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Conserved domains on  [gi|2054315979|emb|CAG2209838|]
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RASSF9_10 [Mytilus edulis]

Protein Classification

ubiquitin family protein( domain architecture ID 13006353)

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_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 40-122 1.02e-41

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: 144.31  E-value: 1.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979  40 EIPVWFTGTQRWVTGLTKRTTCDDVIYALLYNDGKHEDerTDKYTVYERWRDVERPLQGRTKILKIWKAWDEEQRNVQLS 119
Cdd:cd16123     1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQTND--TGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFV 78


                  ...
gi 2054315979 120 MRH 122
Cdd:cd16123    79 LRR 81
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
154-377 2.39e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979 154 PKESTHKHKSSNRLKSIDDLAKTVIKQERKLHDMGYRLEgIDKEIELYETNVHQTRMQTNGTDYVQDAYLKGgLEDSMDE 233
Cdd:COG4717   297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELEEELQLEE-LEQEIAA 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979 234 FLRKIGPDSLEMYIEFCERVLQLESKIKKENSIVQELSyQINEEASFNQAFCGNDNVFEKEfcnSELETELSSLQAELNR 313
Cdd:COG4717   375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLE-ELLGELEELLEALDEEELEEEL---EELEEELEELEEELEE 450

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2054315979 314 IVSanmmqkyEAAEIAREIdtcdKVLSDkQKTIQTLQKELEILdrfenENKVSSEVQEYRAADL 377
Cdd:COG4717   451 LRE-------ELAELEAEL----EQLEE-DGELAELLQELEEL-----KAELRELAEEWAALKL 497
 
Name Accession Description Interval E-value
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 40-122 1.02e-41

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: 144.31  E-value: 1.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979  40 EIPVWFTGTQRWVTGLTKRTTCDDVIYALLYNDGKHEDerTDKYTVYERWRDVERPLQGRTKILKIWKAWDEEQRNVQLS 119
Cdd:cd16123     1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQTND--TGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFV 78


                  ...
gi 2054315979 120 MRH 122
Cdd:cd16123    79 LRR 81
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
154-377 2.39e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979 154 PKESTHKHKSSNRLKSIDDLAKTVIKQERKLHDMGYRLEgIDKEIELYETNVHQTRMQTNGTDYVQDAYLKGgLEDSMDE 233
Cdd:COG4717   297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELEEELQLEE-LEQEIAA 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979 234 FLRKIGPDSLEMYIEFCERVLQLESKIKKENSIVQELSyQINEEASFNQAFCGNDNVFEKEfcnSELETELSSLQAELNR 313
Cdd:COG4717   375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLE-ELLGELEELLEALDEEELEEEL---EELEEELEELEEELEE 450

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2054315979 314 IVSanmmqkyEAAEIAREIdtcdKVLSDkQKTIQTLQKELEILdrfenENKVSSEVQEYRAADL 377
Cdd:COG4717   451 LRE-------ELAELEAEL----EQLEE-DGELAELLQELEEL-----KAELRELAEEWAALKL 497
 
Name Accession Description Interval E-value
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 40-122 1.02e-41

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: 144.31  E-value: 1.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979  40 EIPVWFTGTQRWVTGLTKRTTCDDVIYALLYNDGKHEDerTDKYTVYERWRDVERPLQGRTKILKIWKAWDEEQRNVQLS 119
Cdd:cd16123     1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQTND--TGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFV 78


                  ...
gi 2054315979 120 MRH 122
Cdd:cd16123    79 LRR 81
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 40-126 9.14e-20

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: 84.13  E-value: 9.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979  40 EIPVWFTGTQRWVTGLTKRTTCDDVIYALLY-NDGKHEDER-----TDKYTVYERWRDVERPLQGRTKILKIWKAWDEEQ 113
Cdd:cd16133     1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEeHEATFGEKRfllgqPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80

                          90
                  ....*....|...
gi 2054315979 114 RNVQLSMRHVDEF 126
Cdd:cd16133    81 PNLQFVLVKADAF 93
RA_RASSF10 cd16132
Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); ...
 40-117 1.05e-16

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: 75.71  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979  40 EIPVWFTGTQRWVTGLTKRTTCDDVIYALLyNDGKHEDERT----------------DKYTVYERWRDVERPLQGRTKIL 103
Cdd:cd16132     1 KISVWLCQEEKLVSGLSRRTTCADVVRVLL-EDQNRSQQEEeeeegerdggmlsgppQSYCIVEKWRGFERILPNKTKIL 79

                          90
                  ....*....|....
gi 2054315979 104 KIWKAWDEEQRNVQ 117
Cdd:cd16132    80 RLWAAWGEEQENVR 93
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 40-121 2.26e-16

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: 74.01  E-value: 2.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979  40 EIPVWFTGTQRWVTGLTKRTTCDDVIYALLYNDGkhedeRTDKYTVYERWRDVERPLQGRTKILKIWKAWDEEQRNVQLS 119
Cdd:cd16134     1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATG-----RTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFI 75


                  ..
gi 2054315979 120 MR 121
Cdd:cd16134    76 LR 77
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 40-96 1.80e-07

Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); RASSF7, also termed HRAS1-related cluster protein 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 protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF7 is a potential Ras effector as its function has been linked to some key biological processes including the regulation of cell death and proliferation; for example, RASSF7 is up-regulated in pancreatic cancer.


Pssm-ID: 340552  Cd Length: 83  Bit Score: 48.79  E-value: 1.80e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2054315979  40 EIPVWFTGTQRWVTGLTKRTTCDDVIYALLYNDGKhederTDKYTVYERWRDVERPL 96
Cdd:cd16135     2 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQ-----TGRYVLIQKLRDKERQL 53
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 56-122 1.57e-03

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: 37.68  E-value: 1.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979  56 TKRTTCDDVIYALLyndGKHE-DERTDKYTVYERW--RDVERPLQGRTKILKIWKAWDEEQRNVQLSMRH 122
Cdd:cd17043    21 SSTTTAREVVQLLL---EKYGlEEDPEDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTEFRFVLKR 87
RA_ASPP1_2 cd16125
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ...
 33-122 1.68e-03

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: 37.28  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979  33 DGTEAVTEIPVwftgtqrwvtglTKRTTCDDVIyallynDGKHEDERTDKYTVyERWRDVERPLQGRTKILKIWKAWDEE 112
Cdd:cd16125     9 DNNQTVTEVPI------------TPETTCQDVV------DCCKEPGEENCHLV-EVWRGCERPLPEEENPYEILQQWGSH 69

                          90
                  ....*....|
gi 2054315979 113 QRNVQLSMRH 122
Cdd:cd16125    70 RDEVKFFLRH 79
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
154-377 2.39e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979 154 PKESTHKHKSSNRLKSIDDLAKTVIKQERKLHDMGYRLEgIDKEIELYETNVHQTRMQTNGTDYVQDAYLKGgLEDSMDE 233
Cdd:COG4717   297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELEEELQLEE-LEQEIAA 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979 234 FLRKIGPDSLEMYIEFCERVLQLESKIKKENSIVQELSyQINEEASFNQAFCGNDNVFEKEfcnSELETELSSLQAELNR 313
Cdd:COG4717   375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLE-ELLGELEELLEALDEEELEEEL---EELEEELEELEEELEE 450

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2054315979 314 IVSanmmqkyEAAEIAREIdtcdKVLSDkQKTIQTLQKELEILdrfenENKVSSEVQEYRAADL 377
Cdd:COG4717   451 LRE-------ELAELEAEL----EQLEE-DGELAELLQELEEL-----KAELRELAEEWAALKL 497
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
251-354 5.80e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.46  E-value: 5.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054315979 251 ERVLQLESKIKKENSIVQELSYQINEeasfnqafcgndnvfeKEFCNSELETELSSLQAELNRIVSANMmqkyEAAEIAR 330
Cdd:COG2433   413 EEIRRLEEQVERLEAEVEELEAELEE----------------KDERIERLERELSEARSEERREIRKDR----EISRLDR 472

                          90       100
                  ....*....|....*....|....
gi 2054315979 331 EIDTCDKVLSDKQKTIQTLQKELE 354
Cdd:COG2433   473 EIERLERELEEERERIEELKRKLE 496
 
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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