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Conserved domains on  [gi|304434798|ref|NP_001073990|]
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ras association domain-containing protein 10 [Homo sapiens]

Protein Classification

ubiquitin family protein( domain architecture ID 13006426)

ubiquitin family protein belongs to an diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RA_RASSF10 cd16132
Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); ...
 7-134 4.88e-55

Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); RASSF10 is a member of a family of N-terminus RASSF7-10 proteins. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF10 is expressed in a wide variety of tissues and its expression in human thyroid, pancreas, placenta, heart, lung and kidney has been observed. RASSF10 is the most frequently methylated of the N-terminal RASSFs in some cancers such as in childhood acute lymphoblastic leukemia and both, thyroid cancer cell lines and primary thyroid carcinomas.


:

Pssm-ID: 340549  Cd Length: 102  Bit Score: 179.71  E-value: 4.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434798   7 KISVWICQEEKLVSGLSRRTTCSDVVRVLLEDGCRRRRRQRRSRRlgsagdphgpgelpeppneddedddeALPQGMLCG 86
Cdd:cd16132    1 KISVWLCQEEKLVSGLSRRTTCADVVRVLLEDQNRSQQEEEEEEG--------------------------ERDGGMLSG 54

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 304434798  87 PPQCYCIVEKWRGFERILPNKTRILRLWAAWGEEQENVRFVLVRSEAS 134
Cdd:cd16132   55 PPQSYCIVEKWRGFERILPNKTKILRLWAAWGEEQENVRFVLVRSEAS 102
 
Name Accession Description Interval E-value
RA_RASSF10 cd16132
Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); ...
 7-134 4.88e-55

Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); RASSF10 is a member of a family of N-terminus RASSF7-10 proteins. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF10 is expressed in a wide variety of tissues and its expression in human thyroid, pancreas, placenta, heart, lung and kidney has been observed. RASSF10 is the most frequently methylated of the N-terminal RASSFs in some cancers such as in childhood acute lymphoblastic leukemia and both, thyroid cancer cell lines and primary thyroid carcinomas.


Pssm-ID: 340549  Cd Length: 102  Bit Score: 179.71  E-value: 4.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434798   7 KISVWICQEEKLVSGLSRRTTCSDVVRVLLEDGCRRRRRQRRSRRlgsagdphgpgelpeppneddedddeALPQGMLCG 86
Cdd:cd16132    1 KISVWLCQEEKLVSGLSRRTTCADVVRVLLEDQNRSQQEEEEEEG--------------------------ERDGGMLSG 54

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 304434798  87 PPQCYCIVEKWRGFERILPNKTRILRLWAAWGEEQENVRFVLVRSEAS 134
Cdd:cd16132   55 PPQSYCIVEKWRGFERILPNKTKILRLWAAWGEEQENVRFVLVRSEAS 102
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 88-132 3.23e-04

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: 39.59  E-value: 3.23e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 304434798    88 PQCYCIVEKW-RGFERILPNKTRILRLWAAWGEEQENVRFVLVRSE 132
Cdd:smart00314  45 PEEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNLRFVLRKRD 90
 
Name Accession Description Interval E-value
RA_RASSF10 cd16132
Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); ...
 7-134 4.88e-55

Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); RASSF10 is a member of a family of N-terminus RASSF7-10 proteins. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF10 is expressed in a wide variety of tissues and its expression in human thyroid, pancreas, placenta, heart, lung and kidney has been observed. RASSF10 is the most frequently methylated of the N-terminal RASSFs in some cancers such as in childhood acute lymphoblastic leukemia and both, thyroid cancer cell lines and primary thyroid carcinomas.


Pssm-ID: 340549  Cd Length: 102  Bit Score: 179.71  E-value: 4.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434798   7 KISVWICQEEKLVSGLSRRTTCSDVVRVLLEDGCRRRRRQRRSRRlgsagdphgpgelpeppneddedddeALPQGMLCG 86
Cdd:cd16132    1 KISVWLCQEEKLVSGLSRRTTCADVVRVLLEDQNRSQQEEEEEEG--------------------------ERDGGMLSG 54

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 304434798  87 PPQCYCIVEKWRGFERILPNKTRILRLWAAWGEEQENVRFVLVRSEAS 134
Cdd:cd16132   55 PPQSYCIVEKWRGFERILPNKTKILRLWAAWGEEQENVRFVLVRSEAS 102
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 8-130 5.70e-31

Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, RASSF9, and RASSF10; The RASSF family of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain either in the C-terminus (RASSF1-6) or N-terminus (RASSF7-10). RASSF7-10 lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The structural differences between the C-terminus and N-terminus RASSF subgroups have led to the suggestion that they are two distinct families. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ras proteins are small GTPases that are involved in cellular signal transduction. The N-terminus RASSF proteins are potential Ras effectors that have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia.


Pssm-ID: 340540  Cd Length: 81  Bit Score: 114.65  E-value: 5.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434798   8 ISVWICQEEKLVSGLSRRTTCSDVVRVLLEDGCrrrrrqrrsrrlgsagdphgpgelpeppneddedddealpqgmLCGP 87
Cdd:cd16123    2 LKVWVDGEERVVSGVTERTTCQDVIYALAQATG-------------------------------------------QTND 38

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 304434798  88 PQCYCIVEKWRGFERILPNKTRILRLWAAWGEEQENVRFVLVR 130
Cdd:cd16123   39 TGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLRR 81
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 7-133 6.40e-31

Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, also termed PAM COOH-terminal interactor protein 1 (P-CIP1), or peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor, is a member of N-terminus RASSF7-10 protein family. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of the N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF9 was formerly known as PAM COOH-terminal interactor-1 (P-CIP1) because of its interaction with peptidylglycine alpha-amidating mono-oxygenase (PAM) and possibility of its role in regulating the trafficking of integral membrane PAM. RASSF9 is widely expressed in multiple organs such as testis, kidney, skeletal muscle, liver, lung, brain, and heart. Cloned RASSF9 showed preferential binding to N-Ras and K-Ras.


Pssm-ID: 340550  Cd Length: 93  Bit Score: 114.94  E-value: 6.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434798   7 KISVWICQEEKLVSGLSRRTTCSDVVRVLLEDgcrrrrrqrrsrrlgsagDPHGPGElpeppneddedddealpQGMLCG 86
Cdd:cd16133    1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEE------------------HEATFGE-----------------KRFLLG 45

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 304434798  87 PPQCYCIVEKWRGFERILPNKTRILRLWAAWGEEQENVRFVLVRSEA 133
Cdd:cd16133   46 QPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQPNLQFVLVKADA 92
RA_ASPP1_2 cd16125
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ...
 86-128 6.35e-05

Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ASPP protein (apoptosis-stimulating protein of p53; also called ankyrin repeat-, Src homology 3 domain- and Pro-rich region-containing protein) plays a critical role in regulating apoptosis. The ASPP family consists of three members, ASPP1, ASPP2 and iASPP, all of which bind to p53 and regulate p53-mediated apoptosis. ASPP1 and ASPP2, have a RA domain at their N-terminus and have pro-apoptotic functions, while iASPP is involved in anti-apoptotic responses. 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 the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin.


Pssm-ID: 340542  Cd Length: 80  Bit Score: 41.52  E-value: 6.35e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 304434798  86 GPPQCYcIVEKWRGFERILPNKTRILRLWAAWGEEQENVRFVL 128
Cdd:cd16125   36 GEENCH-LVEVWRGCERPLPEEENPYEILQQWGSHRDEVKFFL 77
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 91-134 1.61e-04

Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); RASSF8, also termed carcinoma-associated protein HOJ-1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF8 has been described as a potential tumor suppressor. RASSF8 might have a role in the regulation of cell-cell adhesion and cell growth.


Pssm-ID: 340551  Cd Length: 82  Bit Score: 40.50  E-value: 1.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 304434798  91 YCIVEKWRGFERILPNKTRILRLWAAWGEEQENVRFVLVRSEAS 134
Cdd:cd16134   39 FTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTGPS 82
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 88-132 3.23e-04

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: 39.59  E-value: 3.23e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 304434798    88 PQCYCIVEKW-RGFERILPNKTRILRLWAAWGEEQENVRFVLVRSE 132
Cdd:smart00314  45 PEEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNLRFVLRKRD 90
 
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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