain a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that functions as scaffolding and regulatory interactions. The RA domain of the classical RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. Classical RASSF members interact either directly or indirectly with activated Ras. Ras proteins are small GTPases that are involved in cellular signal transduction. The classical RASSF protein family seem to modulate some of the growth inhibitory responses mediated by Ras and may serve as tumor suppressor genes. This family contains RASSF2, RASSF4, and RASSF6.


Pssm-ID: 340482  Cd Length: 87  Bit Score: 48.79  E-value: 7.58e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039698 108 GCMNTLHISSTNTVGEVIEALLKKFLVTESPAKFALYKrchredqVYAC----KLSDREHPLYLRLVAGP 173
Cdd:cd01784  12 GSVTNVRVTSLMTTPEVIKLLLEKFKVENSPEEFALYV-------VKDSgerrRLKDDDYPLLTRVLLGP 74
RA_RASSF6 cd17223
Ras-associating (RA) domain found in Ras-association domain-containing protein 6 (RASSF6); ...
108-173 2.94e-07

Ras-associating (RA) domain found in Ras-association domain-containing protein 6 (RASSF6); RASSF6 is a member of a family of six related classical RASSF1-6 proteins and is expressed as four transcripts via alternative splicing. All transcripts variant of RASSF6 contain the RA and SARAH domains. The RA domain of the classical RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RA domains mediate interactions with Ras and other small GTPases, SARAH domains mediate protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF6 is ubiquitiated and degraded by interacting with MDM2 to stabilize P53 and regulates apoptosis and cell cycle. RASSF6 is a tumor suppressor protein and is epigenetically silenced in childhood leukemia and neuroblastomas. Overexpression of RASSF6 causes apoptosis in HeLa cells.


Pssm-ID: 340743  Cd Length: 87  Bit Score: 47.15  E-value: 2.94e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30039698 108 GCMNTLHISSTNTVGEVIEALLKKFLVTESPAKFALYKRCHREDQVyacKLSDREHPLYLRLVAGP 173
Cdd:cd17223  12 GSETKVRINSNMTTQEVIKQLLQKFKIENSPNEFALYIIHATGEKK---RLKNTDFPLWERLLQGP 74
RA_RASSF2 cd17221
Ras-associating (RA) domain found in Ras-association domain-containing protein 2 (RASSF2); ...
108-173 1.86e-05

Ras-associating (RA) domain found in Ras-association domain-containing protein 2 (RASSF2); RASSF2 is a member of a family of six related classical RASSF1-6 proteins. The RASSF2 gene is transcribed into two major isoforms (A and C). RASSF2 is structurally related to RASSF1A but unlike RASSF1A It is primarily a nuclear protein. RASSF2 contains the RA and SARAH domains. The RA domain of the classical RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RA domains mediate interactions with Ras and other small GTPases, and SARAH domains mediate protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF2 is inactivated in different cancers and cancer cell lines by promoter methylation and loss of expression, implicating the correlation and significance of RASSF2 in tumorigenesis. In addition to regulating apoptosis and proliferation RASSF2 may have other functions as RASSF2 knockout mice develop normally for the first two weeks but then develop growth retardation and die 4 weeks after birth.


Pssm-ID: 340741  Cd Length: 87  Bit Score: 41.89  E-value: 1.86e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30039698 108 GCMNTLHISSTNTVGEVIEALLKKFLVTESPAKFALYKRCHREDQVyacKLSDREHPLYLRLVAGP 173
Cdd:cd17221  12 GSVTNVRINSTMTTPQVLKLLLNKFKIENSAEEFALYIVHTSGEKQ---KLKATDYPLIARILQGP 74
RA_RASSF4 cd17222
Ras-associating (RA) domain found in Ras-association domain-containing protein 4 (RASSF4); ...
106-173 1.98e-05

Ras-associating (RA) domain found in Ras-association domain-containing protein 4 (RASSF4); RASSF4 is a member of a family of six related classical RASSF1-6 proteins and is broadly expressed in normal tissues. RASSF4 expression is reduced in tumor cell lines and primary tumors by promoter specific hypermethylation. RASSF4 contains the RA and SARAH domains. The RA domain of the classical RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RA domains mediate interactions with Ras and other small GTPases, and SARAH domains mediate protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. RASSF4 inhibits lung cancer cell proliferation and invasion.


Pssm-ID: 340742  Cd Length: 87  Bit Score: 41.78  E-value: 1.98e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30039698 106 SNGCMNTLHISSTNTVGEVIEALLKKFLVTESPAKFALYKrCHREDQvyACKLSDREHPLYLRLVAGP 173
Cdd:cd17222  10 AYGSVTNVRVNSTMTTPQVLKLLLNKFRVENSPDEFALYL-VHESGE--RTKLKDTEYPLISRILHGP 74
SARAH_RASSF2-like cd21886
C-terminal SARAH domain found in Ras-association domain proteins, RASSF2, RASSF4, and RASSF6; ...
193-233 6.78e-05

C-terminal SARAH domain found in Ras-association domain proteins, RASSF2, RASSF4, and RASSF6; The RASSF subfamily of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain which is located either at the C-terminus (RASSF1-6, the classical group) or at the N-terminus (RASSF7-10). The classical RASSF proteins seem to modulate some of the growth inhibitory responses mediated by Ras and may serve as tumor suppressor genes. They interact either directly or indirectly with activated Ras. Ras proteins are small GTPases that are involved in cellular signal transduction. RASSF1-6 contain a conserved C-terminal SARAH (Salvador-RassF-Hippo) motif adjacent to the RA domain that functions in scaffolding and regulatory interactions. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. This model corresponds to the SARAH domain of RASSF2, RASSF4, and RASSF6. It is a characteristic coiled-coil structure that is important in signal-transduction networks. The central function of the SARAH domain is the mediation of homo- and heterodimerization between SARAH domain-containing proteins.


Pssm-ID: 439180  Cd Length: 45  Bit Score: 39.44  E-value: 6.78e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 30039698 193 FSLPELQNFLRILDKEEDEQLQNLKRRYTAYRQKLEEALRE 233
Cdd:cd21886   5 FSMPELRAFLRKFQEEEEREVEKIKEKYEELKRRIKKRMEE 45
SARAH_RASSF2 cd21893
C-terminal SARAH domain found in Ras-association domain-containing protein 2 (RASSF2); RASSF2 ...
193-234 3.13e-04

C-terminal SARAH domain found in Ras-association domain-containing protein 2 (RASSF2); RASSF2 is one of six related proteins, the classical RASSF proteins (RASSF1-6), that contain a conserved RalGDS/AF6 Ras association (RA) domain located towards the C-terminus. It acts as a potential tumor suppressor that may promote apoptosis and cell cycle arrest. It is a KRAS-specific effector protein. It stabilizes STK3/MST2 by protecting it from proteasomal degradation. The RASSF2 gene is transcribed into two major isoforms (A and C). RASSF2 is structurally related to RASSF1A but unlike RASSF1A, it is primarily a nuclear protein. RASSF2 contains the RA and SARAH (Salvador-RassF-Hippo) domains. The RA domain of the classical RASSF proteins has a beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RA domains mediate interactions with Ras and other small GTPases, and SARAH domains mediate protein-protein interactions crucial in the pathways that induce cell cycle arrest and apoptosis. This model corresponds to the SARAH domain of RASSF2.


Pssm-ID: 439187  Cd Length: 46  Bit Score: 37.48  E-value: 3.13e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 30039698 193 FSLPELQNFLRILDKEEDEQLQNLKRRYTAYRQKLEEALREV 234
Cdd:cd21893   5 FEMPVLKSFIQKLKEEEDREVKKLMRRYTVLRLMIEQRLQEI 46
RA1_Afadin cd01782
Ras-associating (RA) domain 1 found in Afadin; Afadin, also termed ALL1-fused gene from ...
115-169 3.06e-03

Ras-associating (RA) domain 1 found in Afadin; Afadin, also termed ALL1-fused gene from chromosome 6 protein (AF-6), or canoe, is involved in many fundamental signaling cascades in cells. In addition, it is involved in oncogenesis and metastasis. Afadin has multiple domains: from the N-terminus to the C-terminus it has two Ras-associated (RA) domains, a forkhead-associated domain, a dilute domain, a PDZ domain, three proline-rich domains, and an F-actin-binding domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Afadin is abundant at cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. This family corresponds to the first RA domain of afadin, which mediates its self-association.


Pssm-ID: 340480  Cd Length: 112  Bit Score: 36.16  E-value: 3.06e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30039698 115 ISSTNTVGEVIEALLKKFLVTE---SPAKFALYKrCHREDQVYacKLSDREHPLYLRL 169
Cdd:cd01782  42 VSSTATTQDVIETLIEKFRPDMrmlSNPRYSLYE-VHPNGEER--KLDDDEKPLVVQL 96
SARAH_MST_Hpo cd21884
C-terminal SARAH domain found in the mammalian STE20-like protein kinase (MST) subfamily; The ...
194-231 9.29e-03

C-terminal SARAH domain found in the mammalian STE20-like protein kinase (MST) subfamily; The MST subfamily includes MST1 and MST2, as well as Drosophila melanogaster homolog protein, Hippo (Hpo). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 and MST2 are STE20 family stress-activated, pro-apoptotic serine/threonine-protein kinases which, following caspase-cleavage, enter the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. They are key components of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. Hpo, also called STE20-like kinase MST (dMST), is the Drosophila homolog of STE20-like protein kinases, MST1 and MST2. It is a STE20 family serine/threonine-protein kinase that functions as a tumor suppressor by restricting cell proliferation, and promotes apoptosis in conjunction with salvador and warts. Hpo plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain of mammalian STE20-like protein kinases and the Drosophila melanogaster homolog Hippo.


Pssm-ID: 439178  Cd Length: 48  Bit Score: 33.36  E-value: 9.29e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 30039698 194 SLPELQNFLRILDKEEDEQLQNLKRRYTAYRQKLEEAL 231
Cdd:cd21884   8 SYEELQERLALLDPEMEREIEELRKRYQAKRQPILDAI 45
 
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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