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Conserved domains on  [gi|5821937]
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Chain B, PROTO-ONCOGENE SERINE/THREONINE PROTEIN KINASE RAF-1

Protein Classification

RBD_CRAF domain-containing protein( domain architecture ID 13019455)

RBD_CRAF domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RBD_CRAF cd17135
Ras-binding domain (RBD) found in RAF proto-oncogene serine/threonine-protein kinase RAF1/CRAF; ...
 1-77 6.65e-54

Ras-binding domain (RBD) found in RAF proto-oncogene serine/threonine-protein kinase RAF1/CRAF; RAF1/CRAF, also termed proto-oncogene c-RAF (cRaf), or Raf-1, belongs to the RAF family. The RAF family includes three RAF kinases ARAF, BRAF, and RAF1/CRAF, encoded by proto-oncogenes, which activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. RAF1/CRAF is an important effector of Ras-mediated signaling and is a critical regulator of the MAPK/ERK pathway.


:

Pssm-ID: 340655  Cd Length: 77  Bit Score: 161.18  E-value: 6.65e-54
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5821937   1 SNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFL 77
Cdd:cd17135  1 SNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFL 77
 
Name Accession Description Interval E-value
RBD_CRAF cd17135
Ras-binding domain (RBD) found in RAF proto-oncogene serine/threonine-protein kinase RAF1/CRAF; ...
 1-77 6.65e-54

Ras-binding domain (RBD) found in RAF proto-oncogene serine/threonine-protein kinase RAF1/CRAF; RAF1/CRAF, also termed proto-oncogene c-RAF (cRaf), or Raf-1, belongs to the RAF family. The RAF family includes three RAF kinases ARAF, BRAF, and RAF1/CRAF, encoded by proto-oncogenes, which activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. RAF1/CRAF is an important effector of Ras-mediated signaling and is a critical regulator of the MAPK/ERK pathway.


Pssm-ID: 340655  Cd Length: 77  Bit Score: 161.18  E-value: 6.65e-54
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5821937   1 SNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFL 77
Cdd:cd17135  1 SNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFL 77
RBD pfam02196
Raf-like Ras-binding domain;
3-75 2.76e-28

Raf-like Ras-binding domain;


Pssm-ID: 460485  Cd Length: 69  Bit Score: 96.05  E-value: 2.76e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5821937     3 TIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLlhehKGKKARLDWNTDAASLIGEELQVD 75
Cdd:pfam02196  1 LCRVYLPDGQRTVVQVRPGETVRDALSKLCKKRGLNPEACDVYLV----GGDKYPLDLDTDSSTLEGEEVRVE 69
RBD smart00455
Raf-like Ras-binding domain;
3-77 1.14e-27

Raf-like Ras-binding domain;


Pssm-ID: 128731  Cd Length: 70  Bit Score: 94.66  E-value: 1.14e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5821937      3 TIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLlhehkGKKARLDWNTDAASLIGEELQVDFL 77
Cdd:smart00455  1 TCKVHLPDNQRTVVKVRPGKTVRDALAKALKKRGLNPECCVVRLR-----GEKKPLDLNQPISSLDGQELVVEEL 70
 
Name Accession Description Interval E-value
RBD_CRAF cd17135
Ras-binding domain (RBD) found in RAF proto-oncogene serine/threonine-protein kinase RAF1/CRAF; ...
 1-77 6.65e-54

Ras-binding domain (RBD) found in RAF proto-oncogene serine/threonine-protein kinase RAF1/CRAF; RAF1/CRAF, also termed proto-oncogene c-RAF (cRaf), or Raf-1, belongs to the RAF family. The RAF family includes three RAF kinases ARAF, BRAF, and RAF1/CRAF, encoded by proto-oncogenes, which activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. RAF1/CRAF is an important effector of Ras-mediated signaling and is a critical regulator of the MAPK/ERK pathway.


Pssm-ID: 340655  Cd Length: 77  Bit Score: 161.18  E-value: 6.65e-54
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5821937   1 SNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFL 77
Cdd:cd17135  1 SNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFL 77
RBD_RAF cd01816
Ras-binding domain (RBD) found in RAF family serine/threonine kinases; The RAF family includes ...
 2-77 3.71e-33

Ras-binding domain (RBD) found in RAF family serine/threonine kinases; The RAF family includes three RAF serine/threonine kinases ARAF, BRAF, and RAF1/CRAF. These are encoded by proto-oncogenes, and activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340514  Cd Length: 71  Bit Score: 108.43  E-value: 3.71e-33
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5821937   2 NTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRllhehKGKKARLDWNTDAASLIGEELQVDFL 77
Cdd:cd01816  1 SVIRAHLPNQQRTTVEVKPGQTLREALEKAMKRRGLTPEMCVVYR-----KGTREPVSWDTDISTLEGEEISVEIL 71
RBD_ARAF cd17133
Ras-binding domain (RBD) found in serine/threonine-protein kinase ARAF; ARAF, also termed ...
 3-77 7.49e-32

Ras-binding domain (RBD) found in serine/threonine-protein kinase ARAF; ARAF, also termed proto-oncogene ARAF, or proto-oncogene ARAF1, or proto-oncogene PKS2, belongs to the RAF protein family. The RAF family includes three RAF kinases ARAF, BRAF, and RAF1/CRAF, encoded by proto-oncogenes, which activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. ARAF is predominantly found in urogenital tissue with a low basal kinase activity. It directly cross-talks with NODAL/SMAD2 signaling in a MAPK-independent manner. It also promotes MAPK pathway activation and cell migration in a cell type-dependent manner. Moreover, ARAF acts as a scaffold to stabilize BRAF-CRAF heterodimers. Mice deleted for ARAF are viable but die perinatally.


Pssm-ID: 340653  Cd Length: 73  Bit Score: 105.38  E-value: 7.49e-32
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5821937   3 TIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLhehKGKKARLDWNTDAASLIGEELQVDFL 77
Cdd:cd17133  2 TIKVYLPNKQRTVVNVRPGMTVYDSLDKALKVRGLNQDCCAVYRLI---KGRKTLTDWETDITPLVGEELLVEVL 73
RBD pfam02196
Raf-like Ras-binding domain;
3-75 2.76e-28

Raf-like Ras-binding domain;


Pssm-ID: 460485  Cd Length: 69  Bit Score: 96.05  E-value: 2.76e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5821937     3 TIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLlhehKGKKARLDWNTDAASLIGEELQVD 75
Cdd:pfam02196  1 LCRVYLPDGQRTVVQVRPGETVRDALSKLCKKRGLNPEACDVYLV----GGDKYPLDLDTDSSTLEGEEVRVE 69
RBD smart00455
Raf-like Ras-binding domain;
3-77 1.14e-27

Raf-like Ras-binding domain;


Pssm-ID: 128731  Cd Length: 70  Bit Score: 94.66  E-value: 1.14e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5821937      3 TIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLlhehkGKKARLDWNTDAASLIGEELQVDFL 77
Cdd:smart00455  1 TCKVHLPDNQRTVVKVRPGKTVRDALAKALKKRGLNPECCVVRLR-----GEKKPLDLNQPISSLDGQELVVEEL 70
RBD cd01760
Ras-binding domain (RBD), structurally similar to a beta-grasp ubiquitin-like fold; The RBD of ...
 2-76 1.02e-26

Ras-binding domain (RBD), structurally similar to a beta-grasp ubiquitin-like fold; The RBD of the serine/threonine kinase Raf is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. A Raf-like RBD is also present in Regulator of G protein Signaling (RGS12 and RGS14) members of GTPase activating proteins.


Pssm-ID: 340461  Cd Length: 71  Bit Score: 92.47  E-value: 1.02e-26
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5821937   2 NTIRVFLPN-KQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLlhehkGKKARLDWNTDAASLIGEELQVDF 76
Cdd:cd01760  1 NTFRLFLPNnETSVVVAVKPGKSLHEVLMPVLERHGLQLECVDVFLL-----GEKAPLDLNTDASSLIGQELRLDF 71
RBD_BRAF cd17134
Ras-binding domain (RBD) found in serine/threonine-protein kinase BRAF; BRAF, also termed ...
 4-77 2.72e-23

Ras-binding domain (RBD) found in serine/threonine-protein kinase BRAF; BRAF, also termed proto-oncogene B-Raf, or p94, or v-Raf murine sarcoma viral oncogene homolog B1, belongs to the RAF family. The RAF family includes three RAF kinases ARAF, BRAF, and RAF1/CRAF, encoded by proto-oncogenes, which activate the mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) cascade downstream of RAS. They share a common structure consisting of an N-terminal regulatory domain and a C-terminal kinase domain. There are three conserved regions (CR1-3) in the regulatory domain, CR1 contains a Ras-binding domain (RBD) and a cysteine-rich domain (CRD), CR2 is a serine/threonine-rich domain, and CR3 encodes the kinase domain required for RAF. The RBD of RAF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. BRAF is the most effective RAF kinase in terms of induction of MEK/ERK activity. It is somatically mutated in a number of human cancers.


Pssm-ID: 340654  Cd Length: 79  Bit Score: 83.92  E-value: 2.72e-23
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5821937   4 IRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLlheHKGKKARLDWNTDAASLIGEELQVDFL 77
Cdd:cd17134  4 VRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRI---QDGEKKPIGWDTDISWLTGEELHVEVL 74
Ubiquitin_like_fold cd00196
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ...
 4-75 2.52e-09

Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a ubiquitin-like manner but with biochemically distinct roles. Ubiquitin and ubiquitin-like proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some other ubiquitin-like domains have adaptor roles in ubiquitin-signaling by mediating protein-protein interaction. In addition to Ubiquitin-like (Ubl) domain, Ras-associating (RA) domain, F0/F1 sub-domain of FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, TGS (ThrRS, GTPase and SpoT) domain, Ras-binding domain (RBD), Ubiquitin regulatory domain X (UBX), Dublecortin-like domain, and RING finger- and WD40-associated ubiquitin-like (RAWUL) domain have beta-grasp ubiquitin-like folds, and are included in this superfamily.


Pssm-ID: 340450  Cd Length: 68  Bit Score: 48.09  E-value: 2.52e-09
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5821937   4 IRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLlhehkgkKARLDWNTDAA---SLIGEELQVD 75
Cdd:cd00196  1 VKVETPSLKKIVVAVPPSTTLRQVLEKVAKRIGLPPDVIRLLFN-------GQVLDDLMTAKqvgLEPGEELHFV 68
RBD1_RGS12_like cd01817
Ras-binding domain (RBD) 1 of regulator of G protein signaling 12 (RGS12) and similar proteins; ...
 5-75 9.31e-06

Ras-binding domain (RBD) 1 of regulator of G protein signaling 12 (RGS12) and similar proteins; Regulator of G protein signaling (RGS) proteins belong to a large family of GTpase-accelerating proteins (GAPs) which act as key inhibitors of G-protein-mediated cell responses in eukaryotes. This RGS12-like subfamily is composed of RGS12 and RGS14, with multidomain architectures including a RGS domain, two tandem Ras-binding domains (RBDs), and a second Galpha interacting domain, the GoLoco motif. The RBD is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340515  Cd Length: 70  Bit Score: 39.06  E-value: 9.31e-06
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5821937   5 RVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFrLLHEHKGkkarLDWNTDAASLIGEELQVD 75
Cdd:cd01817  4 RVILPDGSTTVVQAKPGETIRQLLTRLLEKRGLSYAAFDVF-IVGSDKP----LDLNEDSSILGGKEVRVE 69
 
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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