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Conserved domains on  [gi|12852405|dbj|BAB29401|]
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unnamed protein product [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_tumor-p73 cd09571
SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a ...
 136-200 2.00e-44

SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a putative protein-protein interaction and lipid-binding domain. p73 is a homolog to the tumor suppressor p53. p73 has a C-terminal SAM domain in the longest spliced alpha form, while p53 doesn't have it. p73 knockout mouse shows significant developmental abnormalities but no increased cancer susceptibility, suggesting that p73 plays a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for the p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain.


:

Pssm-ID: 188970  Cd Length: 65  Bit Score: 145.11  E-value: 2.00e-44
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12852405 136 YHADPSLVSFLTGLGCPNCIECFTSQGLQSIYHLQNLTIEDLGALKVPDQYRMTIWRGLQDLKQS 200
Cdd:cd09571   1 YNPDPSLVSFLTGLGCPNCIDYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMAIWRGLQELKQG 65
P53_tetramer pfam07710
P53 tetramerization motif;
2-31 7.32e-12

P53 tetramerization motif;


:

Pssm-ID: 462238  Cd Length: 42  Bit Score: 58.83  E-value: 7.32e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 12852405     2 FYMHVRGRENFEILMKVKESLELMELVPQP 31
Cdd:pfam07710  12 FTLPVRGRENYEMLKKIKESLELLDMVPQS 41
Gp37 super family cl09862
Gp37 protein; This protein of 154 residues consists of a unit of helices and beta sheets that ...
 195-282 8.51e-04

Gp37 protein; This protein of 154 residues consists of a unit of helices and beta sheets that crystallizes into a beautiful asymmetrical dodecameric barrel-structure, of two six-membered rings one on top of the other. It is expressed in bacteria but is of viral origin as it is found in phage BcepMu and is probably a pathogenesis factor.


The actual alignment was detected with superfamily member pfam09646:

Pssm-ID: 430731  Cd Length: 134  Bit Score: 38.85  E-value: 8.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12852405   195 QDLKQSHDCGQQLL--RSSSNAATISIGGSGELQRQRVMEAVHFRVRHtitipNRGGAGAVTGPDEWADFGFDLPDCKSR 272
Cdd:pfam09646  14 AEYRLNHPVGAVLVsyAGSRFGEPEDTDAVVQTRTLQLELTVLLRQLN-----GRLGALAVLDALRLALGGFRPPDCKRP 88

                          90
                  ....*....|
gi 12852405   273 KQPIKEEFTE 282
Cdd:pfam09646  89 LWLVSERFLG 98
 
Name Accession Description Interval E-value
SAM_tumor-p73 cd09571
SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a ...
 136-200 2.00e-44

SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a putative protein-protein interaction and lipid-binding domain. p73 is a homolog to the tumor suppressor p53. p73 has a C-terminal SAM domain in the longest spliced alpha form, while p53 doesn't have it. p73 knockout mouse shows significant developmental abnormalities but no increased cancer susceptibility, suggesting that p73 plays a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for the p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain.


Pssm-ID: 188970  Cd Length: 65  Bit Score: 145.11  E-value: 2.00e-44
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12852405 136 YHADPSLVSFLTGLGCPNCIECFTSQGLQSIYHLQNLTIEDLGALKVPDQYRMTIWRGLQDLKQS 200
Cdd:cd09571   1 YNPDPSLVSFLTGLGCPNCIDYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMAIWRGLQELKQG 65
P53_tetramer pfam07710
P53 tetramerization motif;
2-31 7.32e-12

P53 tetramerization motif;


Pssm-ID: 462238  Cd Length: 42  Bit Score: 58.83  E-value: 7.32e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 12852405     2 FYMHVRGRENFEILMKVKESLELMELVPQP 31
Cdd:pfam07710  12 FTLPVRGRENYEMLKKIKESLELLDMVPQS 41
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
134-198 2.20e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 58.43  E-value: 2.20e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12852405   134 PPYHADPSLVSFLTGLGCPNCIECFTSQGLQSIYHLQNLTIEDLGALKVPDQY-RMTIWRGLQDLK 198
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGhRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 140-200 2.05e-05

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: 41.51  E-value: 2.05e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12852405    140 PSLVSFLTGLGCPNCIECFTSQGLQSIYHLQNLTIEDLGALKV-PDQYRMTIWRGLQDLKQS 200
Cdd:smart00454   7 ESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
Gp37 pfam09646
Gp37 protein; This protein of 154 residues consists of a unit of helices and beta sheets that ...
 195-282 8.51e-04

Gp37 protein; This protein of 154 residues consists of a unit of helices and beta sheets that crystallizes into a beautiful asymmetrical dodecameric barrel-structure, of two six-membered rings one on top of the other. It is expressed in bacteria but is of viral origin as it is found in phage BcepMu and is probably a pathogenesis factor.


Pssm-ID: 430731  Cd Length: 134  Bit Score: 38.85  E-value: 8.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12852405   195 QDLKQSHDCGQQLL--RSSSNAATISIGGSGELQRQRVMEAVHFRVRHtitipNRGGAGAVTGPDEWADFGFDLPDCKSR 272
Cdd:pfam09646  14 AEYRLNHPVGAVLVsyAGSRFGEPEDTDAVVQTRTLQLELTVLLRQLN-----GRLGALAVLDALRLALGGFRPPDCKRP 88

                          90
                  ....*....|
gi 12852405   273 KQPIKEEFTE 282
Cdd:pfam09646  89 LWLVSERFLG 98
 
Name Accession Description Interval E-value
SAM_tumor-p73 cd09571
SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a ...
 136-200 2.00e-44

SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a putative protein-protein interaction and lipid-binding domain. p73 is a homolog to the tumor suppressor p53. p73 has a C-terminal SAM domain in the longest spliced alpha form, while p53 doesn't have it. p73 knockout mouse shows significant developmental abnormalities but no increased cancer susceptibility, suggesting that p73 plays a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for the p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain.


Pssm-ID: 188970  Cd Length: 65  Bit Score: 145.11  E-value: 2.00e-44
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12852405 136 YHADPSLVSFLTGLGCPNCIECFTSQGLQSIYHLQNLTIEDLGALKVPDQYRMTIWRGLQDLKQS 200
Cdd:cd09571   1 YNPDPSLVSFLTGLGCPNCIDYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMAIWRGLQELKQG 65
SAM_tumor-p63,p73 cd09503
SAM domain of tumor-p63,p73 proteins; SAM (sterile alpha motif) domain of p63, p73 ...
 136-199 7.79e-31

SAM domain of tumor-p63,p73 proteins; SAM (sterile alpha motif) domain of p63, p73 transcriptional factors is a putative protein-protein interaction domain and lipid-binding domain. p63 and p73 are homologs to the tumor suppressor p53. They have a C-terminal SAM domain in their longest spliced alpha forms, while p53 doesn't have it. p63 or p73 knockout mice show significant developmental abnormalities but no increased cancer susceptibility, suggesting that p63 and p73 play a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for p63/p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain.


Pssm-ID: 188902  Cd Length: 65  Bit Score: 109.71  E-value: 7.79e-31
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12852405 136 YHADPSLVSFLTGLGCPNCIECFTSQGLQSIYHLQNLTIEDLGALKVPDQYRMTIWRGLQDLKQ 199
Cdd:cd09503   1 YPTDNSVASWLTKLGCSNYIDNFHQQGLLSIFQLDEFTLEDLAAMKIPEQHRNKIWKGLLEYRQ 64
SAM_tumor-p63 cd09572
SAM domain of tumor-p63 proteins; SAM (sterile alpha motif) domain of p63 proteins is a ...
 136-199 3.21e-19

SAM domain of tumor-p63 proteins; SAM (sterile alpha motif) domain of p63 proteins is a putative protein-protein interaction domain. p63 is homolog to the tumor suppressor p53. p63 has a C-terminal SAM domain in the longest spliced alpha form, while p53 doesn't have it. p63 knockout mice show significant developmental abnormalities but no increased cancer susceptibility, suggesting that p63 plays a role in regulation of normal development. No evidence for homooligomerization through SAM domains was found for the p63 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain. Mutations in the SAM domain of p63 are found in AEC syndrome patients.


Pssm-ID: 188971  Cd Length: 65  Bit Score: 79.63  E-value: 3.21e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12852405 136 YHADPSLVSFLTGLGCPNCIECFTSQGLQSIYHLQNLTIEDLGALKVPDQYRMTIWRGLQDLKQ 199
Cdd:cd09572   1 YPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLSSLKIPEQFRHAIWKGILDHRQ 64
P53_tetramer pfam07710
P53 tetramerization motif;
2-31 7.32e-12

P53 tetramerization motif;


Pssm-ID: 462238  Cd Length: 42  Bit Score: 58.83  E-value: 7.32e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 12852405     2 FYMHVRGRENFEILMKVKESLELMELVPQP 31
Cdd:pfam07710  12 FTLPVRGRENYEMLKKIKESLELLDMVPQS 41
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
134-198 2.20e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 58.43  E-value: 2.20e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12852405   134 PPYHADPSLVSFLTGLGCPNCIECFTSQGLQSIYHLQNLTIEDLGALKVPDQY-RMTIWRGLQDLK 198
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGhRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 140-200 2.05e-05

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: 41.51  E-value: 2.05e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12852405    140 PSLVSFLTGLGCPNCIECFTSQGLQSIYHLQNLTIEDLGALKV-PDQYRMTIWRGLQDLKQS 200
Cdd:smart00454   7 ESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 141-196 1.28e-04

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: 39.14  E-value: 1.28e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 12852405 141 SLVSFLTGLGCPNCIECFTSQGLqSIYHLQNLTIEDLGALKVPD-QYRMTIWRGLQD 196
Cdd:cd09487   1 DVAEWLESLGLEQYADLFRKNEI-DGDALLLLTDEDLKELGITSpGHRKKILRAIQR 56
Gp37 pfam09646
Gp37 protein; This protein of 154 residues consists of a unit of helices and beta sheets that ...
 195-282 8.51e-04

Gp37 protein; This protein of 154 residues consists of a unit of helices and beta sheets that crystallizes into a beautiful asymmetrical dodecameric barrel-structure, of two six-membered rings one on top of the other. It is expressed in bacteria but is of viral origin as it is found in phage BcepMu and is probably a pathogenesis factor.


Pssm-ID: 430731  Cd Length: 134  Bit Score: 38.85  E-value: 8.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12852405   195 QDLKQSHDCGQQLL--RSSSNAATISIGGSGELQRQRVMEAVHFRVRHtitipNRGGAGAVTGPDEWADFGFDLPDCKSR 272
Cdd:pfam09646  14 AEYRLNHPVGAVLVsyAGSRFGEPEDTDAVVQTRTLQLELTVLLRQLN-----GRLGALAVLDALRLALGGFRPPDCKRP 88

                          90
                  ....*....|
gi 12852405   273 KQPIKEEFTE 282
Cdd:pfam09646  89 LWLVSERFLG 98
 
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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