brain tumor, isoform E [Drosophila melanogaster]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| NHL_brat_like | cd14959 | NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ... |
760-1030 | 5.46e-169 | |||||
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; Drosophila brain-tumor (brat) has been identified as a tumor suppressor that negatively regulates cell proliferation during development of the Drosophila larval brain. It appears to be recruited to the 3'-untranslated region of hunchback RNA and regulates its translation by forming a complex with Pumilio (Pum) and Nanos (Nos). The NHL domain of brat appears to be involved by interacting with the RNA-binding Puf repeats of Pumilio, a sequence-specific RNA binding protein. This family also contains the Caenorhabditis elegans homolog NCL-1. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. : Pssm-ID: 271329 [Multi-domain] Cd Length: 274 Bit Score: 496.41 E-value: 5.46e-169
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| CC_brat-like | cd20482 | coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ... |
382-503 | 1.47e-39 | |||||
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs. : Pssm-ID: 467844 [Multi-domain] Cd Length: 122 Bit Score: 142.68 E-value: 1.47e-39
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| Bbox1_BRAT-like | cd19813 | B-box-type 1 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and ... |
178-222 | 4.10e-20 | |||||
B-box-type 1 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and similar proteins; BRAT is a NHL-domain family protein that functions as a translational repressor to inhibit cell proliferation. The family also contains Caenorhabditis elegans B-box type zinc finger protein ncl-1, a C. elegans Brat homolog which functions as a translational repressor that inhibits protein synthesis. BRAT contains Bbox1 and Bbox2 zinc fingers and NHL repeats. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. : Pssm-ID: 380871 Cd Length: 44 Bit Score: 84.38 E-value: 4.10e-20
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| Bbox2_BRAT-like | cd19798 | B-box-type 2 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and ... |
326-366 | 1.71e-18 | |||||
B-box-type 2 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and similar proteins; BRAT is a NHL-domain family protein that functions as a translational repressor to inhibit cell proliferation. This family also contains Caenorhabditis elegans B-box type zinc finger protein ncl-1, a C. elegans Brat homolog which functions as a translational repressor that inhibits protein synthesis. BRAT contains Bbox1 and Bbox2 zinc fingers and NHL repeats. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. : Pssm-ID: 380856 Cd Length: 44 Bit Score: 79.65 E-value: 1.71e-18
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| Name | Accession | Description | Interval | E-value | |||||
| NHL_brat_like | cd14959 | NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ... |
760-1030 | 5.46e-169 | |||||
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; Drosophila brain-tumor (brat) has been identified as a tumor suppressor that negatively regulates cell proliferation during development of the Drosophila larval brain. It appears to be recruited to the 3'-untranslated region of hunchback RNA and regulates its translation by forming a complex with Pumilio (Pum) and Nanos (Nos). The NHL domain of brat appears to be involved by interacting with the RNA-binding Puf repeats of Pumilio, a sequence-specific RNA binding protein. This family also contains the Caenorhabditis elegans homolog NCL-1. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271329 [Multi-domain] Cd Length: 274 Bit Score: 496.41 E-value: 5.46e-169
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| CC_brat-like | cd20482 | coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ... |
382-503 | 1.47e-39 | |||||
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs. Pssm-ID: 467844 [Multi-domain] Cd Length: 122 Bit Score: 142.68 E-value: 1.47e-39
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| Bbox1_BRAT-like | cd19813 | B-box-type 1 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and ... |
178-222 | 4.10e-20 | |||||
B-box-type 1 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and similar proteins; BRAT is a NHL-domain family protein that functions as a translational repressor to inhibit cell proliferation. The family also contains Caenorhabditis elegans B-box type zinc finger protein ncl-1, a C. elegans Brat homolog which functions as a translational repressor that inhibits protein synthesis. BRAT contains Bbox1 and Bbox2 zinc fingers and NHL repeats. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. Pssm-ID: 380871 Cd Length: 44 Bit Score: 84.38 E-value: 4.10e-20
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| Bbox2_BRAT-like | cd19798 | B-box-type 2 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and ... |
326-366 | 1.71e-18 | |||||
B-box-type 2 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and similar proteins; BRAT is a NHL-domain family protein that functions as a translational repressor to inhibit cell proliferation. This family also contains Caenorhabditis elegans B-box type zinc finger protein ncl-1, a C. elegans Brat homolog which functions as a translational repressor that inhibits protein synthesis. BRAT contains Bbox1 and Bbox2 zinc fingers and NHL repeats. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. Pssm-ID: 380856 Cd Length: 44 Bit Score: 79.65 E-value: 1.71e-18
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| Vgb | COG4257 | Streptogramin lyase [Defense mechanisms]; |
772-1018 | 9.13e-10 | |||||
Streptogramin lyase [Defense mechanisms]; Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 60.80 E-value: 9.13e-10
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| NHL | pfam01436 | NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ... |
780-807 | 5.38e-08 | |||||
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is about 40 residues long and resembles the WD repeat pfam00400. The repeats have a catalytic activity in Swiss:P10731, proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Swiss:Q13049 interacts with the activation domain of Tat. This interaction is me diated by the NHL repeats. Pssm-ID: 396153 [Multi-domain] Cd Length: 28 Bit Score: 49.32 E-value: 5.38e-08
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| zf-B_box | pfam00643 | B-box zinc finger; |
328-366 | 5.42e-08 | |||||
B-box zinc finger; Pssm-ID: 459886 [Multi-domain] Cd Length: 42 Bit Score: 49.78 E-value: 5.42e-08
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| BBOX | smart00336 | B-Box-type zinc finger; |
328-357 | 6.36e-04 | |||||
B-Box-type zinc finger; Pssm-ID: 197662 [Multi-domain] Cd Length: 42 Bit Score: 38.47 E-value: 6.36e-04
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| BBOX | smart00336 | B-Box-type zinc finger; |
176-222 | 2.87e-03 | |||||
B-Box-type zinc finger; Pssm-ID: 197662 [Multi-domain] Cd Length: 42 Bit Score: 36.55 E-value: 2.87e-03
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| zf-B_box | pfam00643 | B-box zinc finger; |
176-222 | 3.09e-03 | |||||
B-box zinc finger; Pssm-ID: 459886 [Multi-domain] Cd Length: 42 Bit Score: 36.30 E-value: 3.09e-03
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| Name | Accession | Description | Interval | E-value | |||||
| NHL_brat_like | cd14959 | NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ... |
760-1030 | 5.46e-169 | |||||
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; Drosophila brain-tumor (brat) has been identified as a tumor suppressor that negatively regulates cell proliferation during development of the Drosophila larval brain. It appears to be recruited to the 3'-untranslated region of hunchback RNA and regulates its translation by forming a complex with Pumilio (Pum) and Nanos (Nos). The NHL domain of brat appears to be involved by interacting with the RNA-binding Puf repeats of Pumilio, a sequence-specific RNA binding protein. This family also contains the Caenorhabditis elegans homolog NCL-1. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271329 [Multi-domain] Cd Length: 274 Bit Score: 496.41 E-value: 5.46e-169
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| NHL_TRIM71_like | cd14954 | NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
756-1016 | 5.65e-66 | |||||
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271324 [Multi-domain] Cd Length: 285 Bit Score: 223.96 E-value: 5.65e-66
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| NHL | cd05819 | NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
774-1027 | 7.34e-63 | |||||
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats. Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 214.49 E-value: 7.34e-63
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| NHL_TRIM71_like | cd14954 | NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
766-979 | 5.59e-58 | |||||
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271324 [Multi-domain] Cd Length: 285 Bit Score: 201.24 E-value: 5.59e-58
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| NHL | cd05819 | NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
766-979 | 1.12e-49 | |||||
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats. Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 177.13 E-value: 1.12e-49
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| NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
769-998 | 2.58e-45 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 164.76 E-value: 2.58e-45
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| NHL_TRIM2_like | cd14960 | NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ... |
770-1031 | 6.41e-45 | |||||
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; The E3 ubiquitin-protein ligase TRIM2 is responsible for ubiquinating the apoptosis-inducing Bcl-2-interacting mediator of cell death (Bim), when the latter is phosphorylated by p42/p44 MAPK. TRIM2 regulates the ubiquitination of neurofilament light subunit (NF-L), deficiencies in TRIM2 result in increased NF-L levels in axons and subsequent axonopathy. TRIM2 is also involved in regulating axon outgrowth during development; it contains RING and BBOX domains, the NHL repeat domain is located at its C-terminus. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271330 [Multi-domain] Cd Length: 274 Bit Score: 163.67 E-value: 6.41e-45
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| NHL_like_5 | cd14963 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
773-1026 | 5.60e-44 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271333 [Multi-domain] Cd Length: 268 Bit Score: 160.53 E-value: 5.60e-44
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| NHL_like_5 | cd14963 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
769-979 | 1.50e-40 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271333 [Multi-domain] Cd Length: 268 Bit Score: 150.90 E-value: 1.50e-40
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| NHL_like_2 | cd14957 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
770-989 | 2.91e-40 | |||||
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271327 [Multi-domain] Cd Length: 280 Bit Score: 150.49 E-value: 2.91e-40
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| NHL_like_2 | cd14957 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
766-979 | 1.21e-39 | |||||
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271327 [Multi-domain] Cd Length: 280 Bit Score: 148.57 E-value: 1.21e-39
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| CC_brat-like | cd20482 | coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ... |
382-503 | 1.47e-39 | |||||
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs. Pssm-ID: 467844 [Multi-domain] Cd Length: 122 Bit Score: 142.68 E-value: 1.47e-39
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| NHL_like_4 | cd14955 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
769-993 | 2.58e-39 | |||||
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271325 [Multi-domain] Cd Length: 279 Bit Score: 147.72 E-value: 2.58e-39
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| NHL_like_4 | cd14955 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
769-979 | 1.79e-36 | |||||
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271325 [Multi-domain] Cd Length: 279 Bit Score: 139.25 E-value: 1.79e-36
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| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
771-979 | 6.30e-31 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 123.08 E-value: 6.30e-31
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| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
770-991 | 3.86e-30 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 120.77 E-value: 3.86e-30
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| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
777-943 | 7.83e-30 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 120.00 E-value: 7.83e-30
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| NHL_TRIM32_like | cd14961 | NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ... |
771-1028 | 5.01e-29 | |||||
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; The E3 ubiquitin-protein ligase TRIM32 (HT2A) is widely expressed and is responsible for ubiquinating a large variety of targets, including dysbindin (DTNBP1), NPHP7/Glis2, TAp73, and others. TRIM32 promotes disassociation of the plakoglobin-PI3K complex and reduces PI3K-Akt-FoxO signaling. Mutations in TRIM32 have been implemented in the two diverse diseases limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11 (BBS11). The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271331 [Multi-domain] Cd Length: 273 Bit Score: 117.38 E-value: 5.01e-29
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| NHL | cd05819 | NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
769-908 | 3.86e-28 | |||||
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats. Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 114.72 E-value: 3.86e-28
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| NHL_like_4 | cd14955 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
769-942 | 1.09e-27 | |||||
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271325 [Multi-domain] Cd Length: 279 Bit Score: 113.83 E-value: 1.09e-27
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| NHL_like_2 | cd14957 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
770-899 | 3.77e-23 | |||||
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271327 [Multi-domain] Cd Length: 280 Bit Score: 100.80 E-value: 3.77e-23
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| NHL_like_2 | cd14957 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
813-994 | 4.77e-21 | |||||
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271327 [Multi-domain] Cd Length: 280 Bit Score: 94.64 E-value: 4.77e-21
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| Bbox1_BRAT-like | cd19813 | B-box-type 1 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and ... |
178-222 | 4.10e-20 | |||||
B-box-type 1 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and similar proteins; BRAT is a NHL-domain family protein that functions as a translational repressor to inhibit cell proliferation. The family also contains Caenorhabditis elegans B-box type zinc finger protein ncl-1, a C. elegans Brat homolog which functions as a translational repressor that inhibits protein synthesis. BRAT contains Bbox1 and Bbox2 zinc fingers and NHL repeats. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. Pssm-ID: 380871 Cd Length: 44 Bit Score: 84.38 E-value: 4.10e-20
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| NHL_TRIM2_like | cd14960 | NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ... |
769-889 | 2.18e-19 | |||||
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; The E3 ubiquitin-protein ligase TRIM2 is responsible for ubiquinating the apoptosis-inducing Bcl-2-interacting mediator of cell death (Bim), when the latter is phosphorylated by p42/p44 MAPK. TRIM2 regulates the ubiquitination of neurofilament light subunit (NF-L), deficiencies in TRIM2 result in increased NF-L levels in axons and subsequent axonopathy. TRIM2 is also involved in regulating axon outgrowth during development; it contains RING and BBOX domains, the NHL repeat domain is located at its C-terminus. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271330 [Multi-domain] Cd Length: 274 Bit Score: 89.33 E-value: 2.18e-19
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| Bbox2_BRAT-like | cd19798 | B-box-type 2 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and ... |
326-366 | 1.71e-18 | |||||
B-box-type 2 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and similar proteins; BRAT is a NHL-domain family protein that functions as a translational repressor to inhibit cell proliferation. This family also contains Caenorhabditis elegans B-box type zinc finger protein ncl-1, a C. elegans Brat homolog which functions as a translational repressor that inhibits protein synthesis. BRAT contains Bbox1 and Bbox2 zinc fingers and NHL repeats. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. Pssm-ID: 380856 Cd Length: 44 Bit Score: 79.65 E-value: 1.71e-18
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| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
871-993 | 1.33e-15 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 78.01 E-value: 1.33e-15
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| NHL_TRIM32_like | cd14961 | NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ... |
770-942 | 9.20e-15 | |||||
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; The E3 ubiquitin-protein ligase TRIM32 (HT2A) is widely expressed and is responsible for ubiquinating a large variety of targets, including dysbindin (DTNBP1), NPHP7/Glis2, TAp73, and others. TRIM32 promotes disassociation of the plakoglobin-PI3K complex and reduces PI3K-Akt-FoxO signaling. Mutations in TRIM32 have been implemented in the two diverse diseases limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11 (BBS11). The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271331 [Multi-domain] Cd Length: 273 Bit Score: 75.78 E-value: 9.20e-15
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| NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
769-854 | 3.63e-12 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 68.08 E-value: 3.63e-12
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| NHL_PAL_like | cd14958 | Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ... |
770-899 | 1.46e-11 | |||||
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271328 [Multi-domain] Cd Length: 300 Bit Score: 66.52 E-value: 1.46e-11
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| NHL_PAL_like | cd14958 | Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ... |
772-993 | 2.04e-11 | |||||
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271328 [Multi-domain] Cd Length: 300 Bit Score: 66.13 E-value: 2.04e-11
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| NHL_like_1 | cd14953 | Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
779-979 | 8.57e-10 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 61.39 E-value: 8.57e-10
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| Vgb | COG4257 | Streptogramin lyase [Defense mechanisms]; |
772-1018 | 9.13e-10 | |||||
Streptogramin lyase [Defense mechanisms]; Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 60.80 E-value: 9.13e-10
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| NHL_like_1 | cd14953 | Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
779-979 | 4.64e-09 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 59.08 E-value: 4.64e-09
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| NHL_like_4 | cd14955 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
768-808 | 2.12e-08 | |||||
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271325 [Multi-domain] Cd Length: 279 Bit Score: 56.82 E-value: 2.12e-08
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| NHL | pfam01436 | NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ... |
780-807 | 5.38e-08 | |||||
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is about 40 residues long and resembles the WD repeat pfam00400. The repeats have a catalytic activity in Swiss:P10731, proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Swiss:Q13049 interacts with the activation domain of Tat. This interaction is me diated by the NHL repeats. Pssm-ID: 396153 [Multi-domain] Cd Length: 28 Bit Score: 49.32 E-value: 5.38e-08
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| zf-B_box | pfam00643 | B-box zinc finger; |
328-366 | 5.42e-08 | |||||
B-box zinc finger; Pssm-ID: 459886 [Multi-domain] Cd Length: 42 Bit Score: 49.78 E-value: 5.42e-08
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| NHL_TRIM71_like | cd14954 | NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
758-807 | 7.63e-08 | |||||
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271324 [Multi-domain] Cd Length: 285 Bit Score: 55.25 E-value: 7.63e-08
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| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
766-837 | 8.96e-08 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 54.90 E-value: 8.96e-08
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| Bbox2_TIF1g_C-VI | cd19830 | B-box-type 2 zinc finger found in transcription intermediary factor 1 gamma (TIF1-gamma); ... |
326-356 | 1.49e-07 | |||||
B-box-type 2 zinc finger found in transcription intermediary factor 1 gamma (TIF1-gamma); TIF1-gamma, also known as tripartite motif-containing 33 (TRIM33), ectodermin, RFG7, or PTC7, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TIF1-gamma is an E3-ubiquitin ligase that functions as a regulator of transforming growth factor beta (TGFbeta) signaling. It inhibits the Smad4-mediated TGFbeta response by interaction with Smad2/3 or ubiquitylation of Smad4. Moreover, TIF1gamma is an important regulator of transcription during hematopoiesis, as well as a key actor of tumorigenesis. Like other TIF1 family members, TIF1-gamma also contains an intrinsic transcriptional silencing function. It can control erythroid cell fate by regulating transcription elongation. It can bind to the anaphase-promoting complex/cyclosome (APC/C) and promotes mitosis. Pssm-ID: 380888 Cd Length: 53 Bit Score: 48.90 E-value: 1.49e-07
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| NHL_TRIM32_like | cd14961 | NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ... |
769-890 | 2.44e-07 | |||||
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; The E3 ubiquitin-protein ligase TRIM32 (HT2A) is widely expressed and is responsible for ubiquinating a large variety of targets, including dysbindin (DTNBP1), NPHP7/Glis2, TAp73, and others. TRIM32 promotes disassociation of the plakoglobin-PI3K complex and reduces PI3K-Akt-FoxO signaling. Mutations in TRIM32 have been implemented in the two diverse diseases limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11 (BBS11). The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271331 [Multi-domain] Cd Length: 273 Bit Score: 53.43 E-value: 2.44e-07
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| Bbox2 | cd19756 | B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of ... |
327-366 | 3.18e-07 | |||||
B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interaction. Based on different consensus sequence and the spacing of the 7-8 zinc-binding residues, B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). The family corresponds to type 2 B-box (Bbox2). Pssm-ID: 380814 [Multi-domain] Cd Length: 39 Bit Score: 47.41 E-value: 3.18e-07
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| Bbox2_TIF1_C-VI | cd19775 | B-box-type 2 zinc finger found in transcription intermediary factor 1 (TIF1) family; This ... |
326-356 | 4.30e-07 | |||||
B-box-type 2 zinc finger found in transcription intermediary factor 1 (TIF1) family; This family corresponds to the TIF1 family of transcriptional cofactors including TIF1-alpha (TRIM24), TIF1-beta (TRIM28), and TIF1-gamma (TRIM33), which belong to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1alpha and TIF1beta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. They bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. TIF1gamma is structurally closely related to TIF1alpha and TIF1beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatinic proteins HP1alpha, beta and gamma. It cannot bind to nuclear receptors (NRs). Pssm-ID: 380833 Cd Length: 43 Bit Score: 47.33 E-value: 4.30e-07
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| NHL-2_like | cd14951 | NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ... |
771-977 | 6.49e-07 | |||||
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL repeat-containing protein 2 (NHLRC2) and related bacterial proteins; members of this eukaryotic and bacterial family are uncharacterized, the NHL repeat domain is found C-terminally of a thioredoxin domain. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271321 [Multi-domain] Cd Length: 334 Bit Score: 52.58 E-value: 6.49e-07
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| NHL_like_2 | cd14957 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
766-808 | 1.51e-06 | |||||
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271327 [Multi-domain] Cd Length: 280 Bit Score: 51.11 E-value: 1.51e-06
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| Bbox2_TRIM66-like | cd19794 | B-box-type 2 zinc finger found in tripartite motif-containing protein 66 (TRIM66) and similar ... |
326-368 | 1.63e-06 | |||||
B-box-type 2 zinc finger found in tripartite motif-containing protein 66 (TRIM66) and similar proteins; TRIM66, also termed transcriptional intermediary factor 1 delta (TIF1delta), is a novel heterochromatin protein 1 (HP1)-interacting member of the transcriptional intermediary factor 1 (TIF1) family expressed by elongating spermatids. Like other TIF1 proteins, TRIM66 displays a potent trichostatin A (TSA)-sensitive repression function; TSA is a specific inhibitor of histone deacetylases. Moreover, TRIM66 plays an important role in heterochromatin-mediated gene silencing during postmeiotic phases of spermatogenesis. It functions as a negative regulator of postmeiotic genes acting through HP1 isotype gamma (HP1gamma) complex formation and centromere association. TRIM66 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. Pssm-ID: 380852 Cd Length: 43 Bit Score: 45.53 E-value: 1.63e-06
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| Bbox2_TRIM2-like | cd19759 | B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM2, TRIM3, and ... |
326-357 | 6.00e-06 | |||||
B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM2, TRIM3, and similar proteins; TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It also plays an important role in the central nervous system (CNS). In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. Both TRIM2 and TRIM3 belong to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. Pssm-ID: 380817 [Multi-domain] Cd Length: 42 Bit Score: 43.97 E-value: 6.00e-06
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| Bbox1 | cd19757 | B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of ... |
179-222 | 6.00e-06 | |||||
B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain, in functionally unrelated proteins, most likely mediating protein-protein interactions. Based on different consensus sequences and the spacing of the 7-8 zinc-binding residues, the B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). This family corresponds to the type 1 B-box (Bbox1). Pssm-ID: 380815 [Multi-domain] Cd Length: 44 Bit Score: 44.02 E-value: 6.00e-06
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| Bbox2_TIF1a_C-VI | cd19828 | B-box-type 2 zinc finger found in transcription intermediary factor 1-alpha (TIF1-alpha); ... |
326-356 | 7.52e-06 | |||||
B-box-type 2 zinc finger found in transcription intermediary factor 1-alpha (TIF1-alpha); TIF1-alpha, also known as tripartite motif-containing protein 24 (TRIM24), E3 ubiquitin-protein ligase TRIM24, or RING finger protein 82, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TIF1-alpha interacts specifically and in a ligand-dependent manner with the ligand binding domain (LBD) of several nuclear receptors (NRs), including retinoid X (RXR), retinoic acid (RAR), vitamin D3 (VDR), estrogen (ER), and progesterone (PR) receptors. It also associates with heterochromatin-associated factors HP1alpha, MOD1 (HP1beta), and MOD2 (HP1gamma), as well as the vertebrate Kruppel-type (C2H2) zinc finger proteins that contain the transcriptional silencing domain KRAB. TIF1-alpha is a ligand-dependent co-repressor of retinoic acid receptor (RAR) that interacts with multiple nuclear receptors in vitro via an LXXLL motif and further acts as a gatekeeper of liver carcinogenesis. It also functions as an E3-ubiquitin ligase targeting p53, and is broadly associated with chromatin silencing. Moreover, it is a chromatin regulator that recognizes specific, combinatorial histone modifications through its C-terminal PHD-Bromo region. In addition, it interacts with chromatin and estrogen receptor to activate estrogen-dependent genes associated with cellular proliferation and tumor development. Pssm-ID: 380886 Cd Length: 57 Bit Score: 44.26 E-value: 7.52e-06
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| Bbox2_TIF1b_C-VI | cd19829 | B-box-type 2 zinc finger found in transcription intermediary factor 1-beta (TIF1-beta); ... |
326-356 | 8.67e-06 | |||||
B-box-type 2 zinc finger found in transcription intermediary factor 1-beta (TIF1-beta); TIF1-beta, also known as Kruppel-associated Box (KRAB)-associated protein 1 (KAP-1), KRAB-interacting protein 1 (KRIP-1), nuclear co-repressor KAP-1, RING finger protein 96, tripartite motif-containing protein 28 (TRIM28), or E3 SUMO-protein ligase TRIM28, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD) and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TIF1-beta acts as a nuclear co-repressor that plays a role in transcription and in the DNA damage response. Upon DNA damage, the phosphorylation of KAP-1 on serine 824 by the ataxia telangiectasia-mutated (ATM) kinase enhances cell survival and facilitates chromatin relaxation and heterochromatic DNA repair. It also regulates CHD3 nucleosome remodeling during the DNA double-strand break (DSB) response. Meanwhile, KAP-1 can be dephosphorylated by protein phosphatase PP4C in the DNA damage response. Moreover, KAP-1 is a co-activator of the orphan nuclear receptor NGFI-B (or Nur77) and is involved in NGFI-B-dependent transcription. It is also a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase. The N-terminal RBCC domains of TIF1-beta are responsible for the interaction with KRAB zinc finger proteins (KRAB-ZFPs), MDM2, MM1, C/EBPbeta, and the regulation of homo- and heterodimerization. The C-terminal PHD/Bromo domains are involved in interacting with SETDB1, Mi-2alpha and other proteins to form complexes with histone deacetylase or methyltransferase activity. Pssm-ID: 380887 Cd Length: 44 Bit Score: 43.66 E-value: 8.67e-06
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| Bbox1_TRIM45_C-X | cd19809 | B-box-type 1 zinc finger found in tripartite motif-containing protein 45 (TRIM45) and similar ... |
179-222 | 1.11e-05 | |||||
B-box-type 1 zinc finger found in tripartite motif-containing protein 45 (TRIM45) and similar proteins; TRIM45, also known as RING finger protein 99 (RNF99), is a novel receptor for activated C-kinase (RACK1)-interacting protein that suppresses transcriptional activities of Elk-1 and AP-1, and downregulates mitogen-activated protein kinase (MAPK) signal transduction by inhibiting RACK1/PKC (protein kinase C) complex formation. It also negatively regulates tumor necrosis factor alpha (TNFalpha)-induced nuclear factor-kappaB (NF-kappa B)-mediated transcription, and suppresses cell proliferation. TRIM45 belongs to the C-X subclass of the TRIM (tripartite motif) family of proteins that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a filamin-type immunoglobulin (IG-FLMN) domain and NHL repeats positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. Pssm-ID: 380867 Cd Length: 46 Bit Score: 43.52 E-value: 1.11e-05
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| NHL-2_like | cd14951 | NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ... |
777-808 | 2.10e-05 | |||||
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL repeat-containing protein 2 (NHLRC2) and related bacterial proteins; members of this eukaryotic and bacterial family are uncharacterized, the NHL repeat domain is found C-terminally of a thioredoxin domain. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271321 [Multi-domain] Cd Length: 334 Bit Score: 47.96 E-value: 2.10e-05
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| Bbox2_TRIM45_C-X | cd19785 | B-box-type 2 zinc finger found in tripartite motif-containing protein 45 (TRIM45) and similar ... |
327-356 | 4.15e-05 | |||||
B-box-type 2 zinc finger found in tripartite motif-containing protein 45 (TRIM45) and similar proteins; TRIM45, also known as RING finger protein 99 (RNF99), is a novel receptor for activated C-kinase (RACK1)-interacting protein that suppresses transcriptional activities of Elk-1 and AP-1 and downregulates mitogen-activated protein kinase (MAPK) signal transduction by inhibiting RACK1/PKC (protein kinase C) complex formation. It also negatively regulates tumor necrosis factor alpha (TNFalpha)-induced nuclear factor-kappaB (NF-kappa B)-mediated transcription and suppresses cell proliferation. TRIM45 belongs to the C-X subclass of TRIM (tripartite motif) family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a filamin-type immunoglobulin (IG-FLMN) domain and NHL repeats positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. Pssm-ID: 380843 Cd Length: 43 Bit Score: 41.64 E-value: 4.15e-05
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| YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
785-945 | 4.68e-05 | |||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 46.23 E-value: 4.68e-05
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| NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
770-807 | 5.22e-05 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 46.12 E-value: 5.22e-05
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| Bbox1_TRIM71_C-VII | cd19812 | B-box-type 1 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar ... |
178-209 | 7.20e-05 | |||||
B-box-type 1 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar proteins; TRIM71, also known as protein lineage variant 41 (lin-41), is an E3 ubiquitin-protein ligase that may play essential roles in embryonic stem cells, cellular reprogramming, and the timing of embryonic neurogenesis. It was first identified in the nematode Caenorhabditis elegans as a target of the differentiation-associated microRNA (miRNA) let-7 (lethal 7) and therefore part of a heterochronic gene network that controls larval development. In humans, it regulates let-7 microRNA biogenesis via modulation of Lin28B protein polyubiquitination. TRIM71 localizes to cytoplasmic P-bodies and directly interacts with the miRNA pathway proteins Argonaute 2 (AGO2) and DICER. It represses miRNA activity by promoting degradative ubiquitination of AGO2. Moreover, TRIM71 associates with SHCBP1, a novel component of the fibroblast growth factor (FGF) signaling pathway, and regulates its non-degradative polyubiquitination. It is also involved in the post-transcriptional regulation of the CDKN1A, RBL1 and RBL2 or EGR1 mRNAs by mediating RNA-binding in embryonic stem cells. TRIM71 belongs to the C-VII subclass of the TRIM (tripartite motif) family of proteins that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. Pssm-ID: 380870 Cd Length: 44 Bit Score: 41.23 E-value: 7.20e-05
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| Bbox1_TRIM19_C-V | cd19804 | B-box-type 1 zinc finger found in promyelocytic leukemia protein (PML) and similar proteins; ... |
179-218 | 9.39e-05 | |||||
B-box-type 1 zinc finger found in promyelocytic leukemia protein (PML) and similar proteins; Protein PML, also known as RING finger protein 71 (RNF71) or tripartite motif-containing protein 19 (TRIM19), is predominantly a nuclear protein with a broad intrinsic antiviral activity. It is the eponymous component of PML nuclear bodies (PML NBs) and has been implicated in a wide variety of cellular processes, including DNA damage signaling, apoptosis, and transcription. PML interferes with the replication of many unrelated viruses, including human immunodeficiency virus 1 (HIV-1), human foamy virus (HFV), poliovirus, influenza virus, rabies virus, EMCV, adeno-associated virus (AAV), and vesicular stomatitis virus (VSV). It also selectively interacts with misfolded proteins through distinct substrate recognition sites, and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. PML belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. Pssm-ID: 380862 [Multi-domain] Cd Length: 47 Bit Score: 40.91 E-value: 9.39e-05
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| YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
781-888 | 1.92e-04 | |||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 44.30 E-value: 1.92e-04
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| Vgb | COG4257 | Streptogramin lyase [Defense mechanisms]; |
769-899 | 3.44e-04 | |||||
Streptogramin lyase [Defense mechanisms]; Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 43.85 E-value: 3.44e-04
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| Bbox2_TRIM16-like | cd19769 | B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, ... |
328-363 | 5.79e-04 | |||||
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, TRIM47 and similar proteins; This family includes a group of tripartite motif-containing proteins, such as TRIM16, TRIM29 and TRIM47. TRIM16, also termed estrogen-responsive B box protein (EBBP), is a regulator that may play a role in the regulation of keratinocyte differentiation. It may also act as a tumor suppressor through affecting cell proliferation and migration or tumorigenicity in carcinogenesis. TRIM29, also termed ataxia telangiectasia group D-associated protein (ATDC), plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. TRIM16 and TRIM29 belong to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. TRIM47 belongs to the C-IV subclass of TRIM family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. Pssm-ID: 380827 [Multi-domain] Cd Length: 46 Bit Score: 38.46 E-value: 5.79e-04
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| BBOX | smart00336 | B-Box-type zinc finger; |
328-357 | 6.36e-04 | |||||
B-Box-type zinc finger; Pssm-ID: 197662 [Multi-domain] Cd Length: 42 Bit Score: 38.47 E-value: 6.36e-04
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| Bbox1_TIF1a_C-VI | cd19845 | B-box-type 1 zinc finger found in transcription intermediary factor 1-alpha (TIF1-alpha); ... |
179-219 | 8.44e-04 | |||||
B-box-type 1 zinc finger found in transcription intermediary factor 1-alpha (TIF1-alpha); TIF1-alpha, also known as tripartite motif-containing protein 24 (TRIM24), E3 ubiquitin-protein ligase TRIM24, or RING finger protein 82, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TIF1-alpha interacts specifically and in a ligand-dependent manner with the ligand binding domain (LBD) of several nuclear receptors (NRs), including retinoic X (RXR), retinoic acid (RAR), vitamin D3 (VDR), estrogen (ER), and progesterone (PR) receptors. It also associates with heterochromatin-associated factors HP1alpha, MOD1 (HP1beta), and MOD2 (HP1gamma), as well as the vertebrate Kruppel-type (C2H2) zinc finger proteins that contain the transcriptional silencing domain KRAB. TIF1-alpha is a ligand-dependent co-repressor of retinoic acid receptor (RAR) that interacts with multiple nuclear receptors in vitro via an LXXLL motif and further acts as a gatekeeper of liver carcinogenesis. It also functions as an E3-ubiquitin ligase targeting p53, and is broadly associated with chromatin silencing. Moreover, it is a chromatin regulator that recognizes specific, combinatorial histone modifications through its C-terminal PHD-Bromo region. In addition, it interacts with chromatin and estrogen receptor to activate estrogen-dependent genes associated with cellular proliferation and tumor development. Pssm-ID: 380903 Cd Length: 45 Bit Score: 38.12 E-value: 8.44e-04
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| Bbox1_TIF1b_C-VI | cd19846 | B-box-type 1 zinc finger found in transcription intermediary factor 1-beta (TIF1-beta); ... |
178-219 | 1.23e-03 | |||||
B-box-type 1 zinc finger found in transcription intermediary factor 1-beta (TIF1-beta); TIF1-beta, also known as Kruppel-associated Box (KRAB)-associated protein 1 (KAP-1), KRAB-interacting protein 1 (KRIP-1), nuclear co-repressor KAP-1, RING finger protein 96, tripartite motif-containing protein 28 (TRIM28), or E3 SUMO-protein ligase TRIM28, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TIF1-beta/KAP-1 acts as a nuclear co-repressor that plays a role in transcription and in the DNA damage response. Upon DNA damage, the phosphorylation of KAP-1 on serine 824 by the ataxia telangiectasia-mutated (ATM) kinase enhances cell survival and facilitates chromatin relaxation and heterochromatic DNA repair. It also regulates CHD3 nucleosome remodeling during the DNA double-strand break (DSB) response. Meanwhile, KAP-1 can be dephosphorylated by protein phosphatase PP4C in the DNA damage response. Moreover, KAP-1 is a co-activator of the orphan nuclear receptor NGFI-B (or Nur77) and is involved in NGFI-B-dependent transcription. It is also a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase. The N-terminal RBCC domains of TIF1-beta are responsible for the interaction with KRAB zinc finger proteins (KRAB-ZFPs), MDM2, MM1, C/EBPbeta, and the regulation of homo- and heterodimerization. The C-terminal PHD/Bromo domains are involved in interacting with SETDB1, Mi-2alpha and other proteins to form complexes with histone deacetylase or methyltransferase activity. Pssm-ID: 380904 Cd Length: 52 Bit Score: 37.76 E-value: 1.23e-03
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| Bbox2_TRIM71_C-VII | cd19796 | B-box-type 2 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar ... |
327-357 | 1.60e-03 | |||||
B-box-type 2 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar proteins; TRIM71, also known as protein lineage variant 41 (lin-41), is an E3 ubiquitin-protein ligase that may play essential roles in embryonic stem cells, cellular reprogramming, and the timing of embryonic neurogenesis. It was first identified in the nematode Caenorhabditis elegans as a target of the differentiation-associated microRNA (miRNA) let-7 (lethal 7), and therefore part of a heterochronic gene network that controls larval development. In humans, it regulates let-7 microRNA biogenesis via modulation of Lin28B protein polyubiquitination. TRIM71 localizes to cytoplasmic P-bodies and directly interacts with the miRNA pathway proteins Argonaute 2 (AGO2) and DICER. It represses miRNA activity by promoting degradative ubiquitination of AGO2. Moreover, TRIM71 associates with SHCBP1, a novel component of the fibroblast growth factor (FGF) signaling pathway, and regulates its non-degradative polyubiquitination. It is also involved in the post-transcriptional regulation of the CDKN1A, RBL1 and RBL2 or EGR1 mRNAs through mediating RNA-binding in embryonic stem cells. TRIM71 belongs to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. Pssm-ID: 380854 [Multi-domain] Cd Length: 48 Bit Score: 37.29 E-value: 1.60e-03
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| NHL_like_1 | cd14953 | Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
771-804 | 1.79e-03 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 41.75 E-value: 1.79e-03
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| NHL_like_1 | cd14953 | Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
779-804 | 2.04e-03 | |||||
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 41.36 E-value: 2.04e-03
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| Bbox2_TRIM56_C-V | cd19789 | B-box-type 2 zinc finger found in tripartite motif-containing protein 56 (TRIM56) and similar ... |
327-361 | 2.62e-03 | |||||
B-box-type 2 zinc finger found in tripartite motif-containing protein 56 (TRIM56) and similar proteins; TRIM56, also known as RING finger protein 109 (RNF109), is a virus-inducible E3 ubiquitin ligase that restricts pestivirus infection. It positively regulates the Toll-like receptor 3 (TLR3) antiviral signaling pathway, and possesses antiviral activity against bovine viral diarrhea virus (BVDV), a ruminant pestivirus classified within the family Flaviviridae shared by tick-borne encephalitis virus (TBEV). It also possesses antiviral activity against two classical flaviviruses, yellow fever virus (YFV) and dengue virus (DENV), as well as a human coronavirus, HCoV-OC43, which is responsible for a significant share of common cold cases. It may not act on positive-strand RNA viruses indiscriminately. Moreover, TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses. TRIM56 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. Pssm-ID: 380847 Cd Length: 47 Bit Score: 36.75 E-value: 2.62e-03
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| Bbox2_TRIM46_C-I | cd19786 | B-box-type 2 zinc finger found in tripartite motif-containing protein 46 (TRIM46) and similar ... |
326-368 | 2.77e-03 | |||||
B-box-type 2 zinc finger found in tripartite motif-containing protein 46 (TRIM46) and similar proteins; TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that specifically localizes to the proximal axon, partly overlaps with the axon initial segment (AIS) at later stages, and organizes uniform microtubule orientation in axons. It controls neuronal polarity and axon specification by driving the formation of parallel microtubule arrays. TRIM46 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins, which are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. Pssm-ID: 380844 [Multi-domain] Cd Length: 46 Bit Score: 36.82 E-value: 2.77e-03
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| BBOX | smart00336 | B-Box-type zinc finger; |
176-222 | 2.87e-03 | |||||
B-Box-type zinc finger; Pssm-ID: 197662 [Multi-domain] Cd Length: 42 Bit Score: 36.55 E-value: 2.87e-03
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| NHL | pfam01436 | NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ... |
914-941 | 2.89e-03 | |||||
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is about 40 residues long and resembles the WD repeat pfam00400. The repeats have a catalytic activity in Swiss:P10731, proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Swiss:Q13049 interacts with the activation domain of Tat. This interaction is me diated by the NHL repeats. Pssm-ID: 396153 [Multi-domain] Cd Length: 28 Bit Score: 36.23 E-value: 2.89e-03
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| zf-B_box | pfam00643 | B-box zinc finger; |
176-222 | 3.09e-03 | |||||
B-box zinc finger; Pssm-ID: 459886 [Multi-domain] Cd Length: 42 Bit Score: 36.30 E-value: 3.09e-03
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| Bbox1_TIF1 | cd19805 | B-box-type 1 zinc finger found in transcription intermediary factor 1 (TIF1) family; This ... |
179-208 | 3.49e-03 | |||||
B-box-type 1 zinc finger found in transcription intermediary factor 1 (TIF1) family; This family corresponds to the TIF1 family of transcriptional cofactors including TIF1-alpha (TRIM24), TIF1-beta (TRIM28), and TIF1-gamma (TRIM33), which belongs to the C-VI subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1-alpha and TIF1-beta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. They bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. TIF1-gamma is structurally closely related to TIF1-alpha and TIF1-beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatinic proteins HP1alpha, beta and gamma. It cannot bind to nuclear receptors (NRs). Pssm-ID: 380863 Cd Length: 44 Bit Score: 36.20 E-value: 3.49e-03
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| Bbox2_TRIM14 | cd19768 | B-box-type 2 zinc finger found in tripartite motif-containing protein 14 (TRIM14) and similar ... |
328-354 | 4.25e-03 | |||||
B-box-type 2 zinc finger found in tripartite motif-containing protein 14 (TRIM14) and similar proteins; TRIM14 is a mitochondrial adaptor that facilitates innate immune signaling. It also plays a critical role in tumor development. TRIM14 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. It contains a Bbox2 zinc finger as well as a C-terminal SPRY/B30.2 domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. Pssm-ID: 380826 [Multi-domain] Cd Length: 44 Bit Score: 36.25 E-value: 4.25e-03
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| CPSF_A | pfam03178 | CPSF A subunit region; This family includes a region that lies towards the C-terminus of the ... |
963-1051 | 8.56e-03 | |||||
CPSF A subunit region; This family includes a region that lies towards the C-terminus of the cleavage and polyadenylation specificity factor (CPSF) A (160 kDa) subunit. CPSF is involved in mRNA polyadenylation and binds the AAUAAA conserved sequence in pre-mRNA. CPSF has also been found to be necessary for splicing of single-intron pre-mRNAs. The function of the aligned region is unknown but may be involved in RNA/DNA binding. Pssm-ID: 427182 Cd Length: 319 Bit Score: 39.50 E-value: 8.56e-03
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| NHL | pfam01436 | NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ... |
871-898 | 8.86e-03 | |||||
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is about 40 residues long and resembles the WD repeat pfam00400. The repeats have a catalytic activity in Swiss:P10731, proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Swiss:Q13049 interacts with the activation domain of Tat. This interaction is me diated by the NHL repeats. Pssm-ID: 396153 [Multi-domain] Cd Length: 28 Bit Score: 34.69 E-value: 8.86e-03
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