NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19114195|ref|NP_593283|]
View 

MAPK cascade adaptor protein Ste4 [Schizosaccharomyces pombe]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RA_STE50 cd01786
Ras-associating (RA) domain found in the fungal adaptor protein STE50; The fungal adaptor ...
 168-262 3.66e-29

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: 106.26  E-value: 3.66e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114195 168 VQPSPSVLGSFDLEV-------NDSLTNAEKNRKLNVNLTYNEVLCSMLQRYRIDpNTWMSYDLLINYDDKEHAIPMDVK 240
Cdd:cd01786   1 VSPTSSTIGSPELEPasprngiGPRPPEALKNRKVSVEDPCAKVLPAALKKYKIN-GDWRQYALFIAYGDKERCLSYDEK 79

                        90       100
                ....*....|....*....|..
gi 19114195 241 PLQLFRNLQKRGKSPSFVLSRR 262
Cdd:cd01786  80 PLLVFQRLKEQGKNPVFVLRRI 101
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
8-70 1.52e-14

SAM domain (Sterile alpha motif);


:

Pssm-ID: 429573  Cd Length: 66  Bit Score: 66.52  E-value: 1.52e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114195     8 YWNWNNEAVCNWIEQLGFPH-KEAFEDYHILG-KDIDLLSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQyTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
PRK03992 super family cl32052
proteasome-activating nucleotidase; Provisional
 81-125 4.86e-03

proteasome-activating nucleotidase; Provisional


The actual alignment was detected with superfamily member PRK03992:

Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 37.89  E-value: 4.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 19114195   81 ENKDQELKNIEESYKKLEEKTEHLSDDNVSLEKRVEYLETENTKL 125
Cdd:PRK03992   4 EALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKL 48
 
Name Accession Description Interval E-value
RA_STE50 cd01786
Ras-associating (RA) domain found in the fungal adaptor protein STE50; The fungal adaptor ...
 168-262 3.66e-29

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: 106.26  E-value: 3.66e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114195 168 VQPSPSVLGSFDLEV-------NDSLTNAEKNRKLNVNLTYNEVLCSMLQRYRIDpNTWMSYDLLINYDDKEHAIPMDVK 240
Cdd:cd01786   1 VSPTSSTIGSPELEPasprngiGPRPPEALKNRKVSVEDPCAKVLPAALKKYKIN-GDWRQYALFIAYGDKERCLSYDEK 79

                        90       100
                ....*....|....*....|..
gi 19114195 241 PLQLFRNLQKRGKSPSFVLSRR 262
Cdd:cd01786  80 PLLVFQRLKEQGKNPVFVLRRI 101
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
8-70 1.52e-14

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 66.52  E-value: 1.52e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114195     8 YWNWNNEAVCNWIEQLGFPH-KEAFEDYHILG-KDIDLLSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQyTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 177-263 3.24e-13

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: 63.86  E-value: 3.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114195    177 SFDLEVN--DSLTNAEKNRKLNVNLTYNEVLCSMLQRYRIDPNtWMSYDLLINY-DDKEHAIPMDVKPLQLFRNLQKRGK 253
Cdd:smart00314   2 TFVLRVYvdDLPGGTYKTLRVSSRTTARDVIQQLLEKFHLTDD-PEEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGP 80

                           90
                   ....*....|
gi 19114195    254 SPSFVLSRRS 263
Cdd:smart00314  81 NLRFVLRKRD 90
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 8-70 4.86e-13

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 62.70  E-value: 4.86e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114195      8 YWNWNNEAVCNWIEQLGFPH-KEAFEDYHILGKD-IDLLSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQyADNFRKNGIDGALlLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 176-264 5.13e-13

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: 63.12  E-value: 5.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114195   176 GSFDLEVNDSL---TNAEKNRKLNVNLTYNEVLCSMLQRYRIDpNTWMSYDL--LINYDDKEHAIPMDVKPLQLFRNLQK 250
Cdd:pfam00788   1 DDGVLKVYTEDgkpGTTYKTILVSSSTTAEEVIEALLEKFGLE-DDPRDYVLveVLERGGGERRLPDDECPLQIQLQWPR 79

                          90
                  ....*....|....
gi 19114195   251 RGKSPSFVLSRRSC 264
Cdd:pfam00788  80 DASDSRFLLRKRDD 93
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 16-68 5.05e-10

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 54.17  E-value: 5.05e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 19114195  16 VCNWIEQLGFP-HKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQ 68
Cdd:cd09487   2 VAEWLESLGLEqYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 81-125 4.86e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 37.89  E-value: 4.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 19114195   81 ENKDQELKNIEESYKKLEEKTEHLSDDNVSLEKRVEYLETENTKL 125
Cdd:PRK03992   4 EALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKL 48
iSH2_PIK3R2 cd12926
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
 81-143 7.72e-03

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.


Pssm-ID: 214019 [Multi-domain]  Cd Length: 161  Bit Score: 36.21  E-value: 7.72e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114195  81 ENKDQELKNIEESYKKLEEKTEHLSDDNVSLEKRVEYLETENTKLVKTLNSLNSEFLQlLRKI 143
Cdd:cd12926  76 EGNEKEMQRILLNSERLKSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKPDLMQ-LRKI 137
 
Name Accession Description Interval E-value
RA_STE50 cd01786
Ras-associating (RA) domain found in the fungal adaptor protein STE50; The fungal adaptor ...
 168-262 3.66e-29

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: 106.26  E-value: 3.66e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114195 168 VQPSPSVLGSFDLEV-------NDSLTNAEKNRKLNVNLTYNEVLCSMLQRYRIDpNTWMSYDLLINYDDKEHAIPMDVK 240
Cdd:cd01786   1 VSPTSSTIGSPELEPasprngiGPRPPEALKNRKVSVEDPCAKVLPAALKKYKIN-GDWRQYALFIAYGDKERCLSYDEK 79

                        90       100
                ....*....|....*....|..
gi 19114195 241 PLQLFRNLQKRGKSPSFVLSRR 262
Cdd:cd01786  80 PLLVFQRLKEQGKNPVFVLRRI 101
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
8-70 1.52e-14

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 66.52  E-value: 1.52e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114195     8 YWNWNNEAVCNWIEQLGFPH-KEAFEDYHILG-KDIDLLSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQyTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 177-263 3.24e-13

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: 63.86  E-value: 3.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114195    177 SFDLEVN--DSLTNAEKNRKLNVNLTYNEVLCSMLQRYRIDPNtWMSYDLLINY-DDKEHAIPMDVKPLQLFRNLQKRGK 253
Cdd:smart00314   2 TFVLRVYvdDLPGGTYKTLRVSSRTTARDVIQQLLEKFHLTDD-PEEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGP 80

                           90
                   ....*....|
gi 19114195    254 SPSFVLSRRS 263
Cdd:smart00314  81 NLRFVLRKRD 90
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 8-70 4.86e-13

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 62.70  E-value: 4.86e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114195      8 YWNWNNEAVCNWIEQLGFPH-KEAFEDYHILGKD-IDLLSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQyADNFRKNGIDGALlLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 176-264 5.13e-13

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: 63.12  E-value: 5.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114195   176 GSFDLEVNDSL---TNAEKNRKLNVNLTYNEVLCSMLQRYRIDpNTWMSYDL--LINYDDKEHAIPMDVKPLQLFRNLQK 250
Cdd:pfam00788   1 DDGVLKVYTEDgkpGTTYKTILVSSSTTAEEVIEALLEKFGLE-DDPRDYVLveVLERGGGERRLPDDECPLQIQLQWPR 79

                          90
                  ....*....|....
gi 19114195   251 RGKSPSFVLSRRSC 264
Cdd:pfam00788  80 DASDSRFLLRKRDD 93
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 10-70 8.02e-11

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 56.51  E-value: 8.02e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114195    10 NWNNEAVCNWIEQLGFP-HKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGqYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 16-68 5.05e-10

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 54.17  E-value: 5.05e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 19114195  16 VCNWIEQLGFP-HKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQ 68
Cdd:cd09487   2 VAEWLESLGLEqYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
SAM_MLTK cd09529
SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a ...
 11-68 1.21e-08

SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a protein-protein interaction domain. Besides SAM domain, these proteins have N-terminal protein tyrosine kinase domain and leucine-zipper motif. Proteins of this group act as mitogen-activated protein triple kinase in a number of MAPK cascades. They can be activated by autophosphorylation in response to stress signals. MLTK-alpha is known to phosphorylate histone H3. In mammals, MLTKs participate in the activation of the JNK/SAPK, p38, ERK5 pathways, the transcriptional factor NF-kB, in the regulation of the cell cycle checkpoint, and in the induction of apoptosis in a hepatoma cell line. Some members of this subfamily are proto-oncogenes, thus MLTK-alpha is involved in neoplasmic cell transformation and/or skin cancer development in athymic nude mice. Based on in vivo coprecipitation experiments in mammalian cells, it has been demonstrated that MLTK proteins might form homodimers/oligomers via their SAM domains.


Pssm-ID: 188928  Cd Length: 71  Bit Score: 50.58  E-value: 1.21e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114195  11 WNNEAVCNWIEQLGFP---------HKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQ 68
Cdd:cd09529   2 WTEEDVHFWMQQLVRKgghpselsqYADLFKENHITGKRLLLLTEEDLRDMGIGSKGHIIHLKSAIE 68
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 15-67 1.34e-08

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.


Pssm-ID: 188932  Cd Length: 58  Bit Score: 50.01  E-value: 1.34e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 19114195  15 AVCNWIEQLGFPHKE-AFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAI 67
Cdd:cd09533   1 DVADWLSSLGLPQYEdQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAV 54
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 10-68 7.73e-08

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.


Pssm-ID: 188904  Cd Length: 72  Bit Score: 48.47  E-value: 7.73e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114195  10 NWNNEAVCNWIEQLGFP-HKEAFEDYHILGKDIDLLSSNDL-RDMGIESVGHRIDILSAIQ 68
Cdd:cd09505   4 DWSEEDVCTWLRSIGLEqYVEVFRANNIDGKELLNLTKESLsKDLKIESLGHRNKILRKIE 64
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 10-70 1.59e-07

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 47.41  E-value: 1.59e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114195  10 NWNNEAVCNWIEQLGF-PHKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:cd09507   4 NWTTEEVGAWLESLQLgEYRDIFARNDIRGSELLHLERRDLKDLGITKVGHVKRILQAIKDL 65
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 11-70 2.92e-07

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 46.54  E-value: 2.92e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114195  11 WNNEAVCNWIEQLGF-PHKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:cd09506   5 WTVDDVGDWLESLNLgEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 10-68 8.25e-06

SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) subfamily is a putative protein-protein interaction domain. SAM is widespread domain in proteins involved in signal transduction and regulation. In many cases SAM mediates homodimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188929  Cd Length: 67  Bit Score: 42.69  E-value: 8.25e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114195  10 NWNNEAVCNWIEQLGFP-HKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQ 68
Cdd:cd09530   2 SWDTEDVAEWIEGLGFPqYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIR 61
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 11-70 1.67e-05

SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK-delta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. In particular DGK-delta is involved in the regulation of clathrin-dependent endocytosis. The SAM domain of DGK-delta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-eta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it inhibits the translocation of the protein to the plasma membrane from the cytoplasm. The SAM domain also can bind Zn at multiple (not conserved) sites driving the formation of highly ordered large sheets of polymers, thus suggesting that Zn may play important role in the function of DCK-delta.


Pssm-ID: 188974  Cd Length: 65  Bit Score: 41.86  E-value: 1.67e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114195  11 WNNEAVCNWIEQLGF-PHKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:cd09575   5 WGTEEVAAWLEHLSLcEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 11-70 3.20e-05

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188965  Cd Length: 63  Bit Score: 40.76  E-value: 3.20e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114195  11 WNNEAVCNWIEQLGFP-HKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:cd09566   2 LDTHWVLRWLDDIGLPqYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVL 62
SAM_DGK-eta cd09576
SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily ...
 11-70 1.21e-04

SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases. The SAM domain is located at the C-terminus of two out of three isoforms of DGK-eta protein. DGK-eta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DCK-eta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-delta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it is responsible for sustained endosomal localization of the protein and resulted in negative regulation of DCK-eta catalytic activity.


Pssm-ID: 188975  Cd Length: 65  Bit Score: 39.18  E-value: 1.21e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114195  11 WNNEAVCNWIEQLGF-PHKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:cd09576   5 WGTDEVAAWLDLLSLgEYKEIFIRHDIRGSELLHLERRDLKDLGIPKVGHMKRILQGIKEL 65
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 10-70 1.23e-04

SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation).


Pssm-ID: 188934  Cd Length: 65  Bit Score: 39.08  E-value: 1.23e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114195  10 NWNNEAVCNWIEQLGFP--HKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:cd09535   2 SWSPEQVAEWLLSAGFDdsVCEKFRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEIKSL 64
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 11-68 1.65e-04

SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK (connector enhancer of kinase suppressor of ras (Ksr)) subfamily is a protein-protein interaction domain. CNK proteins are multidomain scaffold proteins containing a few protein-protein interaction domains and are required for connecting Rho and Ras signaling pathways. In Drosophila, the SAM domain of CNK is known to interact with the SAM domain of the aveugle protein, forming a heterodimer. Mutation of the SAM domain in human CNK1 abolishes the ability to cooperate with the Ras effector, supporting the idea that this interaction is necessary for proper Ras signal transduction.


Pssm-ID: 188910  Cd Length: 69  Bit Score: 39.20  E-value: 1.65e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114195  11 WNNEAVCNWIEQLGF---PHKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQ 68
Cdd:cd09511   4 WSPKQVTDWLKGLDDclqQYIYTFEREKVTGEQLLNLSPQDLENLGVTKIGHQELILEAVE 64
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 11-69 2.21e-04

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 38.34  E-value: 2.21e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114195  11 WNNEAVCNWIEQLGF-PHKEAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQS 69
Cdd:cd09534   1 WDEEFVEEWLNELNCgQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKS 60
SAM_HD cd09508
SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily ...
 11-68 3.77e-04

SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily proteins is a putative protein-protein interaction domain. Proteins of this group, additionally to the SAM domain, contain a HD hydrolase domain. Human SAM-HD1 is a nuclear protein involved in innate immune response and may act as a negative regulator of the cell-intrinsic antiviral response. Mutations in this gene lead to Aicardi-Goutieres syndrome (symptoms include cerebral atrophy, leukoencephalopathy, hepatosplenomegaly, and increased production of alpha-interferon).


Pssm-ID: 188907  Cd Length: 70  Bit Score: 38.06  E-value: 3.77e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114195  11 WNNEAVCNWIEQLGFPHKE---AFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAIQ 68
Cdd:cd09508   5 WDPEDVCQFLRGNGFGEPElleIFRENEITGAHLPDLTESRLEKLGVSSLGERLKLLKCLQ 65
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 16-70 1.31e-03

SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188898  Cd Length: 67  Bit Score: 36.51  E-value: 1.31e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114195  16 VCNWIEQLGFPHKEA------FEDYHILGKDIdlLSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:cd09499   5 VGQWLESIGLPQYESklllngFDDVDFLGSGV--MEDQDLKEIGITDEQHRQIILQAARSL 63
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 44-70 2.65e-03

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 35.28  E-value: 2.65e-03
                        10        20
                ....*....|....*....|....*..
gi 19114195  44 LSSNDLRDMGIESVGHRIDILSAIQSM 70
Cdd:cd09488  35 MTAEDLTRLGVTLVGHQKKILNSIQAL 61
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 81-125 4.86e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 37.89  E-value: 4.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 19114195   81 ENKDQELKNIEESYKKLEEKTEHLSDDNVSLEKRVEYLETENTKL 125
Cdd:PRK03992   4 EALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKL 48
SAM_aveugle-like cd09510
SAM domain of aveugle-like subfamily; SAM (sterile alpha motif) domain of SAM_aveugle-like ...
 11-67 6.23e-03

SAM domain of aveugle-like subfamily; SAM (sterile alpha motif) domain of SAM_aveugle-like subfamily is a protein-protein interaction domain. In Drosophila, the aveugle (AVE) protein (also known as HYP (Hyphen)) is involved in normal photoreceptor differentiation, and required for epidermal growth factor receptor (EGFR) signaling between ras and raf genes during eye development and wing vein formation. SAM domain of the HYP(AVE) protein interacts with SAM domain of CNK, the multidomain scaffold protein connector enhancer of kinase suppressor of ras. CNK/HYP(AVE) complex interacts with KSR (kinase suppressor of Ras) protein. This interaction leads to stimulation of Ras-dependent Raf activation. This subfamily also includes vertebrate AVE homologs - Samd10 and Samd12 proteins. Their exact function is unknown, but they may play a role in signal transduction during embryogenesis.


Pssm-ID: 188909  Cd Length: 75  Bit Score: 34.59  E-value: 6.23e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114195  11 WNNEAVCNWIEQlGFPHK-----EAFEDYHILGKDIDLLSSNDLRDMGIESVGHRIDILSAI 67
Cdd:cd09510   6 WSVQDVCKWLKR-HCPDYyllyaELFLQHDITGRALLRLNDNKLERMGITDEDHRQDILREI 66
iSH2_PIK3R2 cd12926
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
 81-143 7.72e-03

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.


Pssm-ID: 214019 [Multi-domain]  Cd Length: 161  Bit Score: 36.21  E-value: 7.72e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114195  81 ENKDQELKNIEESYKKLEEKTEHLSDDNVSLEKRVEYLETENTKLVKTLNSLNSEFLQlLRKI 143
Cdd:cd12926  76 EGNEKEMQRILLNSERLKSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKPDLMQ-LRKI 137
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 92-141 9.68e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 36.73  E-value: 9.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 19114195   92 ESYKKLEEKTEHLSDDNVSLEKRVEYLETENTKLVKTLNSLNSEFLQLLR 141
Cdd:PRK03992   1 ERLEALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKLKS 50
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH