PREDICTED: zinc finger CCCH domain-containing protein 48 [Camelina sativa]
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
WD40 | COG2319 | WD40 repeat [General function prediction only]; |
138-429 | 2.99e-32 | |||||
WD40 repeat [General function prediction only]; : Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 126.56 E-value: 2.99e-32
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zf_CCCH_4 | pfam18345 | Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ... |
114-132 | 3.53e-06 | |||||
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process. : Pssm-ID: 465719 [Multi-domain] Cd Length: 19 Bit Score: 43.17 E-value: 3.53e-06
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Name | Accession | Description | Interval | E-value | |||||
WD40 | COG2319 | WD40 repeat [General function prediction only]; |
138-429 | 2.99e-32 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 126.56 E-value: 2.99e-32
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
142-426 | 3.75e-32 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 123.60 E-value: 3.75e-32
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PTZ00421 | PTZ00421 | coronin; Provisional |
242-337 | 2.44e-07 | |||||
coronin; Provisional Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 52.97 E-value: 2.44e-07
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zf_CCCH_4 | pfam18345 | Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ... |
114-132 | 3.53e-06 | |||||
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process. Pssm-ID: 465719 [Multi-domain] Cd Length: 19 Bit Score: 43.17 E-value: 3.53e-06
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ZnF_C3H1 | smart00356 | zinc finger; |
111-133 | 8.37e-06 | |||||
zinc finger; Pssm-ID: 214632 [Multi-domain] Cd Length: 27 Bit Score: 42.23 E-value: 8.37e-06
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
139-178 | 6.11e-05 | |||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 39.99 E-value: 6.11e-05
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WD40 | pfam00400 | WD domain, G-beta repeat; |
140-178 | 6.27e-05 | |||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 40.02 E-value: 6.27e-05
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Name | Accession | Description | Interval | E-value | |||||
WD40 | COG2319 | WD40 repeat [General function prediction only]; |
138-429 | 2.99e-32 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 126.56 E-value: 2.99e-32
|
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
142-426 | 3.75e-32 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 123.60 E-value: 3.75e-32
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
142-429 | 7.04e-30 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 120.02 E-value: 7.04e-30
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
138-338 | 1.04e-27 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 113.85 E-value: 1.04e-27
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
141-338 | 9.95e-25 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 103.18 E-value: 9.95e-25
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
138-339 | 7.84e-23 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 97.79 E-value: 7.84e-23
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
137-299 | 4.50e-14 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 72.37 E-value: 4.50e-14
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
214-433 | 4.76e-13 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 70.33 E-value: 4.76e-13
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PTZ00421 | PTZ00421 | coronin; Provisional |
242-337 | 2.44e-07 | |||||
coronin; Provisional Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 52.97 E-value: 2.44e-07
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zf_CCCH_4 | pfam18345 | Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ... |
114-132 | 3.53e-06 | |||||
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process. Pssm-ID: 465719 [Multi-domain] Cd Length: 19 Bit Score: 43.17 E-value: 3.53e-06
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ZnF_C3H1 | smart00356 | zinc finger; |
111-133 | 8.37e-06 | |||||
zinc finger; Pssm-ID: 214632 [Multi-domain] Cd Length: 27 Bit Score: 42.23 E-value: 8.37e-06
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
139-178 | 6.11e-05 | |||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 39.99 E-value: 6.11e-05
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WD40 | pfam00400 | WD domain, G-beta repeat; |
140-178 | 6.27e-05 | |||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 40.02 E-value: 6.27e-05
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
302-338 | 7.23e-05 | |||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 39.99 E-value: 7.23e-05
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zf-CCCH_4 | pfam18044 | CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ... |
112-132 | 1.34e-04 | |||||
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and one histidine to coordinate the zinc ion. This domain is found in a wide variety of proteins such as E3 ligases. Pssm-ID: 465626 Cd Length: 22 Bit Score: 38.72 E-value: 1.34e-04
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WD40 | pfam00400 | WD domain, G-beta repeat; |
304-338 | 1.74e-04 | |||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.87 E-value: 1.74e-04
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
138-181 | 3.83e-04 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 42.59 E-value: 3.83e-04
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zf-CCCH | pfam00642 | Zinc finger C-x8-C-x5-C-x3-H type (and similar); |
109-132 | 2.09e-03 | |||||
Zinc finger C-x8-C-x5-C-x3-H type (and similar); Pssm-ID: 459885 [Multi-domain] Cd Length: 27 Bit Score: 35.25 E-value: 2.09e-03
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zf-CCCH_2 | pfam14608 | RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented ... |
113-132 | 4.53e-03 | |||||
RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented by fingers 5-7 of Nab2. Nab2 ZnF5-7 are zinc-fingers of the type C-x8-C-x5-C-x3-H. Nab2 ZnFs function in the generation of export-competent mRNPs. Mab2 is a conserved polyadenosine-RNA-binding Zn finger protein required for both mRNA export and polyadenylation regulation and becomes attached to the mRNP after splicing and during or immediately after polyadenylation. The three ZnFs, 5-7, have almost identical folds and, most unusually, associate with one another to form a single coherent structural unit. ZnF5-7 bind to eight consecutive adenines, and chemical shift perturbations identify residues on each finger that interact with RNA. Pssm-ID: 464217 Cd Length: 19 Bit Score: 34.41 E-value: 4.53e-03
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Blast search parameters | ||||
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