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F-box-like/WD repeat-containing protein TBL1Y [Homo sapiens]
WD40 domain-containing protein( domain architecture ID 10553538)
WD40 domain-containing protein similar to Homo sapiens F-box-like/WD repeat-containing protein TBL1X/TBL1Y/TBL1XR1
List of domain hits
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Name | Accession | Description | Interval | E-value | |||||
WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
174-480 | 8.42e-85 | |||||
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: 264.20 E-value: 8.42e-85
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LisH | pfam08513 | LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ... |
7-31 | 5.71e-07 | |||||
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex. : Pssm-ID: 462501 Cd Length: 25 Bit Score: 45.77 E-value: 5.71e-07
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8prop_heme_binding_protein super family | cl49617 | eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ... |
454-521 | 5.89e-04 | |||||
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> 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 nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion. The actual alignment was detected with superfamily member cd20778: Pssm-ID: 483957 [Multi-domain] Cd Length: 381 Bit Score: 42.27 E-value: 5.89e-04
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Name | Accession | Description | Interval | E-value | ||||||
WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
174-480 | 8.42e-85 | ||||||
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: 264.20 E-value: 8.42e-85
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
172-522 | 1.46e-78 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 251.75 E-value: 1.46e-78
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PTZ00420 | PTZ00420 | coronin; Provisional |
351-440 | 6.81e-11 | ||||||
coronin; Provisional Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 64.59 E-value: 6.81e-11
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
441-480 | 3.20e-10 | ||||||
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: 55.40 E-value: 3.20e-10
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WD40 | pfam00400 | WD domain, G-beta repeat; |
442-480 | 1.53e-09 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 53.12 E-value: 1.53e-09
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LisH | pfam08513 | LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ... |
7-31 | 5.71e-07 | ||||||
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex. Pssm-ID: 462501 Cd Length: 25 Bit Score: 45.77 E-value: 5.71e-07
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LisH | smart00667 | Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
7-36 | 1.44e-05 | ||||||
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly. Pssm-ID: 128913 Cd Length: 34 Bit Score: 42.04 E-value: 1.44e-05
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8prop_hemeD1_NirF | cd20778 | eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
454-521 | 5.89e-04 | ||||||
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: 42.27 E-value: 5.89e-04
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Name | Accession | Description | Interval | E-value | ||||||
WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
174-480 | 8.42e-85 | ||||||
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: 264.20 E-value: 8.42e-85
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
172-522 | 1.46e-78 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 251.75 E-value: 1.46e-78
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
172-483 | 2.99e-78 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 250.98 E-value: 2.99e-78
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
169-522 | 5.88e-63 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 210.92 E-value: 5.88e-63
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
268-522 | 2.72e-58 | ||||||
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: 195.25 E-value: 2.72e-58
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
245-522 | 6.43e-51 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 178.95 E-value: 6.43e-51
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PTZ00420 | PTZ00420 | coronin; Provisional |
351-440 | 6.81e-11 | ||||||
coronin; Provisional Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 64.59 E-value: 6.81e-11
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
441-480 | 3.20e-10 | ||||||
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: 55.40 E-value: 3.20e-10
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PTZ00420 | PTZ00420 | coronin; Provisional |
175-318 | 4.81e-10 | ||||||
coronin; Provisional Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 61.89 E-value: 4.81e-10
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
350-387 | 9.04e-10 | ||||||
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: 53.86 E-value: 9.04e-10
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WD40 | pfam00400 | WD domain, G-beta repeat; |
442-480 | 1.53e-09 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 53.12 E-value: 1.53e-09
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WD40 | pfam00400 | WD domain, G-beta repeat; |
351-387 | 5.66e-09 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 51.58 E-value: 5.66e-09
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PLN00181 | PLN00181 | protein SPA1-RELATED; Provisional |
374-486 | 2.58e-08 | ||||||
protein SPA1-RELATED; Provisional Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 56.63 E-value: 2.58e-08
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PTZ00421 | PTZ00421 | coronin; Provisional |
357-489 | 3.13e-08 | ||||||
coronin; Provisional Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 56.05 E-value: 3.13e-08
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LisH | pfam08513 | LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ... |
7-31 | 5.71e-07 | ||||||
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex. Pssm-ID: 462501 Cd Length: 25 Bit Score: 45.77 E-value: 5.71e-07
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PLN00181 | PLN00181 | protein SPA1-RELATED; Provisional |
359-484 | 1.34e-06 | ||||||
protein SPA1-RELATED; Provisional Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 51.24 E-value: 1.34e-06
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PLN00181 | PLN00181 | protein SPA1-RELATED; Provisional |
281-522 | 1.69e-06 | ||||||
protein SPA1-RELATED; Provisional Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 50.86 E-value: 1.69e-06
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
174-207 | 2.40e-06 | ||||||
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: 44.23 E-value: 2.40e-06
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
393-438 | 3.35e-06 | ||||||
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: 43.84 E-value: 3.35e-06
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WD40 | pfam00400 | WD domain, G-beta repeat; |
393-438 | 1.30e-05 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 42.33 E-value: 1.30e-05
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LisH | smart00667 | Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
7-36 | 1.44e-05 | ||||||
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly. Pssm-ID: 128913 Cd Length: 34 Bit Score: 42.04 E-value: 1.44e-05
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WD40 | pfam00400 | WD domain, G-beta repeat; |
173-207 | 1.59e-05 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 41.95 E-value: 1.59e-05
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
265-304 | 1.83e-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: 1.83e-05
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ANAPC4_WD40 | pfam12894 | Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
186-285 | 2.62e-05 | ||||||
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC, Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 42.65 E-value: 2.62e-05
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PTZ00421 | PTZ00421 | coronin; Provisional |
175-310 | 8.91e-05 | ||||||
coronin; Provisional Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 44.88 E-value: 8.91e-05
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eIF2A | pfam08662 | Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ... |
282-490 | 8.92e-05 | ||||||
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation initiation factors. Pssm-ID: 462552 [Multi-domain] Cd Length: 194 Bit Score: 43.42 E-value: 8.92e-05
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YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
410-522 | 1.31e-04 | ||||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 43.53 E-value: 1.31e-04
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WD40 | pfam00400 | WD domain, G-beta repeat; |
266-304 | 1.41e-04 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.25 E-value: 1.41e-04
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ANAPC4_WD40 | pfam12894 | Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
435-502 | 5.53e-04 | ||||||
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC, Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 39.18 E-value: 5.53e-04
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8prop_hemeD1_NirF | cd20778 | eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
454-521 | 5.89e-04 | ||||||
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: 42.27 E-value: 5.89e-04
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
235-262 | 8.90e-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: 36.91 E-value: 8.90e-04
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ANAPC4_WD40 | pfam12894 | Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
241-329 | 1.06e-03 | ||||||
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC, Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 38.41 E-value: 1.06e-03
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WD40 | pfam00400 | WD domain, G-beta repeat; |
235-262 | 1.07e-03 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.94 E-value: 1.07e-03
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PTZ00420 | PTZ00420 | coronin; Provisional |
166-251 | 1.88e-03 | ||||||
coronin; Provisional Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 41.09 E-value: 1.88e-03
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ANAPC4_WD40 | pfam12894 | Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
336-410 | 3.34e-03 | ||||||
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC, Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 36.87 E-value: 3.34e-03
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Blast search parameters | ||||
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