tripartite motif-containing protein 3 isoform X3 [Macaca mulatta]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| NHL_TRIM2_like | cd14960 | NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ... |
376-649 | 0e+00 | |||||
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: 583.92 E-value: 0e+00
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| BBC | smart00502 | B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
63-189 | 9.86e-38 | |||||
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains : Pssm-ID: 128778 Cd Length: 127 Bit Score: 136.24 E-value: 9.86e-38
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| IG_FLMN | smart00557 | Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ... |
227-324 | 4.13e-27 | |||||
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29). : Pssm-ID: 214720 [Multi-domain] Cd Length: 93 Bit Score: 105.38 E-value: 4.13e-27
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| Bbox_SF super family | cl00034 | B-box-type zinc finger superfamily; The B-box-type zinc finger is a short zinc binding domain ... |
26-58 | 1.01e-18 | |||||
B-box-type zinc finger superfamily; 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, B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). The actual alignment was detected with superfamily member cd19825: Pssm-ID: 469587 [Multi-domain] Cd Length: 47 Bit Score: 80.05 E-value: 1.01e-18
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| Name | Accession | Description | Interval | E-value | |||||
| NHL_TRIM2_like | cd14960 | NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ... |
376-649 | 0e+00 | |||||
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: 583.92 E-value: 0e+00
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| BBC | smart00502 | B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
63-189 | 9.86e-38 | |||||
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains Pssm-ID: 128778 Cd Length: 127 Bit Score: 136.24 E-value: 9.86e-38
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| CC_brat-like | cd20482 | coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ... |
63-183 | 2.56e-36 | |||||
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: 132.27 E-value: 2.56e-36
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| Vgb | COG4257 | Streptogramin lyase [Defense mechanisms]; |
389-640 | 5.16e-29 | |||||
Streptogramin lyase [Defense mechanisms]; Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 116.66 E-value: 5.16e-29
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| IG_FLMN | smart00557 | Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ... |
227-324 | 4.13e-27 | |||||
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29). Pssm-ID: 214720 [Multi-domain] Cd Length: 93 Bit Score: 105.38 E-value: 4.13e-27
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| Filamin | pfam00630 | Filamin/ABP280 repeat; |
227-320 | 7.67e-24 | |||||
Filamin/ABP280 repeat; Pssm-ID: 395505 Cd Length: 89 Bit Score: 95.82 E-value: 7.67e-24
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| Bbox2_TRIM3_C-VII | cd19825 | B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ... |
26-58 | 1.01e-18 | |||||
B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); 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 functions as a tumor suppressor that regulates asymmetric cell division in neuroblastoma. It binds to the ck inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclins D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It corresponds to gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of presynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendrite spine morphology. 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. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 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, 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: 380883 [Multi-domain] Cd Length: 47 Bit Score: 80.05 E-value: 1.01e-18
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| BBOX | smart00336 | B-Box-type zinc finger; |
26-56 | 1.53e-09 | |||||
B-Box-type zinc finger; Pssm-ID: 197662 [Multi-domain] Cd Length: 42 Bit Score: 53.50 E-value: 1.53e-09
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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 ... |
574-601 | 9.93e-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: 48.17 E-value: 9.93e-08
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| zf-B_box | pfam00643 | B-box zinc finger; |
25-56 | 5.16e-07 | |||||
B-box zinc finger; Pssm-ID: 459886 [Multi-domain] Cd Length: 42 Bit Score: 46.31 E-value: 5.16e-07
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| YhaN | COG4717 | Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
62-225 | 1.75e-06 | |||||
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.75e-06
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| PLN02919 | PLN02919 | haloacid dehalogenase-like hydrolase family protein |
402-648 | 2.18e-06 | |||||
haloacid dehalogenase-like hydrolase family protein Pssm-ID: 215497 [Multi-domain] Cd Length: 1057 Bit Score: 51.01 E-value: 2.18e-06
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| Myosin_tail_1 | pfam01576 | Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
58-217 | 1.32e-05 | |||||
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament. Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 1.32e-05
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| sbcc | TIGR00618 | exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
47-166 | 2.47e-04 | |||||
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.47e-04
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| PRK08268 | PRK08268 | 3-hydroxy-acyl-CoA dehydrogenase; Validated |
53-134 | 2.20e-03 | |||||
3-hydroxy-acyl-CoA dehydrogenase; Validated Pssm-ID: 236211 [Multi-domain] Cd Length: 507 Bit Score: 40.99 E-value: 2.20e-03
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| Name | Accession | Description | Interval | E-value | |||||
| NHL_TRIM2_like | cd14960 | NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ... |
376-649 | 0e+00 | |||||
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: 583.92 E-value: 0e+00
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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 ... |
385-645 | 1.89e-98 | |||||
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: 302.32 E-value: 1.89e-98
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| NHL_TRIM71_like | cd14954 | NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
377-641 | 2.24e-96 | |||||
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: 297.54 E-value: 2.24e-96
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| NHL_like_4 | cd14955 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
382-641 | 5.60e-82 | |||||
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: 259.82 E-value: 5.60e-82
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| NHL_like_2 | cd14957 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
379-640 | 1.15e-78 | |||||
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: 251.42 E-value: 1.15e-78
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| NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
382-640 | 1.92e-69 | |||||
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: 226.78 E-value: 1.92e-69
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| NHL_TRIM71_like | cd14954 | NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
417-640 | 1.90e-65 | |||||
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: 216.65 E-value: 1.90e-65
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| NHL_like_2 | cd14957 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
381-602 | 1.15e-64 | |||||
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: 214.44 E-value: 1.15e-64
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| NHL_TRIM32_like | cd14961 | NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ... |
382-646 | 6.83e-63 | |||||
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: 209.44 E-value: 6.83e-63
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| NHL_like_2 | cd14957 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
424-640 | 2.01e-61 | |||||
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: 205.96 E-value: 2.01e-61
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| NHL_like_4 | cd14955 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
428-640 | 4.03e-60 | |||||
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: 202.42 E-value: 4.03e-60
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| NHL_like_5 | cd14963 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
399-639 | 3.72e-59 | |||||
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: 199.44 E-value: 3.72e-59
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| NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
380-601 | 1.64e-55 | |||||
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: 189.80 E-value: 1.64e-55
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| NHL_brat_like | cd14959 | NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ... |
376-648 | 9.20e-55 | |||||
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: 187.86 E-value: 9.20e-55
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| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
386-648 | 1.55e-51 | |||||
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: 179.32 E-value: 1.55e-51
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| NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
428-640 | 9.15e-46 | |||||
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: 163.61 E-value: 9.15e-46
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| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
378-601 | 2.43e-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: 271332 [Multi-domain] Cd Length: 271 Bit Score: 148.50 E-value: 2.43e-40
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| NHL_PAL_like | cd14958 | Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ... |
435-639 | 2.37e-38 | |||||
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: 143.94 E-value: 2.37e-38
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| BBC | smart00502 | B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
63-189 | 9.86e-38 | |||||
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains Pssm-ID: 128778 Cd Length: 127 Bit Score: 136.24 E-value: 9.86e-38
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| NHL_like_1 | cd14953 | Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
391-640 | 2.28e-37 | |||||
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: 141.90 E-value: 2.28e-37
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| CC_brat-like | cd20482 | coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ... |
63-183 | 2.56e-36 | |||||
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: 132.27 E-value: 2.56e-36
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| NHL_like_4 | cd14955 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
517-641 | 5.92e-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: 136.55 E-value: 5.92e-36
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| NHL_like_1 | cd14953 | Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
437-641 | 3.82e-34 | |||||
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: 132.65 E-value: 3.82e-34
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| NHL_like_5 | cd14963 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
521-640 | 5.59e-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: 271333 [Multi-domain] Cd Length: 268 Bit Score: 119.32 E-value: 5.59e-30
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| Vgb | COG4257 | Streptogramin lyase [Defense mechanisms]; |
389-640 | 5.16e-29 | |||||
Streptogramin lyase [Defense mechanisms]; Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 116.66 E-value: 5.16e-29
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| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
377-498 | 1.26e-27 | |||||
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: 112.68 E-value: 1.26e-27
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| IG_FLMN | smart00557 | Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding ... |
227-324 | 4.13e-27 | |||||
Filamin-type immunoglobulin domains; These form a rod-like structure in the actin-binding cytoskeleton protein, filamin. The C-terminal repeats of filamin bind beta1-integrin (CD29). Pssm-ID: 214720 [Multi-domain] Cd Length: 93 Bit Score: 105.38 E-value: 4.13e-27
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| NHL_like_5 | cd14963 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
373-601 | 2.95e-26 | |||||
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: 108.53 E-value: 2.95e-26
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| NHL_like_1 | cd14953 | Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
395-598 | 5.49e-26 | |||||
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: 109.16 E-value: 5.49e-26
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| Vgb | COG4257 | Streptogramin lyase [Defense mechanisms]; |
435-640 | 2.00e-25 | |||||
Streptogramin lyase [Defense mechanisms]; Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 106.26 E-value: 2.00e-25
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| NHL_like_4 | cd14955 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
560-640 | 3.80e-24 | |||||
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: 102.65 E-value: 3.80e-24
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| NHL_PKND_like | cd14952 | NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ... |
391-640 | 4.50e-24 | |||||
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein with a cytosolic kinase domain and an extracellular sensor domain that contains NHL repeats. It plays a key role in the development of central nervous system tuberculosis, by mediating the invasion of host brain endothelia. 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: 271322 [Multi-domain] Cd Length: 247 Bit Score: 101.52 E-value: 4.50e-24
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| Filamin | pfam00630 | Filamin/ABP280 repeat; |
227-320 | 7.67e-24 | |||||
Filamin/ABP280 repeat; Pssm-ID: 395505 Cd Length: 89 Bit Score: 95.82 E-value: 7.67e-24
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| Vgb | COG4257 | Streptogramin lyase [Defense mechanisms]; |
387-610 | 3.95e-23 | |||||
Streptogramin lyase [Defense mechanisms]; Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 99.32 E-value: 3.95e-23
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| NHL_PAL_like | cd14958 | Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ... |
415-602 | 1.98e-22 | |||||
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: 98.10 E-value: 1.98e-22
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| NHL_TRIM71_like | cd14954 | NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
552-640 | 5.97e-21 | |||||
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: 93.38 E-value: 5.97e-21
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| NHL_like_1 | cd14953 | Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
517-641 | 1.36e-19 | |||||
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: 90.28 E-value: 1.36e-19
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| Bbox2_TRIM3_C-VII | cd19825 | B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ... |
26-58 | 1.01e-18 | |||||
B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); 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 functions as a tumor suppressor that regulates asymmetric cell division in neuroblastoma. It binds to the ck inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclins D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It corresponds to gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of presynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendrite spine morphology. 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. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 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, 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: 380883 [Multi-domain] Cd Length: 47 Bit Score: 80.05 E-value: 1.01e-18
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| NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
563-645 | 4.24e-18 | |||||
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: 84.64 E-value: 4.24e-18
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| NHL_like_2 | cd14957 | Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
376-466 | 4.51e-18 | |||||
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: 85.01 E-value: 4.51e-18
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| NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
377-465 | 5.56e-18 | |||||
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: 84.64 E-value: 5.56e-18
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| Bbox2_TRIM2-like | cd19759 | B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM2, TRIM3, and ... |
26-58 | 1.13e-16 | |||||
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: 74.02 E-value: 1.13e-16
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| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
382-467 | 3.78e-14 | |||||
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: 73.00 E-value: 3.78e-14
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| YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
442-641 | 1.08e-12 | |||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 68.18 E-value: 1.08e-12
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| Bbox2_TRIM2_C-VII | cd19824 | B-box-type 2 zinc finger found in tripartite motif-containing protein 2 (TRIM2) and similar ... |
28-58 | 1.41e-12 | |||||
B-box-type 2 zinc finger found in tripartite motif-containing protein 2 (TRIM2) 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. TRIM2 also plays a role in mediating the p42/p44 Semi-independent ubiquitination of the cell death-promoting protein Bcl-2-interacting mediator of cell death (Aim) in rapid ischemic tolerance. TRIM2 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, 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: 380882 [Multi-domain] Cd Length: 42 Bit Score: 62.38 E-value: 1.41e-12
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| NHL_like_1 | cd14953 | Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
564-641 | 2.88e-12 | |||||
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: 68.33 E-value: 2.88e-12
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| YncE | COG3391 | DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
377-602 | 4.19e-12 | |||||
DNA-binding beta-propeller fold protein YncE [General function prediction only]; Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 66.26 E-value: 4.19e-12
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| YvrE | COG3386 | Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
440-608 | 1.25e-11 | |||||
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 65.30 E-value: 1.25e-11
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| BBOX | smart00336 | B-Box-type zinc finger; |
26-56 | 1.53e-09 | |||||
B-Box-type zinc finger; Pssm-ID: 197662 [Multi-domain] Cd Length: 42 Bit Score: 53.50 E-value: 1.53e-09
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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 ... |
574-601 | 9.93e-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: 48.17 E-value: 9.93e-08
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| YvrE | COG3386 | Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
474-647 | 2.76e-07 | |||||
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 52.20 E-value: 2.76e-07
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| zf-B_box | pfam00643 | B-box zinc finger; |
25-56 | 5.16e-07 | |||||
B-box zinc finger; Pssm-ID: 459886 [Multi-domain] Cd Length: 42 Bit Score: 46.31 E-value: 5.16e-07
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| NHL-2_like | cd14951 | NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ... |
429-640 | 5.40e-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: 52.19 E-value: 5.40e-07
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| YhaN | COG4717 | Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
62-225 | 1.75e-06 | |||||
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.75e-06
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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 ... |
28-64 | 1.83e-06 | |||||
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: 44.99 E-value: 1.83e-06
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| PLN02919 | PLN02919 | haloacid dehalogenase-like hydrolase family protein |
402-648 | 2.18e-06 | |||||
haloacid dehalogenase-like hydrolase family protein Pssm-ID: 215497 [Multi-domain] Cd Length: 1057 Bit Score: 51.01 E-value: 2.18e-06
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| YvrE | COG3386 | Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
434-641 | 2.23e-06 | |||||
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 49.51 E-value: 2.23e-06
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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 ... |
527-554 | 2.77e-06 | |||||
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: 43.93 E-value: 2.77e-06
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| NHL-2_like | cd14951 | NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ... |
483-602 | 3.27e-06 | |||||
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: 49.50 E-value: 3.27e-06
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| Vgb | COG4257 | Streptogramin lyase [Defense mechanisms]; |
574-641 | 5.38e-06 | |||||
Streptogramin lyase [Defense mechanisms]; Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 48.48 E-value: 5.38e-06
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| DUF5128 | pfam17170 | 6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ... |
538-647 | 6.05e-06 | |||||
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown function. There is a highly conserved FDxxG motif which might be important. Pssm-ID: 407298 [Multi-domain] Cd Length: 321 Bit Score: 48.86 E-value: 6.05e-06
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| DUF5128 | pfam17170 | 6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ... |
403-562 | 6.55e-06 | |||||
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown function. There is a highly conserved FDxxG motif which might be important. Pssm-ID: 407298 [Multi-domain] Cd Length: 321 Bit Score: 48.48 E-value: 6.55e-06
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| Myosin_tail_1 | pfam01576 | Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
58-217 | 1.32e-05 | |||||
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament. Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 1.32e-05
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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 ... |
26-56 | 1.88e-05 | |||||
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: 42.01 E-value: 1.88e-05
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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 ... |
438-465 | 3.27e-05 | |||||
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: 40.85 E-value: 3.27e-05
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| Bbox2_TRIM16-like | cd19769 | B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, ... |
26-64 | 5.84e-05 | |||||
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: 40.77 E-value: 5.84e-05
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| COG4913 | COG4913 | Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
57-212 | 6.13e-05 | |||||
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 6.13e-05
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| YjiK | COG3204 | Uncharacterized Ca-binding beta-propeller protein YjiK [General function prediction only]; |
435-630 | 6.48e-05 | |||||
Uncharacterized Ca-binding beta-propeller protein YjiK [General function prediction only]; Pssm-ID: 442437 [Multi-domain] Cd Length: 271 Bit Score: 44.96 E-value: 6.48e-05
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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 ... |
391-418 | 7.17e-05 | |||||
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: 40.08 E-value: 7.17e-05
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| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
429-635 | 8.48e-05 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 45.29 E-value: 8.48e-05
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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 ... |
618-645 | 1.10e-04 | |||||
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: 39.69 E-value: 1.10e-04
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| NHL_TRIM71_like | cd14954 | NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
374-418 | 1.24e-04 | |||||
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: 44.46 E-value: 1.24e-04
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| sbcc | TIGR00618 | exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
47-166 | 2.47e-04 | |||||
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.47e-04
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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 ... |
30-59 | 2.56e-04 | |||||
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: 38.94 E-value: 2.56e-04
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| PLN02919 | PLN02919 | haloacid dehalogenase-like hydrolase family protein |
516-640 | 5.41e-04 | |||||
haloacid dehalogenase-like hydrolase family protein Pssm-ID: 215497 [Multi-domain] Cd Length: 1057 Bit Score: 43.30 E-value: 5.41e-04
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| COG4913 | COG4913 | Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
46-228 | 5.68e-04 | |||||
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.68e-04
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| COG4913 | COG4913 | Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
55-219 | 6.29e-04 | |||||
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 6.29e-04
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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 ... |
480-507 | 1.36e-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: 36.61 E-value: 1.36e-03
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
60-241 | 1.57e-03 | |||||
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.57e-03
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| Bbox2_TIF1g_C-VI | cd19830 | B-box-type 2 zinc finger found in transcription intermediary factor 1 gamma (TIF1-gamma); ... |
21-64 | 1.63e-03 | |||||
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: 36.96 E-value: 1.63e-03
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| PLN02919 | PLN02919 | haloacid dehalogenase-like hydrolase family protein |
364-459 | 1.93e-03 | |||||
haloacid dehalogenase-like hydrolase family protein Pssm-ID: 215497 [Multi-domain] Cd Length: 1057 Bit Score: 41.38 E-value: 1.93e-03
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| COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
60-212 | 1.96e-03 | |||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.96e-03
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| SGL | pfam08450 | SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ... |
576-605 | 1.96e-03 | |||||
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30), gluconolactonase and luciferin-regenerating enzyme (LRE). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 and LRE. Pssm-ID: 462480 [Multi-domain] Cd Length: 246 Bit Score: 40.32 E-value: 1.96e-03
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| PRK08268 | PRK08268 | 3-hydroxy-acyl-CoA dehydrogenase; Validated |
53-134 | 2.20e-03 | |||||
3-hydroxy-acyl-CoA dehydrogenase; Validated Pssm-ID: 236211 [Multi-domain] Cd Length: 507 Bit Score: 40.99 E-value: 2.20e-03
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| NHL_like_6 | cd14962 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
345-418 | 2.74e-03 | |||||
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: 40.26 E-value: 2.74e-03
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| NHL-2_like | cd14951 | NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ... |
396-498 | 2.77e-03 | |||||
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: 40.25 E-value: 2.77e-03
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| COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
56-325 | 2.97e-03 | |||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 2.97e-03
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| PLN02919 | PLN02919 | haloacid dehalogenase-like hydrolase family protein |
516-602 | 4.60e-03 | |||||
haloacid dehalogenase-like hydrolase family protein Pssm-ID: 215497 [Multi-domain] Cd Length: 1057 Bit Score: 40.22 E-value: 4.60e-03
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| PRK10246 | PRK10246 | exonuclease subunit SbcC; Provisional |
57-202 | 5.14e-03 | |||||
exonuclease subunit SbcC; Provisional Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.17 E-value: 5.14e-03
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| Smc | COG1196 | Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
57-307 | 5.84e-03 | |||||
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 5.84e-03
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| Bbox2_TIF1_C-VI | cd19775 | B-box-type 2 zinc finger found in transcription intermediary factor 1 (TIF1) family; This ... |
28-52 | 6.12e-03 | |||||
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: 35.00 E-value: 6.12e-03
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| DUF5128 | pfam17170 | 6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown ... |
446-610 | 6.21e-03 | |||||
6-bladed beta-propeller; This family is a 6-bladed beta-propeller structure of unknown function. There is a highly conserved FDxxG motif which might be important. Pssm-ID: 407298 [Multi-domain] Cd Length: 321 Bit Score: 39.23 E-value: 6.21e-03
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| Bbox2_TIF1a_C-VI | cd19828 | B-box-type 2 zinc finger found in transcription intermediary factor 1-alpha (TIF1-alpha); ... |
21-67 | 7.76e-03 | |||||
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: 35.02 E-value: 7.76e-03
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