RING finger protein [Arabidopsis thaliana]
ubiquitin family protein( domain architecture ID 1000087)
ubiquitin family protein belongs to an diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes
List of domain hits
Name | Accession | Description | Interval | E-value | ||
Ubl1_cv_Nsp3_N-like super family | cl28922 | first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ... |
236-291 | 1.89e-22 | ||
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model. The actual alignment was detected with superfamily member cd17087: Pssm-ID: 475130 Cd Length: 104 Bit Score: 89.40 E-value: 1.89e-22
|
||||||
Name | Accession | Description | Interval | E-value | ||
RAWUL_DRIP_like | cd17087 | RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in DREB2A-interacting ... |
236-291 | 1.89e-22 | ||
RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in DREB2A-interacting protein (DRIP) and similar proteins; Dehydration-Responsive Element-Binding Protein 2A (DREB2A) regulates the expression of stress-inducible genes via the dehydration-responsive elements and requires posttranslational modification for its activation. DREB2A-Interacting Protein (DRIP) contains a RING finger, and a RING finger- and WD40-associated ubiquitin-like (RAWUL) domain. DRIP interacts with DREB2A and functions as a E3 ubiquitin ligases that negatively regulates DREB2A expression. Pssm-ID: 340607 Cd Length: 104 Bit Score: 89.40 E-value: 1.89e-22
|
||||||
Name | Accession | Description | Interval | E-value | ||
RAWUL_DRIP_like | cd17087 | RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in DREB2A-interacting ... |
236-291 | 1.89e-22 | ||
RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in DREB2A-interacting protein (DRIP) and similar proteins; Dehydration-Responsive Element-Binding Protein 2A (DREB2A) regulates the expression of stress-inducible genes via the dehydration-responsive elements and requires posttranslational modification for its activation. DREB2A-Interacting Protein (DRIP) contains a RING finger, and a RING finger- and WD40-associated ubiquitin-like (RAWUL) domain. DRIP interacts with DREB2A and functions as a E3 ubiquitin ligases that negatively regulates DREB2A expression. Pssm-ID: 340607 Cd Length: 104 Bit Score: 89.40 E-value: 1.89e-22
|
||||||
RAWUL_PCGF_like | cd16102 | RRING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in PCGF1-6, RING1 and -2, ... |
237-291 | 8.72e-05 | ||
RRING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in PCGF1-6, RING1 and -2, DRIP and similar proteins; structurally similar to a beta-grasp ubiquitin-like fold; The family includes six Polycomb Group (PcG) RING finger homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) that use epigenetic mechanisms to maintain or repress expression of their target genes. They were first discovered in fruit flies that can remodel chromatin such that epigenetic silencing of genes takes place, and are well known for silencing Hox genes through modulation of chromatin structure during embryonic development in fruit flies. PCGF homologs play important roles in cell proliferation, differentiation, and tumorigenesis. They all have been found to associate with ring finger protein 2 (RNF2). The RNF2-PCGF heterodimer is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF homologs are critical components in the assembly of distinct Polycomb Repression Complex 1 (PRC1) related complexes which are involved in the maintenance of gene repression and target different genes through distinct mechanisms. The Drosophila PRC1 core complex is formed by the Polycomb (Pc), Polyhomeotic (Ph), Posterior sex combs (Psc), and Sex combs extra (Sce, also known as Ring) subunits. In mammals, the composition of PRC1 is much more diverse and varies depending on the cellular context. All PRC1 complexes contain homologs of the Drosophila Ring protein. Ring1A/RNF1 and Ring1B/RNF2 are E3 ubiquitin ligases that mark lysine 119 of histone H2A with a single ubiquitin group (H2AK119ub). Mammalian homologs of the Drosophila Psc protein, such as PCGF2/Mel-18 or PCGF4/BMI1, regulate PRC1 enzymatic activity. PRC1 complexes can be divided into at least two classes according to the presence or absence of CBX proteins, which are homologs of Drosophila Pc. Canonical PRC1 complexes contain CBX proteins that recognize and bind H3K27me3, the mark deposited by PRC2. Therefore, canonical PRC1 complexes and PRC2 can act together to repress gene transcription and maintain this repression through cell division. Non-canonical PRC1 complexes, containing RYBP (together with additional proteins, such as L3mbtl2 or Kdm2b) rather than the CBX proteins, have recently been described in mammals. PCGF homologs contain a C3HC4-type RING-HC finger, and a RAWUL domain that might be responsible for interaction with Cbx members of the Polycomb repression complexes. Pssm-ID: 340519 Cd Length: 87 Bit Score: 40.34 E-value: 8.72e-05
|
||||||
RAWUL_PCGF6 | cd17085 | RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in polycomb group RING ... |
250-291 | 1.45e-03 | ||
RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in polycomb group RING finger protein 6 (PCGF6) and similar proteins; PCGF6, also termed Mel18 and Bmi1-like RING finger (MBLR), or RING finger protein 134 (RNF134), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5 and PCGF6/MBLR), and serves as the core component of a noncanonical Polycomb repressive complex 1 (PRC1)-like L3MBTL2 complex, which is composed of some canonical components, such as RNF2, CBX3, CXB4, CXB6, CXB7 and CXB8, as well as some noncanonical components, such as L3MBTL2, E2F6, WDR5, HDAC1 and RYBP, and plays critical roles in epigenetic transcriptional silencing in higher eukaryotes. Like other PCGF homologs, PCGF6 possesses the transcriptional repression activity, and also associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF6 can regulate the enzymatic activity of JARID1d/KDM5D, a trimethyl H3K4 demethylase, through the direct interaction with it. Furthermore, PCGF6 is expressed predominantly in meiotic and post-meiotic male germ cells and may play important roles in mammalian male germ cell development. It also regulates mesodermal lineage differentiation in mammalian embryonic stem cells (ESCs) and functions in induced pluripotent stem (iPS) reprogramming. The activity of PCGF6 is found to be regulated by cell cycle dependent phosphorylation. PCGF6 contains a C3HC4-type RING-HC finger, and a RAWUL domain. Pssm-ID: 340605 Cd Length: 89 Bit Score: 36.88 E-value: 1.45e-03
|
||||||
Blast search parameters | ||||
|