conserved hypothetical protein [Leishmania braziliensis MHOM/BR/75/M2904]
Protein Classification
RING-Ubox_PRP19 and Prp19 domain-containing protein( domain architecture ID 11616145)
protein containing domains RING-Ubox_PRP19, Prp19, and WD40
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Prp19 | pfam08606 | Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ... |
72-131 | 6.41e-26 | |||||
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region represented by this family covers the sequence implicated in self-interaction and a coiled-coiled motif. PRP19-like proteins form an oligomer that is necessary for spliceosome assembly. : Pssm-ID: 400774 Cd Length: 65 Bit Score: 100.28 E-value: 6.41e-26
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| RING-Ubox_PRP19 | cd16656 | U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ... |
2-53 | 4.33e-22 | |||||
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins; Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment. : Pssm-ID: 438318 Cd Length: 54 Bit Score: 89.16 E-value: 4.33e-22
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| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
227-515 | 1.34e-15 | |||||
WD40 repeat [General function prediction only]; : Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 78.80 E-value: 1.34e-15
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| Name | Accession | Description | Interval | E-value | |||||
| Prp19 | pfam08606 | Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ... |
72-131 | 6.41e-26 | |||||
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region represented by this family covers the sequence implicated in self-interaction and a coiled-coiled motif. PRP19-like proteins form an oligomer that is necessary for spliceosome assembly. Pssm-ID: 400774 Cd Length: 65 Bit Score: 100.28 E-value: 6.41e-26
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| RING-Ubox_PRP19 | cd16656 | U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ... |
2-53 | 4.33e-22 | |||||
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins; Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment. Pssm-ID: 438318 Cd Length: 54 Bit Score: 89.16 E-value: 4.33e-22
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| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
227-515 | 1.34e-15 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 78.80 E-value: 1.34e-15
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
247-510 | 1.77e-14 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 73.91 E-value: 1.77e-14
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| Ubox | smart00504 | Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ... |
1-52 | 7.46e-12 | |||||
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination. Pssm-ID: 128780 [Multi-domain] Cd Length: 63 Bit Score: 60.33 E-value: 7.46e-12
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| Name | Accession | Description | Interval | E-value | |||||
| Prp19 | pfam08606 | Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ... |
72-131 | 6.41e-26 | |||||
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region represented by this family covers the sequence implicated in self-interaction and a coiled-coiled motif. PRP19-like proteins form an oligomer that is necessary for spliceosome assembly. Pssm-ID: 400774 Cd Length: 65 Bit Score: 100.28 E-value: 6.41e-26
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| RING-Ubox_PRP19 | cd16656 | U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ... |
2-53 | 4.33e-22 | |||||
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins; Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment. Pssm-ID: 438318 Cd Length: 54 Bit Score: 89.16 E-value: 4.33e-22
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| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
227-515 | 1.34e-15 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 78.80 E-value: 1.34e-15
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| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
232-515 | 7.83e-15 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 76.49 E-value: 7.83e-15
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| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
232-512 | 1.43e-14 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 75.33 E-value: 1.43e-14
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
247-510 | 1.77e-14 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 73.91 E-value: 1.77e-14
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| Ubox | smart00504 | Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ... |
1-52 | 7.46e-12 | |||||
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination. Pssm-ID: 128780 [Multi-domain] Cd Length: 63 Bit Score: 60.33 E-value: 7.46e-12
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| RING-Ubox_PUB | cd16664 | U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ... |
1-51 | 7.46e-08 | |||||
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain. Pssm-ID: 438326 [Multi-domain] Cd Length: 53 Bit Score: 48.71 E-value: 7.46e-08
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| RING-Ubox | cd16453 | U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ... |
2-46 | 3.24e-07 | |||||
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. Pssm-ID: 438117 [Multi-domain] Cd Length: 44 Bit Score: 46.78 E-value: 3.24e-07
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| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
252-515 | 4.00e-07 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 51.57 E-value: 4.00e-07
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| mRING_PEX12 | cd16451 | Modified RING finger found in peroxin-12 (PEX12) and similar proteins; PEX12, also known as ... |
3-52 | 5.16e-06 | |||||
Modified RING finger found in peroxin-12 (PEX12) and similar proteins; PEX12, also known as peroxisome assembly protein 12 or peroxisome assembly factor 3 (PAF-3), is a RING finger domain-containing integral membrane peroxin required for protein import into peroxisomes. Mutations in human PEX12 result in the peroxisome deficiency Zellweger syndrome of complementation group III (CG-III), a lethal neurological disorder. PEX12 also functions as an E3-ubiquitin ligase that facilitates the PEX4-dependent monoubiquitination of PEX5, a key player in peroxisomal matrix protein import, to control PEX5 receptor recycling or degradation. PEX12 contains a modified RING finger that lacks the third, fourth, and eighth zinc-binding residues of the consensus RING finger motif, suggesting PEX12 may only bind one zinc ion. Pssm-ID: 438115 [Multi-domain] Cd Length: 54 Bit Score: 43.77 E-value: 5.16e-06
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| RING-Ubox_PPIL2 | cd16663 | U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 ... |
4-55 | 7.48e-06 | |||||
U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2) and similar proteins; PPIL2 (EC 5.2.1.8), also known as PPIase, CYC4, cyclophilin-60 (Cyp60), cyclophilin-like protein Cyp-60, or Rotamase PPIL2, is a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c and regulates gene expression. PPIL2 belongs to the cyclophilin family of peptidylprolyl isomerases and catalyzes cis-trans isomerization of proline-peptide bonds, which is often a rate-limiting step in protein folding. It positively regulates beta-site amyloid precursor protein cleaving enzyme (BACE1) expression and beta-secretase activity. Moreover, PPIL2 plays an important role in the translocation of CD147 to the cell surface, and thus may present a novel target for therapeutic interventions in diseases where CD147 functions as a pathogenic factor in cancer, human immunodeficiency virus infection, or rheumatoid arthritis. PPIL2 contains an N-terminal RING-like U-box domain and a C-terminal cyclophilin (Cyp)-like chaperone domain. Pssm-ID: 438325 Cd Length: 73 Bit Score: 43.71 E-value: 7.48e-06
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| RING-Ubox_WDSUB1-like | cd16655 | U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ... |
2-52 | 3.31e-05 | |||||
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis. Pssm-ID: 438317 [Multi-domain] Cd Length: 55 Bit Score: 41.33 E-value: 3.31e-05
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| RING-Ubox2_NOSIP | cd16662 | U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein ... |
4-52 | 1.04e-04 | |||||
U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein (NOSIP) and similar proteins; NOSIP, also known as endothelial NO synthase (eNOS)-interacting protein, p33RUL, is an E3 ubiquitin-protein ligase implicated in the control of airway and vascular diameter, mucosal secretion, NO synthesis in ciliated epithelium, and, therefore, of mucociliary and bronchial function. The loss of NOSIP may cause holoprosencephaly and facial anomalies including cleft lip/palate, cyclopia and facial midline clefting. NOSIP interacts with neuronal nitric oxide synthase (nNOS) and eNOS by inhibiting nitric oxide (NO) production. It acts as a novel type of modulator that promotes translocation of eNOS from the plasma membrane to intracellular sites, thereby uncoupling eNOS from plasma membrane caveolae and inhibiting NO synthesis. NOSIP also interacts with protein phosphatase PP2A and mediates the monoubiquitination of the PP2A catalytic subunit. Thus, it is a critical modulator of brain and craniofacial development in mice and a candidate gene for holoprosencephaly in humans. Moreover, NOSIP associates with the erythropoietin (Epo) receptor (EpoR), mediates ubiquitination of EpoR, and plays an essential role in erythropoietin-induced proliferation. NOSIP contains an atypical N-terminal RING-like U-box domain that is split into two parts by an interjacent stretch of 104 amino acid residues, as well as a C-terminal RING-like U-box domain. This model corresponds to the second U-box domain. Pssm-ID: 438324 Cd Length: 68 Bit Score: 40.36 E-value: 1.04e-04
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| Blast search parameters | ||||
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