RecName: Full=DDB1- and CUL4-associated factor 5; AltName: Full=Breakpoint cluster region protein 2; Short=BCRP2; AltName: Full=WD repeat-containing protein 22
WD40 repeat domain-containing protein( domain architecture ID 11455410)
WD40 repeat domain-containing protein similar to proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly
List of domain hits
Name | Accession | Description | Interval | E-value | ||||||
WD40 | COG2319 | WD40 repeat [General function prediction only]; |
49-362 | 1.63e-33 | ||||||
WD40 repeat [General function prediction only]; : Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 133.88 E-value: 1.63e-33
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Name | Accession | Description | Interval | E-value | ||||||
WD40 | COG2319 | WD40 repeat [General function prediction only]; |
49-362 | 1.63e-33 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 133.88 E-value: 1.63e-33
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
49-361 | 4.47e-31 | ||||||
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: 123.98 E-value: 4.47e-31
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
140-171 | 3.02e-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: 41.91 E-value: 3.02e-05
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PTZ00420 | PTZ00420 | coronin; Provisional |
286-360 | 1.21e-04 | ||||||
coronin; Provisional Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 45.71 E-value: 1.21e-04
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WD40 | pfam00400 | WD domain, G-beta repeat; |
49-81 | 1.61e-04 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.64 E-value: 1.61e-04
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Name | Accession | Description | Interval | E-value | ||||||
WD40 | COG2319 | WD40 repeat [General function prediction only]; |
49-362 | 1.63e-33 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 133.88 E-value: 1.63e-33
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
49-361 | 4.47e-31 | ||||||
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: 123.98 E-value: 4.47e-31
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
3-362 | 2.44e-30 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 124.64 E-value: 2.44e-30
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
46-171 | 3.19e-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: 74.29 E-value: 3.19e-14
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
49-132 | 3.26e-09 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 59.92 E-value: 3.26e-09
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
140-171 | 3.02e-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: 41.91 E-value: 3.02e-05
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PTZ00420 | PTZ00420 | coronin; Provisional |
286-360 | 1.21e-04 | ||||||
coronin; Provisional Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 45.71 E-value: 1.21e-04
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
327-361 | 1.56e-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: 39.99 E-value: 1.56e-04
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WD40 | pfam00400 | WD domain, G-beta repeat; |
49-81 | 1.61e-04 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.64 E-value: 1.61e-04
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PLN00181 | PLN00181 | protein SPA1-RELATED; Provisional |
19-224 | 1.73e-04 | ||||||
protein SPA1-RELATED; Provisional Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 45.46 E-value: 1.73e-04
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WD40 | pfam00400 | WD domain, G-beta repeat; |
140-171 | 2.27e-04 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.25 E-value: 2.27e-04
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
51-82 | 9.34e-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: 37.68 E-value: 9.34e-04
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WD40 | pfam00400 | WD domain, G-beta repeat; |
327-361 | 1.39e-03 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.32 E-value: 1.39e-03
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YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
59-172 | 1.92e-03 | ||||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 40.83 E-value: 1.92e-03
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8prop_hemeD1_NirF | cd20778 | eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
117-175 | 9.09e-03 | ||||||
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC. Pssm-ID: 467722 [Multi-domain] Cd Length: 381 Bit Score: 39.57 E-value: 9.09e-03
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Blast search parameters | ||||
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