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Conserved domains on  [gi|393715061|ref|NP_001257320|]
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ras association domain-containing protein 6 isoform c [Homo sapiens]

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 ...
 189-239 2.13e-24

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: 475130  Cd Length: 87  Bit Score: 94.14  E-value: 2.13e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 393715061 189 EIENSPQDFALHIIFATGEQRRLKKTDIPLLQRLLQGPSEKNARIFLMDKD 239
Cdd:cd17223   37 KIENSPNEFALYIIHATGEKKRLKNTDFPLWERLLQGPSGKIAKMFLMDKD 87
SARAH_RASSF6 cd21895
C-terminal SARAH domain found in Ras-association domain-containing protein 6 (RASSF6); RASSF6 ...
 249-294 4.44e-19

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: 78.91  E-value: 4.44e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 393715061 249 QYINFHFSLLESILQRLNEEEKREIQRIVTKFNKEKAIILKCLQNK 294
Cdd:cd21895    1 QYINFELPFLESILQKLNEEEEREIQKIVAKYKKEKAILLQCLRSK 46
 
Name Accession Description Interval E-value
RA_RASSF6 cd17223
Ras-associating (RA) domain found in Ras-association domain-containing protein 6 (RASSF6); ...
 189-239 2.13e-24

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: 94.14  E-value: 2.13e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 393715061 189 EIENSPQDFALHIIFATGEQRRLKKTDIPLLQRLLQGPSEKNARIFLMDKD 239
Cdd:cd17223   37 KIENSPNEFALYIIHATGEKKRLKNTDFPLWERLLQGPSGKIAKMFLMDKD 87
SARAH_RASSF6 cd21895
C-terminal SARAH domain found in Ras-association domain-containing protein 6 (RASSF6); RASSF6 ...
 249-294 4.44e-19

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: 78.91  E-value: 4.44e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 393715061 249 QYINFHFSLLESILQRLNEEEKREIQRIVTKFNKEKAIILKCLQNK 294
Cdd:cd21895    1 QYINFELPFLESILQKLNEEEEREIQKIVAKYKKEKAILLQCLRSK 46
Nore1-SARAH pfam16517
Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain; The Nore1-SARAH, C-terminal, ...
 252-291 8.88e-10

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: 53.27  E-value: 8.88e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 393715061  252 NFHFSLLESILQRLNEEEKREIQRIVTKFNKEKAIILKCL 291
Cdd:pfam16517   1 AFSLPELENFLRILDEEEEREIQQIRRKYTALRQKLQQAL 40
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 190-240 6.38e-03

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: 35.39  E-value: 6.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 393715061  190 IENSPQDFAL-HIIFATGEQRRLKKTDIPLLQRLLQGPSEKNARIFLMDKDA 240
Cdd:pfam00788  42 LEDDPRDYVLvEVLERGGGERRLPDDECPLQIQLQWPRDASDSRFLLRKRDD 93
 
Name Accession Description Interval E-value
RA_RASSF6 cd17223
Ras-associating (RA) domain found in Ras-association domain-containing protein 6 (RASSF6); ...
 189-239 2.13e-24

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: 94.14  E-value: 2.13e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 393715061 189 EIENSPQDFALHIIFATGEQRRLKKTDIPLLQRLLQGPSEKNARIFLMDKD 239
Cdd:cd17223   37 KIENSPNEFALYIIHATGEKKRLKNTDFPLWERLLQGPSGKIAKMFLMDKD 87
RA_RASSF2_like cd01784
Ras-associating (RA) domain found in Ras-association domain family members, RASSF2, RASSF4, ...
 190-239 8.44e-22

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: 87.31  E-value: 8.44e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 393715061 190 IENSPQDFALHIIFATGEQRRLKKTDIPLLQRLLQGPSEKNARIFLMDKD 239
Cdd:cd01784   38 VENSPEEFALYVVKDSGERRRLKDDDYPLLTRVLLGPSEDVAKIFIMERA 87
SARAH_RASSF6 cd21895
C-terminal SARAH domain found in Ras-association domain-containing protein 6 (RASSF6); RASSF6 ...
 249-294 4.44e-19

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: 78.91  E-value: 4.44e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 393715061 249 QYINFHFSLLESILQRLNEEEKREIQRIVTKFNKEKAIILKCLQNK 294
Cdd:cd21895    1 QYINFELPFLESILQKLNEEEEREIQKIVAKYKKEKAILLQCLRSK 46
RA_RASSF2 cd17221
Ras-associating (RA) domain found in Ras-association domain-containing protein 2 (RASSF2); ...
 189-239 1.97e-16

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: 73.09  E-value: 1.97e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 393715061 189 EIENSPQDFALHIIFATGEQRRLKKTDIPLLQRLLQGPSEKNARIFLMDKD 239
Cdd:cd17221   37 KIENSAEEFALYIVHTSGEKQKLKATDYPLIARILQGPCEQVSKVFLMEKD 87
RA_RASSF4 cd17222
Ras-associating (RA) domain found in Ras-association domain-containing protein 4 (RASSF4); ...
 190-239 1.09e-13

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: 65.28  E-value: 1.09e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 393715061 190 IENSPQDFALHIIFATGEQRRLKKTDIPLLQRLLQGPSEKNARIFLMDKD 239
Cdd:cd17222   38 VENSPDEFALYLVHESGERTKLKDTEYPLISRILHGPCEKIARIFLMETD 87
SARAH_RASSF2-like cd21886
C-terminal SARAH domain found in Ras-association domain proteins, RASSF2, RASSF4, and RASSF6; ...
 249-292 3.92e-10

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: 54.46  E-value: 3.92e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 393715061 249 QYINFHFSLLESILQRLNEEEKREIQRIVTKFNKEKAIILKCLQ 292
Cdd:cd21886    1 QYLNFSMPELRAFLRKFQEEEEREVEKIKEKYEELKRRIKKRME 44
Nore1-SARAH pfam16517
Novel Ras effector 1 C-terminal SARAH (Sav/Rassf/Hpo) domain; The Nore1-SARAH, C-terminal, ...
 252-291 8.88e-10

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: 53.27  E-value: 8.88e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 393715061  252 NFHFSLLESILQRLNEEEKREIQRIVTKFNKEKAIILKCL 291
Cdd:pfam16517   1 AFSLPELENFLRILDEEEEREIQQIRRKYTALRQKLQQAL 40
SARAH_RASSF4 cd21894
C-terminal SARAH domain found in Ras-association domain-containing protein 4 (RASSF4); RASSF4 ...
 249-294 1.35e-04

C-terminal SARAH domain found in Ras-association domain-containing protein 4 (RASSF4); RASSF4 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 also functions as a KRAS effector protein. RASSF4 is broadly expressed in normal tissues. Its expression is reduced in tumor cell lines and primary tumors by promoter specific hypermethylation. RASSF4 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 RASSF4.


Pssm-ID: 439188  Cd Length: 46  Bit Score: 38.99  E-value: 1.35e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 393715061 249 QYINFHFSLLESILQRLNEEEKREIQRIVTKFNKEKAIILKCLQNK 294
Cdd:cd21894    1 QYIKFEMPVLDSFVEKLKEEEEREIIKLTRKYSALRSMILQQLEQL 46
SARAH_RASSF2 cd21893
C-terminal SARAH domain found in Ras-association domain-containing protein 2 (RASSF2); RASSF2 ...
 249-292 6.78e-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: 36.71  E-value: 6.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 393715061 249 QYINFHFSLLESILQRLNEEEKREIQRIVTKFNKEKAIILKCLQ 292
Cdd:cd21893    1 QYIKFEMPVLKSFIQKLKEEEDREVKKLMRRYTVLRLMIEQRLQ 44
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 190-240 6.38e-03

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: 35.39  E-value: 6.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 393715061  190 IENSPQDFAL-HIIFATGEQRRLKKTDIPLLQRLLQGPSEKNARIFLMDKDA 240
Cdd:pfam00788  42 LEDDPRDYVLvEVLERGGGERRLPDDECPLQIQLQWPRDASDSRFLLRKRDD 93
 
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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