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Conserved domains on  [gi|568918021|ref|XP_006500061|]
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mitogen-activated protein kinase kinase kinase 20 isoform X2 [Mus musculus]

Protein Classification

SAM_MLTK domain-containing protein( domain architecture ID 10175787)

SAM_MLTK domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SAM_MLTK cd09529
SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a ...
22-92 2.08e-29

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: 109.90  E-value: 2.08e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568918021  22 AWTEDDVYFWVQQLVRKGESSVEMSGYASLFKENNITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEKLT 92
Cdd:cd09529    1 AWTEEDVHFWMQQLVRKGGHPSELSQYADLFKENHITGKRLLLLTEEDLRDMGIGSKGHIIHLKSAIEKLT 71
PTZ00112 super family cl36513
origin recognition complex 1 protein; Provisional
292-411 8.78e-03

origin recognition complex 1 protein; Provisional


The actual alignment was detected with superfamily member PTZ00112:

Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 38.82  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918021  292 QDSYAAAVRRTQTPVKYQQ--ITP---------SINPSRSSSPTQYGLSRNFSSlnlsSRDSGFSSLNDSSSERGRYSDR 360
Cdd:PTZ00112   88 HDFYIDLNERSKTPIKNNDnvTTPikankkekhNLDSSSSSSISSSLTNISFFS----SPTSIYSCLSNSLSSKHSPKVI 163
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568918021  361 SRNKYYRGSVSLNSSPKGRYGGKSQHSTPSRERYSGKFYRLPQSALNTHQS 411
Cdd:PTZ00112  164 KENQSTHVNISSDNSPRNKEISNKQLKKQTNVTHTTCYDKMRRSPRNTSTI 214
 
Name Accession Description Interval E-value
SAM_MLTK cd09529
SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a ...
22-92 2.08e-29

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: 109.90  E-value: 2.08e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568918021  22 AWTEDDVYFWVQQLVRKGESSVEMSGYASLFKENNITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEKLT 92
Cdd:cd09529    1 AWTEEDVHFWMQQLVRKGGHPSELSQYADLFKENHITGKRLLLLTEEDLRDMGIGSKGHIIHLKSAIEKLT 71
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
23-91 1.60e-03

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: 36.89  E-value: 1.60e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918021    23 WTEDDVYFWVQQLVrkgessveMSGYASLFKENNITGKRLLLLEEEDL-KDMGIVSKGHIIHFKSAIEKL 91
Cdd:smart00454   4 WSPESVADWLESIG--------LEQYADNFRKNGIDGALLLLLTSEEDlKELGITKLGHRKKILKAIQKL 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
23-91 4.25e-03

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: 35.71  E-value: 4.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568918021   23 WTEDDVYFWVQQLvrkgessvEMSGYASLFKENNITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEKL 91
Cdd:pfam00536   3 WSVEDVGEWLESI--------GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
292-411 8.78e-03

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 38.82  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918021  292 QDSYAAAVRRTQTPVKYQQ--ITP---------SINPSRSSSPTQYGLSRNFSSlnlsSRDSGFSSLNDSSSERGRYSDR 360
Cdd:PTZ00112   88 HDFYIDLNERSKTPIKNNDnvTTPikankkekhNLDSSSSSSISSSLTNISFFS----SPTSIYSCLSNSLSSKHSPKVI 163
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568918021  361 SRNKYYRGSVSLNSSPKGRYGGKSQHSTPSRERYSGKFYRLPQSALNTHQS 411
Cdd:PTZ00112  164 KENQSTHVNISSDNSPRNKEISNKQLKKQTNVTHTTCYDKMRRSPRNTSTI 214
 
Name Accession Description Interval E-value
SAM_MLTK cd09529
SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a ...
22-92 2.08e-29

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: 109.90  E-value: 2.08e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568918021  22 AWTEDDVYFWVQQLVRKGESSVEMSGYASLFKENNITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEKLT 92
Cdd:cd09529    1 AWTEEDVHFWMQQLVRKGGHPSELSQYADLFKENHITGKRLLLLTEEDLRDMGIGSKGHIIHLKSAIEKLT 71
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
23-91 5.06e-05

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: 41.24  E-value: 5.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568918021  23 WTEDDVYFWVqqlvrkgeSSVEMSGYASLFKENNITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEKL 91
Cdd:cd09507    5 WTTEEVGAWL--------ESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITKVGHVKRILQAIKDL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
23-91 1.60e-03

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: 36.89  E-value: 1.60e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918021    23 WTEDDVYFWVQQLVrkgessveMSGYASLFKENNITGKRLLLLEEEDL-KDMGIVSKGHIIHFKSAIEKL 91
Cdd:smart00454   4 WSPESVADWLESIG--------LEQYADNFRKNGIDGALLLLLTSEEDlKELGITKLGHRKKILKAIQKL 65
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
23-60 3.52e-03

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.


Pssm-ID: 188903  Cd Length: 74  Bit Score: 36.16  E-value: 3.52e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568918021  23 WTEDDVYFWVqqlvrkgESSVEMSGYASLFKENNITGK 60
Cdd:cd09504    5 WTVEDTVEWL-------VNSVELPQYVEAFKENGVDGS 35
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
27-90 3.98e-03

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: 35.68  E-value: 3.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568918021  27 DVYFWVQQLvrkgessvEMSGYASLFKENNITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEK 90
Cdd:cd09487    1 DVAEWLESL--------GLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
23-91 4.25e-03

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: 35.71  E-value: 4.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568918021   23 WTEDDVYFWVQQLvrkgessvEMSGYASLFKENNITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEKL 91
Cdd:pfam00536   3 WSVEDVGEWLESI--------GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
20-80 7.10e-03

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: 35.37  E-value: 7.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918021  20 IGAWTEDDVYFWVQqlvrkgesSVEMSGYASLFKENNITGKR-LLLLEEEDLKDMGIVSKGH 80
Cdd:cd09505    2 LQDWSEEDVCTWLR--------SIGLEQYVEVFRANNIDGKElLNLTKESLSKDLKIESLGH 55
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
292-411 8.78e-03

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 38.82  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918021  292 QDSYAAAVRRTQTPVKYQQ--ITP---------SINPSRSSSPTQYGLSRNFSSlnlsSRDSGFSSLNDSSSERGRYSDR 360
Cdd:PTZ00112   88 HDFYIDLNERSKTPIKNNDnvTTPikankkekhNLDSSSSSSISSSLTNISFFS----SPTSIYSCLSNSLSSKHSPKVI 163
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568918021  361 SRNKYYRGSVSLNSSPKGRYGGKSQHSTPSRERYSGKFYRLPQSALNTHQS 411
Cdd:PTZ00112  164 KENQSTHVNISSDNSPRNKEISNKQLKKQTNVTHTTCYDKMRRSPRNTSTI 214
 
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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