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Conserved domains on  [gi|568936262|ref|XP_006535307|]
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ras association domain-containing protein 6 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
207-293 3.06e-47

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd17223:

Pssm-ID: 452900  Cd Length: 87  Bit Score: 155.00  E-value: 3.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936262 207 DHETSIFTPTFGSETKVRANSIMRTEEVIKQLLQKFKIENSPRDFALYIIFGTGEQRKLKKTDVPLLQRLLQGPSKSNAR 286
Cdd:cd17223    1 NYKTSVFTPAFGSETKVRINSNMTTQEVIKQLLQKFKIENSPNEFALYIIHATGEKKRLKNTDFPLWERLLQGPSGKIAK 80

                 ....*..
gi 568936262 287 IFLMDKD 293
Cdd:cd17223   81 MFLMDKD 87
SARAH_RASSF6 cd21895
C-terminal SARAH domain found in Ras-association domain-containing protein 6 (RASSF6); RASSF6 ...
304-348 2.77e-16

C-terminal SARAH domain found in Ras-association domain-containing protein 6 (RASSF6); RASSF6 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 tumor suppressor protein involved in the induction of apoptosis, through both caspase-dependent and caspase-independent pathways. RASSF6 may function as a Ras effector protein. It is ubiquitinated and degraded by interacting with MDM2 to stabilize P53, and it regulates apoptosis and the cell cycle. RASSF6 is expressed as four transcripts via alternative splicing. All transcript variants of RASSF6 contain the RA and SARAH (Salvador-RassF-Hippo) domains. The RA domain of the classical RASSF proteins 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. This model corresponds to the SARAH domain of RASSF6.


:

Pssm-ID: 439189  Cd Length: 46  Bit Score: 71.97  E-value: 2.77e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568936262 304 YINFHFSFLESILQRLDEEEKMEIERIMAKFNTERAFILKCLQSK 348
Cdd:cd21895    2 YINFELPFLESILQKLNEEEEREIQKIVAKYKKEKAILLQCLRSK 46
 
Name Accession Description Interval E-value
RA_RASSF6 cd17223
Ras-associating (RA) domain found in Ras-association domain-containing protein 6 (RASSF6); ...
207-293 3.06e-47

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: 155.00  E-value: 3.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936262 207 DHETSIFTPTFGSETKVRANSIMRTEEVIKQLLQKFKIENSPRDFALYIIFGTGEQRKLKKTDVPLLQRLLQGPSKSNAR 286
Cdd:cd17223    1 NYKTSVFTPAFGSETKVRINSNMTTQEVIKQLLQKFKIENSPNEFALYIIHATGEKKRLKNTDFPLWERLLQGPSGKIAK 80

                 ....*..
gi 568936262 287 IFLMDKD 293
Cdd:cd17223   81 MFLMDKD 87
SARAH_RASSF6 cd21895
C-terminal SARAH domain found in Ras-association domain-containing protein 6 (RASSF6); RASSF6 ...
304-348 2.77e-16

C-terminal SARAH domain found in Ras-association domain-containing protein 6 (RASSF6); RASSF6 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 tumor suppressor protein involved in the induction of apoptosis, through both caspase-dependent and caspase-independent pathways. RASSF6 may function as a Ras effector protein. It is ubiquitinated and degraded by interacting with MDM2 to stabilize P53, and it regulates apoptosis and the cell cycle. RASSF6 is expressed as four transcripts via alternative splicing. All transcript variants of RASSF6 contain the RA and SARAH (Salvador-RassF-Hippo) domains. The RA domain of the classical RASSF proteins 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. This model corresponds to the SARAH domain of RASSF6.


Pssm-ID: 439189  Cd Length: 46  Bit Score: 71.97  E-value: 2.77e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568936262 304 YINFHFSFLESILQRLDEEEKMEIERIMAKFNTERAFILKCLQSK 348
Cdd:cd21895    2 YINFELPFLESILQKLNEEEEREIQKIVAKYKKEKAILLQCLRSK 46
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
206-294 2.13e-12

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: 62.35  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936262  206 YDHETSIFTP--TFGSETK-VRANSIMRTEEVIKQLLQKFKIENSPRDFALY-IIFGTGEQRKLKKTDVPLLQRLLQGPS 281
Cdd:pfam00788   1 DDGVLKVYTEdgKPGTTYKtILVSSSTTAEEVIEALLEKFGLEDDPRDYVLVeVLERGGGERRLPDDECPLQIQLQWPRD 80
                          90
                  ....*....|...
gi 568936262  282 KSNARIFLMDKDA 294
Cdd:pfam00788  81 ASDSRFLLRKRDD 93
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
204-293 1.89e-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: 59.62  E-value: 1.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936262   204 HVYDHETSIFTPTFGSETKVRANSIMRTEEVIKQLLQKFKIENSPRDFALYIIFGTGEQRKLKKTDVPLLQRLLQGPSKS 283
Cdd:smart00314   1 DTFVLRVYVDDLPGGTYKTLRVSSRTTARDVIQQLLEKFHLTDDPEEYVLVEVLPDGKERVLPDDENPLQLQKLWPRRGP 80
                           90
                   ....*....|
gi 568936262   284 NARIFLMDKD 293
Cdd:smart00314  81 NLRFVLRKRD 90
Nore1-SARAH pfam16517
Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain; The Nore1-SARAH, C-terminal, ...
306-345 1.50e-08

Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain; The Nore1-SARAH, C-terminal, domain of Nore1, the tumor-suppressor, a novel Ras effector, has a characteristic 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 characteristics 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: 49.80  E-value: 1.50e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568936262  306 NFHFSFLESILQRLDEEEKMEIERIMAKFNTERAFILKCL 345
Cdd:pfam16517   1 AFSLPELENFLRILDEEEEREIQQIRRKYTALRQKLQQAL 40
 
Name Accession Description Interval E-value
RA_RASSF6 cd17223
Ras-associating (RA) domain found in Ras-association domain-containing protein 6 (RASSF6); ...
207-293 3.06e-47

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: 155.00  E-value: 3.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936262 207 DHETSIFTPTFGSETKVRANSIMRTEEVIKQLLQKFKIENSPRDFALYIIFGTGEQRKLKKTDVPLLQRLLQGPSKSNAR 286
Cdd:cd17223    1 NYKTSVFTPAFGSETKVRINSNMTTQEVIKQLLQKFKIENSPNEFALYIIHATGEKKRLKNTDFPLWERLLQGPSGKIAK 80

                 ....*..
gi 568936262 287 IFLMDKD 293
Cdd:cd17223   81 MFLMDKD 87
RA_RASSF2_like cd01784
Ras-associating (RA) domain found in Ras-association domain family members, RASSF2, RASSF4, ...
207-293 4.72e-43

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: 143.93  E-value: 4.72e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936262 207 DHETSIFTPTFGSETKVRANSIMRTEEVIKQLLQKFKIENSPRDFALYIIFGTGEQRKLKKTDVPLLQRLLQGPSKSNAR 286
Cdd:cd01784    1 NRKTSVFTPPYGSVTNVRVTSLMTTPEVIKLLLEKFKVENSPEEFALYVVKDSGERRRLKDDDYPLLTRVLLGPSEDVAK 80

                 ....*..
gi 568936262 287 IFLMDKD 293
Cdd:cd01784   81 IFIMERA 87
RA_RASSF2 cd17221
Ras-associating (RA) domain found in Ras-association domain-containing protein 2 (RASSF2); ...
207-293 8.21e-35

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: 122.78  E-value: 8.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936262 207 DHETSIFTPTFGSETKVRANSIMRTEEVIKQLLQKFKIENSPRDFALYIIFGTGEQRKLKKTDVPLLQRLLQGPSKSNAR 286
Cdd:cd17221    1 NHKTSVFTPAYGSVTNVRINSTMTTPQVLKLLLNKFKIENSAEEFALYIVHTSGEKQKLKATDYPLIARILQGPCEQVSK 80

                 ....*..
gi 568936262 287 IFLMDKD 293
Cdd:cd17221   81 VFLMEKD 87
RA_RASSF4 cd17222
Ras-associating (RA) domain found in Ras-association domain-containing protein 4 (RASSF4); ...
207-293 1.04e-29

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: 109.19  E-value: 1.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936262 207 DHETSIFTPTFGSETKVRANSIMRTEEVIKQLLQKFKIENSPRDFALYIIFGTGEQRKLKKTDVPLLQRLLQGPSKSNAR 286
Cdd:cd17222    1 NHKTSVFTPAYGSVTNVRVNSTMTTPQVLKLLLNKFRVENSPDEFALYLVHESGERTKLKDTEYPLISRILHGPCEKIAR 80

                 ....*..
gi 568936262 287 IFLMDKD 293
Cdd:cd17222   81 IFLMETD 87
SARAH_RASSF6 cd21895
C-terminal SARAH domain found in Ras-association domain-containing protein 6 (RASSF6); RASSF6 ...
304-348 2.77e-16

C-terminal SARAH domain found in Ras-association domain-containing protein 6 (RASSF6); RASSF6 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 tumor suppressor protein involved in the induction of apoptosis, through both caspase-dependent and caspase-independent pathways. RASSF6 may function as a Ras effector protein. It is ubiquitinated and degraded by interacting with MDM2 to stabilize P53, and it regulates apoptosis and the cell cycle. RASSF6 is expressed as four transcripts via alternative splicing. All transcript variants of RASSF6 contain the RA and SARAH (Salvador-RassF-Hippo) domains. The RA domain of the classical RASSF proteins 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. This model corresponds to the SARAH domain of RASSF6.


Pssm-ID: 439189  Cd Length: 46  Bit Score: 71.97  E-value: 2.77e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568936262 304 YINFHFSFLESILQRLDEEEKMEIERIMAKFNTERAFILKCLQSK 348
Cdd:cd21895    2 YINFELPFLESILQKLNEEEEREIQKIVAKYKKEKAILLQCLRSK 46
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
206-294 2.13e-12

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: 62.35  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936262  206 YDHETSIFTP--TFGSETK-VRANSIMRTEEVIKQLLQKFKIENSPRDFALY-IIFGTGEQRKLKKTDVPLLQRLLQGPS 281
Cdd:pfam00788   1 DDGVLKVYTEdgKPGTTYKtILVSSSTTAEEVIEALLEKFGLEDDPRDYVLVeVLERGGGERRLPDDECPLQIQLQWPRD 80
                          90
                  ....*....|...
gi 568936262  282 KSNARIFLMDKDA 294
Cdd:pfam00788  81 ASDSRFLLRKRDD 93
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
204-293 1.89e-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: 59.62  E-value: 1.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936262   204 HVYDHETSIFTPTFGSETKVRANSIMRTEEVIKQLLQKFKIENSPRDFALYIIFGTGEQRKLKKTDVPLLQRLLQGPSKS 283
Cdd:smart00314   1 DTFVLRVYVDDLPGGTYKTLRVSSRTTARDVIQQLLEKFHLTDDPEEYVLVEVLPDGKERVLPDDENPLQLQKLWPRRGP 80
                           90
                   ....*....|
gi 568936262   284 NARIFLMDKD 293
Cdd:smart00314  81 NLRFVLRKRD 90
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
221-290 7.15e-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: 55.02  E-value: 7.15e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568936262 221 TKVRANSIMRTEEVIKQLLQKFKIENSPRDFALYIIFGTGE-QRKLKKTDVPLLQRLLQGPSKSNARIFLM 290
Cdd:cd17043   16 KSILVSSTTTAREVVQLLLEKYGLEEDPEDYSLYEVSEKQEtERVLHDDECPLLIQLEWGPQGTEFRFVLK 86
Nore1-SARAH pfam16517
Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain; The Nore1-SARAH, C-terminal, ...
306-345 1.50e-08

Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain; The Nore1-SARAH, C-terminal, domain of Nore1, the tumor-suppressor, a novel Ras effector, has a characteristic 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 characteristics 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: 49.80  E-value: 1.50e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568936262  306 NFHFSFLESILQRLDEEEKMEIERIMAKFNTERAFILKCL 345
Cdd:pfam16517   1 AFSLPELENFLRILDEEEEREIQQIRRKYTALRQKLQQAL 40
SARAH_RASSF2-like cd21886
C-terminal SARAH domain found in Ras-association domain proteins, RASSF2, RASSF4, and RASSF6; ...
304-347 1.46e-07

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: 47.15  E-value: 1.46e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568936262 304 YINFHFSFLESILQRLDEEEKMEIERIMAKFNTERAFILKCLQS 347
Cdd:cd21886    2 YLNFSMPELRAFLRKFQEEEEREVEKIKEKYEELKRRIKKRMEE 45
RA_RASSF1_like cd01778
Ras-associating (RA) domain found in Ras-association domain family members, RASSF1, RASSF3, ...
226-289 2.66e-07

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: 48.82  E-value: 2.66e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568936262 226 NSIMRTEEVIKQLLQKFKIENSPRDFALY----IIFGTGEQRKLKKTDVPLLQRLLQGPSKSNARIFL 289
Cdd:cd01778   60 TSDTTAREVIEALLKKFKITDNPRKFALYerthEEEGKVKLRKLSDDERPLYLCLLWGSQGDSKSFVL 127
RA_RASSF5 cd17220
Ras-associating (RA) domain of Ras-association domain family 5 (RASSF5); RASSF5, also called ...
207-280 9.28e-07

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: 47.93  E-value: 9.28e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936262 207 DHETSIFTPtFGSETKVRANSIMRTEEVIKQLLQKFKIENSPRDFALYIIFGTGEQ---RKLKKTDVPLLQRLLQGP 280
Cdd:cd17220   65 DKRTSFYLP-LDAIKQLHISSTTTVSEVIQGLLKKFMVVDNPQKFALFKRMRKDGQvlfQKLPLTEYPLYLRLLAGP 140
RA_RASSF1 cd17218
Ras-associating (RA) domain found in Ras-association domain-containing protein 1 (RASSF1); ...
227-281 7.39e-06

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: 45.61  E-value: 7.39e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568936262 227 SIMRTEEVIKQLLQKFKIENSPRDFALYIIFGTGEQ---RKLKKTDVPLLQRLLQGPS 281
Cdd:cd17218   89 SKTRASEVIEALLKKFTVVDNPRKFALFERTEKDDQvylRKLSDDEQPLYLRLLAGPN 146
RA1_Afadin cd01782
Ras-associating (RA) domain 1 found in Afadin; Afadin, also termed ALL1-fused gene from ...
221-276 4.38e-05

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: 42.33  E-value: 4.38e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936262 221 TK-VRANSIMRTEEVIKQLLQKFKIEN---SPRDFALYIIFGTGEQRKLKKTDVPLLQRL 276
Cdd:cd01782   37 TKcIRVSSTATTQDVIETLIEKFRPDMrmlSNPRYSLYEVHPNGEERKLDDDEKPLVVQL 96
RA_RASSF3 cd17219
Ras-associating (RA) domain found in Ras-association domain-containing protein 3 (RASSF3); ...
209-281 7.11e-05

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: 42.17  E-value: 7.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568936262 209 ETSIFTPTfGSETKVRANSIMRTEEVIKQLLQKFKIENSPRDFALYIIFGTGEQR---KLKKTDVPLLQRLLQGPS 281
Cdd:cd17219   56 ETAFYLPK-GSVNTLHISSTNTVREVIEALLKKFLVADNPAKFALYKRCHKEDQVyacKLSDREHPLYLRLVAGPN 130
RA_STE50 cd01786
Ras-associating (RA) domain found in the fungal adaptor protein STE50; The fungal adaptor ...
230-276 7.35e-03

Ras-associating (RA) domain found in the fungal adaptor protein STE50; The fungal adaptor protein STE50 is an essential component of three MAPK-mediated signaling pathways that control the mating response, invasive/filamentous growth and osmotolerance (HOG pathway), respectively. STE50 functions in cell signaling between the activated G protein and STE11. The domain architecture of STE50 includes an amino-terminal SAM (sterile alpha motif) domain in addition to the carboxy-terminal ubiquitin-like RA (RAS-associated) domain. RA domain of STE50 interacts with the small GTPase Cdc42p, a member of Rho type of the Ras superfamily. This interaction activates Ste11p/Ste7p/Kss1pMAP kinase cascade that controls filamentous growth. 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 in eukaryotes.


Pssm-ID: 340484  Cd Length: 101  Bit Score: 35.77  E-value: 7.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568936262 230 RTEEVIKQLLQKFKIENSPRDFALYIIFGTGEqRKLKKTDVPLL--QRL 276
Cdd:cd01786   40 PCAKVLPAALKKYKINGDWRQYALFIAYGDKE-RCLSYDEKPLLvfQRL 87
SARAH_RASSF2 cd21893
C-terminal SARAH domain found in Ras-association domain-containing protein 2 (RASSF2); RASSF2 ...
304-346 7.49e-03

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: 34.02  E-value: 7.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568936262 304 YINFHFSFLESILQRLDEEEKMEIERIMAKFNTERAFILKCLQ 346
Cdd:cd21893    2 YIKFEMPVLKSFIQKLKEEEDREVKKLMRRYTVLRLMIEQRLQ 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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