zinc finger CCCH domain-containing protein 48 [Brassica rapa]
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
WD40 | COG2319 | WD40 repeat [General function prediction only]; |
123-419 | 7.55e-34 | |||||
WD40 repeat [General function prediction only]; : Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 130.80 E-value: 7.55e-34
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ZnF_C3H1 | smart00356 | zinc finger; |
100-122 | 2.07e-06 | |||||
zinc finger; : Pssm-ID: 214632 [Multi-domain] Cd Length: 27 Bit Score: 43.77 E-value: 2.07e-06
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Name | Accession | Description | Interval | E-value | |||||
WD40 | COG2319 | WD40 repeat [General function prediction only]; |
123-419 | 7.55e-34 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 130.80 E-value: 7.55e-34
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
131-415 | 2.48e-33 | |||||
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: 126.68 E-value: 2.48e-33
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ZnF_C3H1 | smart00356 | zinc finger; |
100-122 | 2.07e-06 | |||||
zinc finger; Pssm-ID: 214632 [Multi-domain] Cd Length: 27 Bit Score: 43.77 E-value: 2.07e-06
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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 ... |
103-121 | 3.88e-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: 3.88e-06
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PTZ00421 | PTZ00421 | coronin; Provisional |
231-326 | 6.46e-06 | |||||
coronin; Provisional Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 48.35 E-value: 6.46e-06
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
291-327 | 8.66e-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: 39.60 E-value: 8.66e-05
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WD40 | pfam00400 | WD domain, G-beta repeat; |
129-167 | 1.57e-04 | |||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.87 E-value: 1.57e-04
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Name | Accession | Description | Interval | E-value | |||||
WD40 | COG2319 | WD40 repeat [General function prediction only]; |
123-419 | 7.55e-34 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 130.80 E-value: 7.55e-34
|
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
131-415 | 2.48e-33 | |||||
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: 126.68 E-value: 2.48e-33
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
131-418 | 4.25e-32 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 125.79 E-value: 4.25e-32
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
127-327 | 1.15e-29 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 118.86 E-value: 1.15e-29
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
130-327 | 4.16e-26 | |||||
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: 106.65 E-value: 4.16e-26
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
127-328 | 1.78e-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: 99.33 E-value: 1.78e-23
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
118-288 | 1.54e-15 | |||||
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: 76.60 E-value: 1.54e-15
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
203-419 | 8.27e-14 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 72.64 E-value: 8.27e-14
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ZnF_C3H1 | smart00356 | zinc finger; |
100-122 | 2.07e-06 | |||||
zinc finger; Pssm-ID: 214632 [Multi-domain] Cd Length: 27 Bit Score: 43.77 E-value: 2.07e-06
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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 ... |
103-121 | 3.88e-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: 3.88e-06
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PTZ00421 | PTZ00421 | coronin; Provisional |
231-326 | 6.46e-06 | |||||
coronin; Provisional Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 48.35 E-value: 6.46e-06
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
291-327 | 8.66e-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: 39.60 E-value: 8.66e-05
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WD40 | pfam00400 | WD domain, G-beta repeat; |
129-167 | 1.57e-04 | |||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.87 E-value: 1.57e-04
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
128-167 | 1.59e-04 | |||||
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: 38.83 E-value: 1.59e-04
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WD40 | pfam00400 | WD domain, G-beta repeat; |
293-327 | 1.97e-04 | |||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.48 E-value: 1.97e-04
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zf-CCCH | pfam00642 | Zinc finger C-x8-C-x5-C-x3-H type (and similar); |
98-121 | 2.80e-04 | |||||
Zinc finger C-x8-C-x5-C-x3-H type (and similar); Pssm-ID: 459885 [Multi-domain] Cd Length: 27 Bit Score: 37.94 E-value: 2.80e-04
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zf-CCCH_4 | pfam18044 | CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ... |
101-121 | 3.96e-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: 37.57 E-value: 3.96e-04
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
127-170 | 1.56e-03 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 40.66 E-value: 1.56e-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 ... |
102-121 | 3.97e-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: 3.97e-03
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Blast search parameters | ||||
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