PB1-p53-T2A-Mmj-MDM2 [synthetic construct]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| GFP | pfam01353 | Green fluorescent protein; |
240-430 | 3.38e-52 | ||||
Green fluorescent protein; : Pssm-ID: 426217 Cd Length: 211 Bit Score: 178.53 E-value: 3.38e-52
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| MDM2 | cd17672 | p53-binding domain found in E3 ubiquitin-protein ligase MDM2 and similar proteins; MDM2, also ... |
523-605 | 8.67e-41 | ||||
p53-binding domain found in E3 ubiquitin-protein ligase MDM2 and similar proteins; MDM2, also known as double minute 2 protein (Hdm2), or oncoprotein MDM2, or p53-binding protein, exerts its oncogenic activity predominantly by binding the p53 tumor suppressor and blocking its transcriptional activity. It forms homo-oligomers and displays E3 ubiquitin ligase activity, catalyzing the attachment of ubiquitin to p53 as an essential step in the regulation of its expression levels in cells. Moreover, in response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through the interaction with ribosomal proteins L5, L11, and L23. MDM2 also has a p53-independent role in tumorigenesis and cell growth regulation. In addition, it binds interferon (IFN) regulatory factor-2 (IRF-2), an IFN-regulated transcription factor, and mediates its ubiquitination. MDM2 contains an N-terminal p53-binding domain and a C-terminal zinc RING-finger domain conferring E3 ligase activity that is required for ubiquitination and nuclear export of p53. It is also responsible for the hetero-oligomerization of MDM2, which is crucial for the suppression of P53 activity during embryonic development, and the recruitment of E2 ubiquitin-conjugating enzymes. MDM2 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain, as well as a nuclear localization signal (NLS) and a nuclear export signal (NES), near the central acidic region. : Pssm-ID: 349491 Cd Length: 83 Bit Score: 143.04 E-value: 8.67e-41
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| PB1_p62 | cd06402 | The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ... |
4-102 | 6.19e-39 | ||||
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) involved in cell signaling, receptor internalization, and protein turnover. The PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. : Pssm-ID: 99723 Cd Length: 87 Bit Score: 137.85 E-value: 6.19e-39
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| TAD2 | pfam18521 | Transactivation domain 2; This is a N-terminal transactivation domain (TAD) domain 2 found in ... |
175-199 | 1.06e-12 | ||||
Transactivation domain 2; This is a N-terminal transactivation domain (TAD) domain 2 found in p53 proteins. In p53 two TAD domains are found termed TAD1 (residues 1-39) and TAD2 (residues 40-61), both of which have been shown to be able to independently activate gene transcription and are intrinsically disordered protein domains that adopt a helical conformation for at least part of their length when bound. This inherent flexibility allows the TADs to adapt to and bind a broad range of proteins. This entry describes TAD2 which can independently interact with Taz2 domain of the histone acetyltransferase p300. It has also been shown to bind to OB-fold domain of replication protein 70 A (RPA) as well as the pleckstrin homology (PH) domain of the p62 and Tfb1 subunits of human and yeast TFIIH. : Pssm-ID: 375947 Cd Length: 25 Bit Score: 62.08 E-value: 1.06e-12
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| P53_TAD | pfam08563 | P53 transactivation motif; The binding of the p53 transactivation domain by regulatory ... |
146-170 | 1.37e-09 | ||||
P53 transactivation motif; The binding of the p53 transactivation domain by regulatory proteins regulates p53 transcription activation. This motif is comprised of a single amphipathic alpha helix and contains a highly conserved sequence. : Pssm-ID: 462520 Cd Length: 25 Bit Score: 53.33 E-value: 1.37e-09
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| Name | Accession | Description | Interval | E-value | ||||
| GFP | pfam01353 | Green fluorescent protein; |
240-430 | 3.38e-52 | ||||
Green fluorescent protein; Pssm-ID: 426217 Cd Length: 211 Bit Score: 178.53 E-value: 3.38e-52
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| MDM2 | cd17672 | p53-binding domain found in E3 ubiquitin-protein ligase MDM2 and similar proteins; MDM2, also ... |
523-605 | 8.67e-41 | ||||
p53-binding domain found in E3 ubiquitin-protein ligase MDM2 and similar proteins; MDM2, also known as double minute 2 protein (Hdm2), or oncoprotein MDM2, or p53-binding protein, exerts its oncogenic activity predominantly by binding the p53 tumor suppressor and blocking its transcriptional activity. It forms homo-oligomers and displays E3 ubiquitin ligase activity, catalyzing the attachment of ubiquitin to p53 as an essential step in the regulation of its expression levels in cells. Moreover, in response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through the interaction with ribosomal proteins L5, L11, and L23. MDM2 also has a p53-independent role in tumorigenesis and cell growth regulation. In addition, it binds interferon (IFN) regulatory factor-2 (IRF-2), an IFN-regulated transcription factor, and mediates its ubiquitination. MDM2 contains an N-terminal p53-binding domain and a C-terminal zinc RING-finger domain conferring E3 ligase activity that is required for ubiquitination and nuclear export of p53. It is also responsible for the hetero-oligomerization of MDM2, which is crucial for the suppression of P53 activity during embryonic development, and the recruitment of E2 ubiquitin-conjugating enzymes. MDM2 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain, as well as a nuclear localization signal (NLS) and a nuclear export signal (NES), near the central acidic region. Pssm-ID: 349491 Cd Length: 83 Bit Score: 143.04 E-value: 8.67e-41
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| PB1_p62 | cd06402 | The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ... |
4-102 | 6.19e-39 | ||||
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) involved in cell signaling, receptor internalization, and protein turnover. The PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. Pssm-ID: 99723 Cd Length: 87 Bit Score: 137.85 E-value: 6.19e-39
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| TAD2 | pfam18521 | Transactivation domain 2; This is a N-terminal transactivation domain (TAD) domain 2 found in ... |
175-199 | 1.06e-12 | ||||
Transactivation domain 2; This is a N-terminal transactivation domain (TAD) domain 2 found in p53 proteins. In p53 two TAD domains are found termed TAD1 (residues 1-39) and TAD2 (residues 40-61), both of which have been shown to be able to independently activate gene transcription and are intrinsically disordered protein domains that adopt a helical conformation for at least part of their length when bound. This inherent flexibility allows the TADs to adapt to and bind a broad range of proteins. This entry describes TAD2 which can independently interact with Taz2 domain of the histone acetyltransferase p300. It has also been shown to bind to OB-fold domain of replication protein 70 A (RPA) as well as the pleckstrin homology (PH) domain of the p62 and Tfb1 subunits of human and yeast TFIIH. Pssm-ID: 375947 Cd Length: 25 Bit Score: 62.08 E-value: 1.06e-12
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| PB1 | smart00666 | PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ... |
3-99 | 6.71e-12 | ||||
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate. Pssm-ID: 214770 Cd Length: 81 Bit Score: 61.45 E-value: 6.71e-12
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| PB1 | pfam00564 | PB1 domain; |
44-102 | 3.45e-10 | ||||
PB1 domain; Pssm-ID: 395447 Cd Length: 84 Bit Score: 56.53 E-value: 3.45e-10
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| P53_TAD | pfam08563 | P53 transactivation motif; The binding of the p53 transactivation domain by regulatory ... |
146-170 | 1.37e-09 | ||||
P53 transactivation motif; The binding of the p53 transactivation domain by regulatory proteins regulates p53 transcription activation. This motif is comprised of a single amphipathic alpha helix and contains a highly conserved sequence. Pssm-ID: 462520 Cd Length: 25 Bit Score: 53.33 E-value: 1.37e-09
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| SWIB | pfam02201 | SWIB/MDM2 domain; This family includes the SWIB domain and the MDM2 domain. The p53-associated ... |
543-590 | 5.30e-06 | ||||
SWIB/MDM2 domain; This family includes the SWIB domain and the MDM2 domain. The p53-associated protein (MDM2) is an inhibitor of the p53 tumour suppressor gene binding the transactivation domain and down regulating the ability of p53 to activate transcription. This family contains the p53 binding domain of MDM2. Pssm-ID: 460488 [Multi-domain] Cd Length: 73 Bit Score: 44.40 E-value: 5.30e-06
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| Name | Accession | Description | Interval | E-value | ||||
| GFP | pfam01353 | Green fluorescent protein; |
240-430 | 3.38e-52 | ||||
Green fluorescent protein; Pssm-ID: 426217 Cd Length: 211 Bit Score: 178.53 E-value: 3.38e-52
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| MDM2 | cd17672 | p53-binding domain found in E3 ubiquitin-protein ligase MDM2 and similar proteins; MDM2, also ... |
523-605 | 8.67e-41 | ||||
p53-binding domain found in E3 ubiquitin-protein ligase MDM2 and similar proteins; MDM2, also known as double minute 2 protein (Hdm2), or oncoprotein MDM2, or p53-binding protein, exerts its oncogenic activity predominantly by binding the p53 tumor suppressor and blocking its transcriptional activity. It forms homo-oligomers and displays E3 ubiquitin ligase activity, catalyzing the attachment of ubiquitin to p53 as an essential step in the regulation of its expression levels in cells. Moreover, in response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through the interaction with ribosomal proteins L5, L11, and L23. MDM2 also has a p53-independent role in tumorigenesis and cell growth regulation. In addition, it binds interferon (IFN) regulatory factor-2 (IRF-2), an IFN-regulated transcription factor, and mediates its ubiquitination. MDM2 contains an N-terminal p53-binding domain and a C-terminal zinc RING-finger domain conferring E3 ligase activity that is required for ubiquitination and nuclear export of p53. It is also responsible for the hetero-oligomerization of MDM2, which is crucial for the suppression of P53 activity during embryonic development, and the recruitment of E2 ubiquitin-conjugating enzymes. MDM2 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain, as well as a nuclear localization signal (NLS) and a nuclear export signal (NES), near the central acidic region. Pssm-ID: 349491 Cd Length: 83 Bit Score: 143.04 E-value: 8.67e-41
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| PB1_p62 | cd06402 | The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ... |
4-102 | 6.19e-39 | ||||
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) involved in cell signaling, receptor internalization, and protein turnover. The PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. Pssm-ID: 99723 Cd Length: 87 Bit Score: 137.85 E-value: 6.19e-39
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| MDM2_like | cd10566 | p53-binding domain found in E3 ubiquitin-protein ligase MDM2, MDM4, and similar proteins; MDM2 ... |
538-605 | 3.37e-29 | ||||
p53-binding domain found in E3 ubiquitin-protein ligase MDM2, MDM4, and similar proteins; MDM2 (also termed HDM2) and MDM4 (also termed MDMX or HDMX) are the primary negative regulators of p53 tumor suppressor. They have non-redundant roles in the regulation of p53. MDM2 mainly functions to control p53 stability, while MDM4 controls p53 transcriptional activity. Both MDM2 and MDM4 contain an N-terminal p53-binding domain, a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region, and a C-terminal RING domain. Mdm2 can form homo-oligomers through its RING domain and display E3 ubiquitin ligase activity that catalyzes the attachment of ubiquitin to p53 as an essential step in the regulation of its level in cells. Despite its RING domain and structural similarity with MDM2, MDM4 does not homo-oligomerize and lacks ubiquitin-ligase function, but inhibits the transcriptional activity of p53. In addition, both their RING domains are responsible for the hetero-oligomerization, which is crucial for the suppression of p53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. Moreover, MDM2 and MDM4 can be phosphorylated and destabilized in response to DNA damage stress. In response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through the interaction with ribosomal proteins L5, L11 and L23. However, MDM4 is not bound to ribosomal proteins, suggesting its different response to regulation by small basic proteins such as ribosomal proteins and ARF. Pssm-ID: 349488 Cd Length: 75 Bit Score: 110.34 E-value: 3.37e-29
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| MDM4 | cd17673 | p53-binding domain found in MDM4 and similar proteins; MDM4, also known as double minute 4 ... |
538-606 | 5.41e-29 | ||||
p53-binding domain found in MDM4 and similar proteins; MDM4, also known as double minute 4 protein, MDM2-like p53-binding protein, protein MDMX, HDMX, or p53-binding protein MDM4, exerts its oncogenic activity predominantly by binding the p53 tumor suppressor and blocking its transcriptional activity. MDM4 is phosphorylated and destabilized in response to DNA damage stress. It can also be specifically dephosphorylated through directly interacting with protein phosphatase 1 (PP1), which may increase its stability and thus inhibit p53 activity. MDM4 also has a p53-independent role in tumorigenesis and cell growth regulation. MDM4 contains an N-terminal p53-binding domain and a C-terminal zinc RING-finger domain responsible for its hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. MDM4 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region. Pssm-ID: 349492 Cd Length: 79 Bit Score: 109.92 E-value: 5.41e-29
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| SWIB-MDM2 | cd00855 | SWIB/MDM2 domain family; The SWIB/MDM2 protein domain, short for SWI/SNF complex B/MDM2, has ... |
544-604 | 2.69e-16 | ||||
SWIB/MDM2 domain family; The SWIB/MDM2 protein domain, short for SWI/SNF complex B/MDM2, has been found in both SWI/SNF complex B (SWIB) and the negative regulator of the p53 tumor suppressor MDM2, which are homologous and share a common fold. The SWIB domain is a conserved region found within proteins in the SWI/SNF (SWItch/Sucrose Non-Fermentable) family of complexes. SWI/SNF complex proteins display helicase and ATPase activities and are thought to regulate transcription of certain genes by altering the chromatin structure around those genes. The mammalian complexes are made up of 9-12 proteins called BAFs (BRG1-associated factors). MDM2 is an inhibitor of p53 tumor repressor. It binds to the transactivation domain and down-regulates the ability of p53 to activate transcription. This family corresponds to the SWIB domain and the p53 binding domain of MDM2. Pssm-ID: 349487 [Multi-domain] Cd Length: 69 Bit Score: 73.41 E-value: 2.69e-16
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| TAD2 | pfam18521 | Transactivation domain 2; This is a N-terminal transactivation domain (TAD) domain 2 found in ... |
175-199 | 1.06e-12 | ||||
Transactivation domain 2; This is a N-terminal transactivation domain (TAD) domain 2 found in p53 proteins. In p53 two TAD domains are found termed TAD1 (residues 1-39) and TAD2 (residues 40-61), both of which have been shown to be able to independently activate gene transcription and are intrinsically disordered protein domains that adopt a helical conformation for at least part of their length when bound. This inherent flexibility allows the TADs to adapt to and bind a broad range of proteins. This entry describes TAD2 which can independently interact with Taz2 domain of the histone acetyltransferase p300. It has also been shown to bind to OB-fold domain of replication protein 70 A (RPA) as well as the pleckstrin homology (PH) domain of the p62 and Tfb1 subunits of human and yeast TFIIH. Pssm-ID: 375947 Cd Length: 25 Bit Score: 62.08 E-value: 1.06e-12
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| PB1 | smart00666 | PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ... |
3-99 | 6.71e-12 | ||||
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate. Pssm-ID: 214770 Cd Length: 81 Bit Score: 61.45 E-value: 6.71e-12
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| PB1 | cd05992 | The PB1 domain is a modular domain mediating specific protein-protein interactions which play ... |
4-100 | 3.06e-11 | ||||
The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. Pssm-ID: 99716 [Multi-domain] Cd Length: 81 Bit Score: 59.60 E-value: 3.06e-11
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| PB1 | pfam00564 | PB1 domain; |
44-102 | 3.45e-10 | ||||
PB1 domain; Pssm-ID: 395447 Cd Length: 84 Bit Score: 56.53 E-value: 3.45e-10
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| P53_TAD | pfam08563 | P53 transactivation motif; The binding of the p53 transactivation domain by regulatory ... |
146-170 | 1.37e-09 | ||||
P53 transactivation motif; The binding of the p53 transactivation domain by regulatory proteins regulates p53 transcription activation. This motif is comprised of a single amphipathic alpha helix and contains a highly conserved sequence. Pssm-ID: 462520 Cd Length: 25 Bit Score: 53.33 E-value: 1.37e-09
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| SWIB | pfam02201 | SWIB/MDM2 domain; This family includes the SWIB domain and the MDM2 domain. The p53-associated ... |
543-590 | 5.30e-06 | ||||
SWIB/MDM2 domain; This family includes the SWIB domain and the MDM2 domain. The p53-associated protein (MDM2) is an inhibitor of the p53 tumour suppressor gene binding the transactivation domain and down regulating the ability of p53 to activate transcription. This family contains the p53 binding domain of MDM2. Pssm-ID: 460488 [Multi-domain] Cd Length: 73 Bit Score: 44.40 E-value: 5.30e-06
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| SWIB_like | cd10568 | SWIB domain found in the 60 kda subunit of the ATP-dependent SWI/SNF chromatin-remodeling ... |
547-593 | 3.94e-04 | ||||
SWIB domain found in the 60 kda subunit of the ATP-dependent SWI/SNF chromatin-remodeling complexes and similar proteins; SWIB domain is a conserved region found within proteins in the SWI/SNF family of complexes. SWI/SNF complex proteins display helicase and ATPase activities and are thought to regulate transcription of certain genes by altering the chromatin structure around those genes. The mammalian complexes are made up of 9-12 proteins called BAFs (BRG1-associated factors), among which the BAF60 subunit serves as a key link between the core complexes and specific transcriptional factors. The BAF60 subunit have at least three members: BAF60a, which is ubiquitous, BAF60b and BAF60c, which are expressed in muscle and pancreatic tissues, respectively. The family also includes Saccharomyces cerevisiae transcription regulatory protein SNF12 and remodel the structure of chromatin complex subunit 6 (RSC6), and Schizosaccharomyces pombe SWI/SNF and RSC complexes subunit SSR3. SNF12, also termed 73-kDa subunit of the SWI/SNF transcriptional regulatory complex, or SWI/SNF complex component SWP73, is involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). RSC6 and SSR3 are components of the RSC, which is involved in transcription regulation and nucleosome positioning. RSC6 is essential for mitotic growth and suppresses formamide sensitivity of the RSC8 mutants. Pssm-ID: 349490 [Multi-domain] Cd Length: 69 Bit Score: 39.05 E-value: 3.94e-04
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| PB1_Joka2 | cd06398 | The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with ... |
47-89 | 1.15e-03 | ||||
The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with sulfur stress inducible UP9 protein. The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. Pssm-ID: 99720 Cd Length: 91 Bit Score: 38.54 E-value: 1.15e-03
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